Autophagy in neurons

Stavoe, Andrea K.H.; Holzbaur, Erika L.F.

doi:10.1146/annurev-cellbio-100818-125242

Cited by 328Autophagy in Disease and TherapyUbiquitin and proteasome pathwaysGenetics, Aging, and Longevity in Model Organisms

Autophagy in neurons

Open access

Stavoe, Andrea K.H., Holzbaur, Erika L.F.·2019·Annual Review of Cell and Developmental Biology

DOI 10.1146/annurev-cellbio-100818-125242PMC PMC6996145

Open this paper in CoChat — free account

Abstract

Autophagy is the major cellular pathway to degrade dysfunctional organelles and protein aggregates. Autophagy is particularly important in neurons, which are terminally differentiated cells that must last the lifetime of the organism. There are both constitutive and stress-induced pathways for autophagy in neurons, which catalyze the turnover of aged or damaged mitochondria, endoplasmic reticulum, other cellular organelles, and aggregated proteins. These pathways are required in neurodevelopment as well as in the maintenance of neuronal homeostasis. Here we review the core components of the pathway for autophagosome biogenesis, as well as the cell biology of bulk and selective autophagy in neurons. Finally, we discuss the role of autophagy in neuronal development, homeostasis, and aging and the links between deficits in autophagy and neurodegeneration.

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Integrity signals

Registry

Crossref · 10.1146/annurev-cellbio-100818-125242

Cites

155 of 155 references verified0 citation errors · 0 not checkable

Statistics

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Reducing tau acetylation restores its degradation through CMA.
“Reducing tau acetylation restores its degradation through CMA (Figure 5).90,147”
From The lysosome and proteostatic stress at the intersection of pediatric neurological disorders and adult neurodegenerative diseases (2025) · cites this paper as [147]
The Introduction (page not available) mentions chaperone-mediated autophagy as a neuronal protein-degradation pathway, but does not discuss tau. Searches for tau, acetylation, and CMA found no passage stating that reducing tau acetylation restores its degradation through CMA. (LLM, conf=0.76)
Experimental — accuracy not yet measured
Tau acetylation impairs tau clearance through CMA by reducing entry into the lysosome and proteolysis by the lysosome.
“Tau acetylation contributes to tau pathology via multiple potential mechanisms: promoting tau fibrillation146 and impairing tau clearance through CMA both by reducing entry into the lysosome and proteolysis by the lysosome.147”
From The lysosome and proteostatic stress at the intersection of pediatric neurological disorders and adult neurodegenerative diseases (2025) · cites this paper as [147]
The Introduction describes chaperone-mediated autophagy as a neuronal protein-degradation pathway, and “Autophagy in Disease” says defects in that pathway may contribute to neurodegeneration. Neither passage addresses tau acetylation, tau entry into lysosomes, or its lysosomal proteolysis; searches for those terms found no supporting passage in our copy. Page numbers were not available. (LLM, conf=0.75)
Experimental — accuracy not yet measured

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

1 retracted

RETRACTED ARTICLE: Parkin and PINK1 mitigate STING-induced inflammation
Sliter, D. A., Martinez, J., Hao, L., Chen, X., Sun, N., Fischer, T. D., Burman, J. L., Li, Y., Zhang, Z., Narendra, D. P., et al. (2018) · Nature · doi:10.1038/s41586-018-0448-9 · Cited by 1,287 · cited 1× · see citing works
“The importance of more fully understanding mitochondrial quality control is emphasized by the observation that both PINK1 and Parkin knockout mice are susceptible to stress, and that this in turn leads to inflammation (Sliter et al. 2018).”
Background
Retracted
p62/SQSTM1 Binds Directly to Atg8/LC3 to Facilitate Degradation of Ubiquitinated Protein Aggregates by Autophagy
Pankiv, S., Clausen, T. H., Lamark, T., Brech, A., Bruun, J.-A., Outzen, H., Øvervatn, A., Bjørkøy, G., & Johansen, T. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m702824200 · Cited by 4,578 · cited 1× · see citing works
“The best characterized autophagy receptor known to function in aggrephagy is p62/ SQSTM1 (Bjørkøy et al. 2005, Komatsu et al. 2007a, Pankiv et al. 2007).”
Background
Parkin is recruited selectively to impaired mitochondria and promotes their autophagy
Narendra, D., Tanaka, A., Suen, D.-F., & Youle, R. J. (2008) · The Journal of Cell Biology · doi:10.1083/jcb.200809125 · Cited by 4,026 · cited 1× · see citing works
“Work has shown that PINK1 is a mitochondrially-targeted kinase involved in the recruitment of the E3 ubiquitin ligase Parkin to impaired mitochondria (Narendra et al. 2008, 2010a).”
Background
Suppression of basal autophagy in neural cells causes neurodegenerative disease in mice
Hara, T., Nakamura, K., Matsui, M., Yamamoto, A., Nakahara, Y., Suzuki-Migishima, R., Yokoyama, M., Mishima, K., Saito, I., Okano, H., et al. (2006) · Nature · doi:10.1038/nature04724 · Cited by 3,882 · cited 2× · see citing works
“While many questions remain, the importance of autophagy in neurons is clear, as the neuron-specific ablation of autophagy leads to neurodegeneration (Hara et al. 2006, Komatsu et al. 2006).”
Background
Loss of autophagy in the central nervous system causes neurodegeneration in mice
Komatsu, M., Waguri, S., Chiba, T., Murata, S., Iwata, J.-I., Tanida, I., Ueno, T., Koike, M., Uchiyama, Y., Kominami, E., et al. (2006) · Nature · doi:10.1038/nature04723 · Cited by 3,500 · cited 3× · see citing works
“While many questions remain, the importance of autophagy in neurons is clear, as the neuron-specific ablation of autophagy leads to neurodegeneration (Hara et al. 2006, Komatsu et al. 2006).”
Background
p62/SQSTM1 forms protein aggregates degraded by autophagy and has a protective effect on huntingtin-induced cell death
Bjørkøy, G., Lamark, T., Brech, A., Outzen, H., Perander, M., Øvervatn, A., Stenmark, H., & Johansen, T. (2005) · The Journal of Cell Biology · doi:10.1083/jcb.200507002 · Cited by 3,276 · cited 10× · see citing works
“21(12):1995–2003 [PubMed: 21885617] Haack TBB, Iuso A, Kremer LSS, Hartig M, Strom TMM, et al. 2016 Absence of the Autophagy Adaptor SQSTM1/p62 Causes Childhood-Onset Neurodegeneration with Ataxia, Dystonia, and Gaze Palsy.”
BackgroundInfluential
PINK1 Is Selectively Stabilized on Impaired Mitochondria to Activate Parkin
Narendra, D. P., Jin, S. M., Tanaka, A., Suen, D.-F., Gautier, C. A., Shen, J., Cookson, M. R., & Youle, R. J. (2010) · PLoS Biology · doi:10.1371/journal.pbio.1000298 · Cited by 2,944 · see citing works
The ubiquitin kinase PINK1 recruits autophagy receptors to induce mitophagy
Lazarou, M., Sliter, D. A., Kane, L. A., Sarraf, S. A., Wang, C., Burman, J. L., Sideris, D. P., Fogel, A. I., & Youle, R. J. (2015) · Nature · doi:10.1038/nature14893 · Cited by 2,774 · cited 3× · see citing works
“Depletion of a single receptor such as OPTN may induce a delay in mitochondrial engulfment (Moore & Holzbaur 2016) but does not block mitophagy completely (Lazarou et al. 2015), indicating some redundancy in the system.”
Background
In vivo analysis of autophagy in response to nutrient starvation using transgenic mice expressing a fluorescent autophagosome marker.
Mizushima, N., Yamamoto, A., Matsui, M., Yoshimori, T., & Ohsumi, Y. (2003) · Molecular Biology of the Cell · doi:10.1091/mbc.e03-09-0704 · Cited by 2,436 · cited 8× · see citing works
“Upon stimulation with low-dose NMDA, dendritic spines displayed an increase in GFP-LC3 puncta.”
BackgroundInfluential
Homeostatic levels of p62 control cytoplasmic inclusion body formation in autophagy-deficient mice.
Komatsu, M., Waguri, S., Koike, M., Sou, Y.-S., Ueno, T., Hara, T., Mizushima, N., Iwata, J.-I., Ezaki, J., Murata, S., et al. (2007) · Cell · doi:10.1016/j.cell.2007.10.035 · Cited by 2,124 · cited 3× · see citing works
“Likewise, conditionally knocking out Atg7 in Purkinje cells using the Pcp2 promoter in mice did not appear to affect dendrites, but did lead to neuronal and axonal dystrophy, degeneration of axon terminals, and eventual neuronal death (Komatsu et al. 2007b).”
Background
A ubiquitin-like system mediates protein lipidation
Ichimura, Y., Kirisako, T., Takao, T., Satomi, Y., Shimonishi, Y., Ishihara, N., Mizushima, N., Tanida, I., Kominami, E., Ohsumi, M., et al. (2000) · Nature · doi:10.1038/35044114 · Cited by 2,098 · cited 1× · see citing works
“Elongation of the autophagosome membrane is mediated by the aptly named elongation complex, composed of two ubiquitin-like conjugation complexes (Ichimura et al. 2000, Mizushima et al. 1998).”
Background
The machinery of macroautophagy
Feng, Y., He, D., Yao, Z., & Klionsky, D. J. (2014) · Cell Research · doi:10.1038/cr.2013.168 · Cited by 2,083 · cited 7× · see citing works
“ATG9 is thought to shuttle between the membrane source and the growing autophagosome, possibly bringing lipids to the autophagosome.”
BackgroundInfluential
A protein conjugation system essential for autophagy
Mizushima, N., Noda, T., Yoshimori, T., Tanaka, Y., Ishii, T., George, M. D., Klionsky, D., Ohsumi, M., & Ohsumi, Y. (1998) · Nature · doi:10.1038/26506 · Cited by 1,731 · cited 1× · see citing works
“Elongation of the autophagosome membrane is mediated by the aptly named elongation complex, composed of two ubiquitin-like conjugation complexes (Ichimura et al. 2000, Mizushima et al. 1998).”
Background
Extensive Involvement of Autophagy in Alzheimer Disease: An Immuno-Electron Microscopy Study
Nixon, R. A., Wegiel, J., Kumar, A., Yu, W. H., Peterhoff, C., Cataldo, A., & Cuervo, A. M. (2005) · Journal of Neuropathology & Experimental Neurology · doi:10.1093/jnen/64.2.113 · Cited by 1,588 · cited 1× · see citing works
“…al. 2018, Rui et al. 2015, Stavoe & Holzbaur 2018), cargo-loading (Martinez-Vicente et al. 2010, Rudnick et al. 2017), intracellular transport (Nicolas et al. 2018, Wong & Holzbaur 2014b), and autophagosomelysosome fusion or acidification (Lie & Nixon 2018, Nixon et al. 2005) across disease models.”
Background
ULK1 induces autophagy by phosphorylating Beclin-1 and activating Vps34 lipid kinase
Russell, R. C., Tian, Y., Yuan, H.-X., Park, H., Chang, Y.-Y., Kim, J., Kim, H., Neufeld, T. P., Dillin, A., & Guan, K. (2013) · Nature Cell Biology · doi:10.1038/ncb2757 · Cited by 1,543 · cited 1× · see citing works
“When activated, ULK1 phosphorylates other autophagy pathway components, including Beclin1 (BECN1) and ATG9 (Feng et al. 2014, Kamada et al. 2000, Russell et al. 2013, Zhou et al. 2017).”
Background
Mitochondria Supply Membranes for Autophagosome Biogenesis during Starvation
Hailey, D. W., Rambold, A. S., Satpute‐Krishnan, P., Mitra, K., Sougrat, R., Kim, P. K., & Lippincott‐Schwartz, J. (2010) · Cell · doi:10.1016/j.cell.2010.04.009 · Cited by 1,491 · cited 2× · see citing works
“Virtually every possible membrane source, including plasma membrane (Hollenbeck 1993; Ravikumar 2010), mitochondria (Hailey et al. 2010), Golgi (van der Vaart et al.”
Background
Dissection of Autophagosome Formation Using Apg5-Deficient Mouse Embryonic Stem Cells
Mizushima, N., Yamamoto, A., Hatano, M., Kobayashi, Y., Kabeya, Y., Suzuki, K., Tokuhisa, T., Ohsumi, Y., & Yoshimori, T. (2001) · The Journal of Cell Biology · doi:10.1083/jcb.152.4.657 · Cited by 1,361 · cited 1× · see citing works
“The ATG12-ATG5 conjugate, along with ATG16L1, acts as the E3-like enzyme to conjugate mATG8s to phosphatidylethanolamine (PE) (Mizushima et al. 2001, Suzuki et al. 2001).”
Background
PINK1 phosphorylates ubiquitin to activate Parkin E3 ubiquitin ligase activity
Kane, L. A., Lazarou, M., Fogel, A. I., Li, Y., Yamano, K., Sarraf, S. A., Banerjee, S., & Youle, R. J. (2014) · Journal of Cell Biology · doi:10.1083/jcb.201402104 · Cited by 1,298 · cited 1× · see citing works
“PINK1 also phosphorylates ubiquitin, which further enhances Parkin activity (Kane et al. 2014).”
Background
Mutations of optineurin in amyotrophic lateral sclerosis
Maruyama, H., Morino, H., Ito, H., Izumi, Y., Kato, H., Watanabe, Y., Kinoshita, Y., Kamada, M., Nodera, H., Suzuki, H., et al. (2010) · Nature · doi:10.1038/nature08971 · Cited by 1,265 · cited 1× · see citing works
“…that OPTN and TBK1 are involved in mitophagy downstream from PINK1 and Parkin, is particularly interesting because mutations in both OPTN and TBK1 are causative for rare forms of familial amyotrophic lateral sclerosis (ALS) (Cirulli et al. 2015, Freischmidt et al. 2015, Maruyama et al. 2010).”
Background
Two Beclin 1-binding proteins, Atg14L and Rubicon, reciprocally regulate autophagy at different stages
Matsunaga, K., Saitoh, T., Tabata, K., Omori, H., Satoh, T., Kurotori, N., Maejima, I., Shirahama-Noda, K., Ichimura, T., Isobe, T., et al. (2009) · Nature Cell Biology · doi:10.1038/ncb1846 · Cited by 1,235 · cited 2× · see citing works
“Beclin1 is a component of the nucleation complex, along with ATG14, lipid kinase VPS34/PI3KIII, and VPS15/PIK3R4 (Itakura et al. 2008, Matsunaga et al. 2009, Sun et al. 2008, Zhong et al. 2009).”
Background
The autophagy-related protein beclin 1 shows reduced expression in early Alzheimer disease and regulates amyloid beta accumulation in mice.
Pickford, F., Masliah, E., Britschgi, M., Lucin, K. M., Narasimhan, R., Jaeger, P. A., Small, S., Spencer, B., Rockenstein, E., Levine, B., et al. (2008) · Journal of Clinical Investigation · doi:10.1172/jci33585 · Cited by 1,186 · cited 1× · see citing works
“In transgenic mice overexpressing amyloid precursor protein (APP) and heterozygous for a Beclin1 deletion, synapses and dendrites degenerated in neocortex and hippocampus and layer II neurons of the entorhinal cortex were lost (Pickford et al. 2008).”
Background
Beclin 1 Forms Two Distinct Phosphatidylinositol 3-Kinase Complexes with Mammalian Atg14 and UVRAG
Itakura, E., Kishi, C., Inoue, K., & Mizushima, N. (2008) · Molecular Biology of the Cell · doi:10.1091/mbc.e08-01-0080 · Cited by 1,176 · cited 1× · see citing works
“Beclin1 is a component of the nucleation complex, along with ATG14, lipid kinase VPS34/PI3KIII, and VPS15/PIK3R4 (Itakura et al. 2008, Matsunaga et al. 2009, Sun et al. 2008, Zhong et al. 2009).”
Background
Loss of mTOR-Dependent Macroautophagy Causes Autistic-like Synaptic Pruning Deficits
Tang, G., Gudsnuk, K., Kuo, S.-H., Cotrina, M. L., Rosoklija, G., Sosunov, A., Sonders, M. S., Kanter, E., Castagna, C., Yamamoto, A., et al. (2014) · Neuron · doi:10.1016/j.neuron.2014.07.040 · Cited by 1,146 · cited 1× · see citing works
“These results indicated that basal autophagy is necessary for postnatal spine pruning (Tang et al. 2014).”
Background
Tor-Mediated Induction of Autophagy via an Apg1 Protein Kinase Complex
Kamada, Y., Funakoshi, T., Shintani, T., Nagano, K., Ohsumi, M., & Ohsumi, Y. (2000) · The Journal of Cell Biology · doi:10.1083/jcb.150.6.1507 · Cited by 1,145 · cited 1× · see citing works
“When activated, ULK1 phosphorylates other autophagy pathway components, including Beclin1 (BECN1) and ATG9 (Feng et al. 2014, Kamada et al. 2000, Russell et al. 2013, Zhou et al. 2017).”
Background
A subdomain of the endoplasmic reticulum forms a cradle for autophagosome formation
Hayashi-Nishino, M., Fujita, N., Noda, T., Yamaguchi, A., Yoshimori, T., & Yamamoto, A. (2009) · Nature Cell Biology · doi:10.1038/ncb1991 · Cited by 1,083 · cited 1× · see citing works
“…plasma membrane (Hollenbeck 1993; Ravikumar 2010), mitochondria (Hailey et al. 2010), Golgi (van der Vaart et al. 2010), ER (Hamasaki et al. 2013, Hayashi-Nishino et al. 2009, Ylä-Anttila et al. 2009), and recycling endosomes (Puri et al. 2018), has been implicated in autophagy at some point.”
Background
The pre‐autophagosomal structure organized by concerted functions of APG genes is essential for autophagosome formation
Suzuki, K., Kirisako, T., Kamada, Y., Mizushima, N., Noda, T., & Ohsumi, Y. (2001) · EMBO Journal · doi:10.1093/emboj/20.21.5971 · Cited by 1,069 · cited 1× · see citing works
“The ATG12-ATG5 conjugate, along with ATG16L1, acts as the E3-like enzyme to conjugate mATG8s to phosphatidylethanolamine (PE) (Mizushima et al. 2001, Suzuki et al. 2001).”
Background
Historical landmarks of autophagy research
Ohsumi, Y. (2013) · Cell Research · doi:10.1038/cr.2013.169 · Cited by 1,030 · cited 1× · see citing works
“The molecular players in this pathway have been well-defined from decades of elegant work in yeast (Ohsumi 2014).”
Background
Distinct regulation of autophagic activity by Atg14L and Rubicon associated with Beclin 1–phosphatidylinositol-3-kinase complex
Zhong, Y., Wang, Q. J., Li, X., Yan, Y., Backer, J. M., Chait, B. T., Heintz, N., & Yue, Z. (2009) · Nature Cell Biology · doi:10.1038/ncb1854 · Cited by 1,005 · cited 2× · see citing works
“Beclin1 is a component of the nucleation complex, along with ATG14, lipid kinase VPS34/PI3KIII, and VPS15/PIK3R4 (Itakura et al. 2008, Matsunaga et al. 2009, Sun et al. 2008, Zhong et al. 2009).”
Background
Two Distinct Vps34 Phosphatidylinositol 3–Kinase Complexes Function in Autophagy and Carboxypeptidase Y Sorting in Saccharomyces cerevisiae
Kihara, A., Noda, T., Ishihara, N., & Ohsumi, Y. (2001) · The Journal of Cell Biology · doi:10.1083/jcb.152.3.519 · Cited by 1,004 · cited 1× · see citing works
“The nucleation complex generates PI3P, an important component of the autophagosome membrane during biogenesis (Kihara et al. 2001, Obara et al. 2006).”
Background
Exome sequencing in amyotrophic lateral sclerosis identifies risk genes and pathways
Cirulli, E. T., Lasseigne, B. N., Petrovski, S., Sapp, P. C., Dion, P. A., Leblond, C. S., Couthouis, J., Lu, Y.-F., Wang, Q., Krueger, B. J., et al. (2015) · Science · doi:10.1126/science.aaa3650 · Cited by 966 · cited 12× · see citing works
“J. Neurosci 23(4):1254–64 [PubMed: 12598614] Freischmidt A, Wieland T, Richter B, Ruf W, Schaeffer V, et al. 2015 Haploinsufficiency of TBK1 causes familial ALS and fronto-temporal dementia.”
BackgroundInfluential
Regulation of endoplasmic reticulum turnover by selective autophagy
Khaminets, A., Heinrich, T., Mari, M., Grumati, P., Huebner, A. K., Akutsu, M., Liebmann, L., Stolz, A., Nietzsche, S., Koch, N., et al. (2015) · Nature · doi:10.1038/nature14498 · Cited by 956 · cited 2× · see citing works
“Similarly, Fam134b−/− mice exhibit sensory neuropathy and an age-dependent loss of sensory axons, with impaired ER turnover apparent at the cellular level (Khaminets et al. 2015).”
Background
PINK1 is activated by mitochondrial membrane potential depolarization and stimulates Parkin E3 ligase activity by phosphorylating Serine 65
Kondapalli, C., Kazlauskaite, A., Zhang, N., Woodroof, H. I., Campbell, D. G., Gourlay, R., Burchell, L., Walden, H., Macartney, T. J., Deak, M., et al. (2012) · Open Biology · doi:10.1098/rsob.120080 · Cited by 940 · cited 1× · see citing works
“This allows PINK1 to phosphorylate Parkin, leading to Parkin recruitment and activation (Kondapalli et al. 2012, Shiba-Fukushima et al. 2012).”
Background
Parkin-deficient Mice Exhibit Nigrostriatal Deficits but Not Loss of Dopaminergic Neurons
Goldberg, M. S., Fleming, S. M., Palacino, J. J., Cepeda, C., Lam, H. A., Bhatnagar, A., Meloni, E. G., Wu, N., Ackerson, L. C., Klapstein, G. J., et al. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m308947200 · Cited by 913 · cited 1× · see citing works
“Knockout mice exhibit relatively subtle phenotypes, including altered synaptic excitability and decreased dopamine release, which do not clearly model human PD (Goldberg et al. 2003, Kitada et al. 2007, Perez & Palmiter 2005).”
Background
Plasma membrane contributes to the formation of pre-autophagosomal structures
Ravikumar, B., Moreau, K., Jahreiss, L., Puri, C., & Rubinsztein, D. C. (2010) · Nature Cell Biology · doi:10.1038/ncb2078 · Cited by 902 · see citing works
Cargo recognition failure is responsible for inefficient autophagy in Huntington’s disease
Martinez-Vicente, M., Talloczy, Z., Wong, E., Tang, G., Koga, H., Kaushik, S., de Vries, R., Arias, E., Harris, S., Sulzer, D., et al. (2010) · Nature Neuroscience · doi:10.1038/nn.2528 · Cited by 885 · cited 1× · see citing works
“…at multiple points in the pathway, including autophagosome biogenesis (De Pace et al. 2018, Rui et al. 2015, Stavoe & Holzbaur 2018), cargo-loading (Martinez-Vicente et al. 2010, Rudnick et al. 2017), intracellular transport (Nicolas et al. 2018, Wong & Holzbaur 2014b), and autophagosomelysosome…”
Background
Characterization of autophagosome formation site by a hierarchical analysis of mammalian Atg proteins
Itakura, E., & Mizushima, N. (2010) · Autophagy · doi:10.4161/auto.6.6.12709 · Cited by 843 · cited 1× · see citing works
“The step-wise autophagosome biogenesis pathway elucidated in yeast and mammalian cell culture (Itakura & Mizushima 2010, Koyama-Honda et al. 2013) appears to be consistent with the pathway for biogenesis in the distal axon (Maday & Holzbaur 2014).”
Result
Optineurin is an autophagy receptor for damaged mitochondria in parkin-mediated mitophagy that is disrupted by an ALS-linked mutation
Wong, Y. C., & Holzbaur, E. L. F. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1405752111 · Cited by 812 · see citing works
Self-citation
The Rab7 effector protein RILP controls lysosomal transport by inducing the recruitment of dynein-dynactin motors
Jordens, I., Fernandez-Borja, M., Marsman, M., Dusseljee, S., Janssen, L., Calafat, J., Janssen, H., Wubbolts, R., & Neefjes, J. (2001) · Current Biology · doi:10.1016/s0960-9822(01)00531-0 · Cited by 811 · cited 1× · see citing works
“Dynein is recruited to autophagosomes by RAB7 and RILP (Cheng et al. 2015, Jordens et al. 2001, Wijdeven et al. 2016).”
Background
p62/SQSTM1 is required for Parkin-induced mitochondrial clustering but not mitophagy; VDAC1 is dispensable for both
Narendra, D. P., Kane, L. A., Hauser, D., Fearnley, I., & Youle, R. (2010) · Autophagy · doi:10.4161/auto.6.8.13426 · Cited by 800 · cited 5× · see citing works
“This feedforward mechanism leads to the rapid ubiquitination of OMM proteins by Parkin (Narendra et al. 2010b) that serve as a binding platform for ubiquitin-binding mitophagy receptors.”
BackgroundInfluential
Beclin1-binding UVRAG targets the class C Vps complex to coordinate autophagosome maturation and endocytic trafficking
Liang, C., Lee, J.-S., Inn, K.-S., Gack, M. U., Li, Q., Roberts, E. A., Vergne, I., Deretic, V., Feng, P., Akazawa, C., et al. (2008) · Nature Cell Biology · doi:10.1038/ncb1740 · Cited by 792 · cited 1× · see citing works
“Several components of the nucleation complex also function in cellular processes other than autophagy (Liang et al. 2008, Lindmo & Stenmark 2006, Annu Rev Cell Dev Biol.”
Background
Mouse Apg16L, a novel WD-repeat protein, targets to the autophagic isolation membrane with the Apg12-Apg5 conjugate
Mizushima, N., Kuma, A., Kobayashi, Y., Yamamoto, A., Matsubae, M., Takao, T., Natsume, T., Ohsumi, Y., & Yoshimori, T. (2003) · Journal of Cell Science · doi:10.1242/jcs.00381 · Cited by 791 · cited 1× · see citing works
“Around the time the autophagosome membrane fuses with itself, the biogenesis machinery dissociates from the fully formed autophagosome, with the exception of the mATG8s, which remain tightly associated with the limiting membrane (Mizushima et al. 2003).”
Background
Haploinsufficiency of TBK1 causes familial ALS and fronto-temporal dementia
Freischmidt, A., Wieland, T., Richter, B., Ruf, W., Schaeffer, V., Müller, K., Marroquin, N., Nordin, F., Hübers, A., Weydt, P., et al. (2015) · Nature Neuroscience · doi:10.1038/nn.4000 · Cited by 786 · cited 1× · see citing works
“…that OPTN and TBK1 are involved in mitophagy downstream from PINK1 and Parkin, is particularly interesting because mutations in both OPTN and TBK1 are causative for rare forms of familial amyotrophic lateral sclerosis (ALS) (Cirulli et al. 2015, Freischmidt et al. 2015, Maruyama et al. 2010).”
Background
Phosphorylation of OPTN by TBK1 enhances its binding to Ub chains and promotes selective autophagy of damaged mitochondria
Richter, B., Sliter, D. A., Herhaus, L., Stolz, A., Wang, C., Beli, P., Zaffagnini, G., Wild, P., Martens, S., Wagner, S. A., et al. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1523926113 · Cited by 755 · see citing works
GABAA-receptor-associated protein links GABAA receptors and the cytoskeleton
Wang, H.-B., Bedford, F., Brandon, N., Moss, S., & Olsen, R. (1999) · Nature · doi:10.1038/16264 · Cited by 754 · cited 2× · see citing works
“Dendritic autophagy The GABARAP subfamily of mATG8s, as its name suggests, was initially identified to interact with GABAA receptors by yeast-two-hybrid screening (Wang et al. 1999).”
Background
Promoting basal levels of autophagy in the nervous system enhances longevity and oxidant resistance in adult Drosophila
Simonsen, A., Cumming, R. C., Brech, A., Isakson, P., Schubert, D. R., & Finley, K. D. (2008) · Autophagy · doi:10.4161/auto.5269 · Cited by 716 · cited 2× · see citing works
“However, driving dAtg8 overexpression pan-neuronally using earlier-expressing ELAV-Gal4 did not extend lifespan, suggesting that the age of autophagy ectopic induction is important (Simonsen et al. 2008).”
Background
Autophagosomes initiate distally and mature during transport toward the cell soma in primary neurons
Maday, S., Wallace, K. E., & Holzbaur, E. L. F. (2012) · Journal of Cell Biology · doi:10.1083/jcb.201106120 · Cited by 681 · cited 6× · see citing works
“These autophagosomes were then rapidly transported back to the cell body (Cheng et al. 2015, Lee et al. 2011, Maday & Holzbaur 2014, Maday et al. 2012).”
BackgroundInfluentialSelf-citation
Genome-wide analysis reveals mechanisms modulating autophagy in normal brain aging and in Alzheimer’s disease
Lipinski, M. M., Zheng, B., Lu, T., Yan, Z., Py, B. F., Ng, A., Xavier, R. J., Li, C., Yankner, B. A., Scherzer, C. R., et al. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1009485107 · Cited by 680 · cited 1× · see citing works
“Similarly, in human brain, mRNA levels of Atg5, Atg7, Beclin1, and GABARAPL2 decrease with age; however, correlated protein level decreases were not assessed (Lipinski et al. 2010, Shibata et al. 2006).”
Background
3D tomography reveals connections between the phagophore and endoplasmic reticulum
Ylä-Anttila, P., Vihinen, H., Jokitalo, E., & Eskelinen, E.-L. (2009) · Autophagy · doi:10.4161/auto.5.8.10274 · Cited by 665 · cited 1× · see citing works
“…plasma membrane (Hollenbeck 1993; Ravikumar 2010), mitochondria (Hailey et al. 2010), Golgi (van der Vaart et al. 2010), ER (Hamasaki et al. 2013, Hayashi-Nishino et al. 2009, Ylä-Anttila et al. 2009), and recycling endosomes (Puri et al. 2018), has been implicated in autophagy at some point.”
Background
<emph type="ital">SQSTM1</emph> Mutations in Familial and Sporadic Amyotrophic Lateral Sclerosis
Fecto, F. (2011) · Archives of Neurology · doi:10.1001/archneurol.2011.250 · Cited by 650 · cited 1× · see citing works
“Supporting the importance of p62 in neurons, mutations in p62/SQSTM1 are implicated in ALS/FTD (frontotemporal dementia) and ataxia (Fecto et al. 2011, Haack et al. 2016).”
Background
Essential role for autophagy protein Atg7 in the maintenance of axonal homeostasis and the prevention of axonal degeneration
Komatsu, M., Wang, Q. J., Holstein, G. R., Friedrich, V. L., Iwata, J.-I., Kominami, E., Chait, B. T., Tanaka, K., & Yue, Z. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0701311104 · Cited by 614 · cited 3× · see citing works
“Likewise, conditionally knocking out Atg7 in Purkinje cells using the Pcp2 promoter in mice did not appear to affect dendrites, but did lead to neuronal and axonal dystrophy, degeneration of axon terminals, and eventual neuronal death (Komatsu et al. 2007b).”
Background
Beclin 1 Gene Transfer Activates Autophagy and Ameliorates the Neurodegenerative Pathology in α-Synuclein Models of Parkinson's and Lewy Body Diseases
Spencer, B., Potkar, R., Trejo, M., Rockenstein, E., Patrick, C., Gindi, R., Adame, A., Wyss-Coray, T., & Masliah, E. (2009) · The Journal of Neuroscience · doi:10.1523/jneurosci.4390-09.2009 · Cited by 595 · cited 1× · see citing works
“A uthor M anuscript A uthor M anuscript A uthor M anuscript A uthor M anuscript α-synuclein accumulation (Spencer et al. 2009).”
Background
Basal Mitophagy Occurs Independently of PINK1 in Mouse Tissues of High Metabolic Demand
McWilliams, T. G., Prescott, A. R., Montava-Garriga, L., Ball, G., Singh, F., Barini, E., Muqit, M. M. K., Brooks, S. P., & Ganley, I. G. (2018) · Cell Metabolism · doi:10.1016/j.cmet.2017.12.008 · Cited by 591 · cited 1× · see citing works
“Analysis of mitochondrial turnover in PINK1 knockout mice suggests that there are additional, PINK1-independent pathways leading to mitophagy in neurons under basal conditions (McWilliams et al. 2018), which remain to be more fully characterized.”
Background
PINK1-mediated phosphorylation of the Parkin ubiquitin-like domain primes mitochondrial translocation of Parkin and regulates mitophagy
Shiba-Fukushima, K., Imai, Y., Yoshida, S., Ishihama, Y., Kanao, T., Sato, S., & Hattori, N. (2012) · Scientific Reports · doi:10.1038/srep01002 · Cited by 577 · cited 1× · see citing works
“This allows PINK1 to phosphorylate Parkin, leading to Parkin recruitment and activation (Kondapalli et al. 2012, Shiba-Fukushima et al. 2012).”
Background
Impaired dopamine release and synaptic plasticity in the striatum of PINK1-deficient mice
Kitada, T., Pisani, A., Porter, D. R., Yamaguchi, H., Tscherter, A., Martella, G., Bonsi, P., Zhang, C., Pothos, E. N., & Shen, J. (2007) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.0702717104 · Cited by 562 · cited 1× · see citing works
“Knockout mice exhibit relatively subtle phenotypes, including altered synaptic excitability and decreased dopamine release, which do not clearly model human PD (Goldberg et al. 2003, Kitada et al. 2007, Perez & Palmiter 2005).”
Background
Promoting the clearance of neurotoxic proteins in neurodegenerative disorders of ageing
Boland, B., Yu, W. H., Corti, O., Mollereau, B., Henriques, A., Bézard, E., Pastores, G., Rubinsztein, D. C., Nixon, R. A., Duchen, M. R., et al. (2018) · Nature Reviews Drug Discovery · doi:10.1038/nrd.2018.109 · Cited by 561 · cited 2× · see citing works
“Observations from both experimental models and post-mortem analysis of human tissues suggest that dysfunction of autophagy may be a common contributor to the pathogenic process across these diseases (recently reviewed by (Boland et al. 2018, Chu 2018)).”
Background
VPS13A and VPS13C are lipid transport proteins differentially localized at ER contact sites
Kumar, N., Leonzino, M., Hancock-Cerutti, W., Horenkamp, F., Li, P., Lees, J., Wheeler, H., Reinisch, K., & Camilli, P. D. (2018) · Journal of Cell Biology · doi:10.1083/jcb.201807019 · Cited by 544 · cited 1× · see citing works
“VPS13 is a lipid transporter between ER and other membranes, raising the possibility that ATG2 also functions as a lipid transporter that supplies lipids to the growing autophagosomal membrane (Kumar et al. 2018).”
Background
Identification of Barkor as a mammalian autophagy-specific factor for Beclin 1 and class III phosphatidylinositol 3-kinase
Sun, Q., Fan, W., Chen, K., Ding, X., Chen, S., & Zhong, Q. (2008) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.0810452105 · Cited by 523 · cited 1× · see citing works
“Beclin1 is a component of the nucleation complex, along with ATG14, lipid kinase VPS34/PI3KIII, and VPS15/PIK3R4 (Itakura et al. 2008, Matsunaga et al. 2009, Sun et al. 2008, Zhong et al. 2009).”
Background
Mitophagy of damaged mitochondria occurs locally in distal neuronal axons and requires PINK1 and Parkin
Ashrafi, G., Schlehe, J. S., LaVoie, M. J., & Schwarz, T. L. (2014) · Journal of Cell Biology · doi:10.1083/jcb.201401070 · Cited by 502 · cited 1× · see citing works
“One group reported localized mitophagy along the axons of hippocampal neurons upon induction of cellular stress via mitochondrial depolarization or ROS generation (Ashrafi et al. 2014).”
Background
mito-QC illuminates mitophagy and mitochondrial architecture in vivo
McWilliams, T. G., Prescott, A., Allen, G., Tamjar, J., Munson, M. J., Thomson, C., Muqit, M., & Ganley, I. (2016) · Journal of Cell Biology · doi:10.1083/jcb.201603039 · Cited by 493 · cited 2× · see citing works
“For example, non-selective axonal autophagy is differentially regulated than the selective removal of damaged mitochondria from the soma (Cornelissen et al. 2018, Devireddy et al. 2015, McWilliams et al. 2016, Sung et al. 2016).”
Background
The ATG conjugation systems are important for degradation of the inner autophagosomal membrane
Tsuboyama, K., Koyama-Honda, I., Sakamaki, Y., Koike, M., Morishita, H., & Mizushima, N. (2016) · Science · doi:10.1126/science.aaf6136 · Cited by 485 · cited 1× · see citing works
“However, the mATG8s have been implicated in this step (Tsuboyama et al. 2016).”
Background
Parkin-deficient mice are not a robust model of parkinsonism
Perez, F. A., & Palmiter, R. D. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0409598102 · Cited by 477 · cited 1× · see citing works
“Knockout mice exhibit relatively subtle phenotypes, including altered synaptic excitability and decreased dopamine release, which do not clearly model human PD (Goldberg et al. 2003, Kitada et al. 2007, Perez & Palmiter 2005).”
Background
Regulation of membrane traffic by phosphoinositide 3-kinases
Lindmo, K., & Stenmark, H. (2006) · Journal of Cell Science · doi:10.1242/jcs.02855 · Cited by 463 · cited 1× · see citing works
“Several components of the nucleation complex also function in cellular processes other than autophagy (Liang et al. 2008, Lindmo & Stenmark 2006, Annu Rev Cell Dev Biol.”
Background
Lysosomal proteolysis inhibition selectively disrupts axonal transport of degradative organelles and causes an Alzheimer’s-like axonal dystrophy
Lee, S., Sato, Y., & Nixon, R. (2011) · Journal of Neuroscience · doi:10.1523/jneurosci.6412-10.2011 · Cited by 461 · cited 2× · see citing works
“One significant difference is that axonal autophagosomes form constitutively under fed conditions (Cheng et al. 2015, Lee et al. 2011, Maday & Holzbaur 2014, 2016; Maday et al. 2012, Stavoe et al. 2016), in contrast, to the induction of autophagy in nutrient-limiting conditions observed in many…”
Background
Regulation of intracellular accumulation of mutant Huntingtin by Beclin 1
Shibata, M., Lu, T., Furuya, T., Degterev, A., Mizushima, N., Yoshimori, T., MacDonald, M., Yankner, B., & Yuan, J. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m600364200 · Cited by 458 · cited 1× · see citing works
“Similarly, in human brain, mRNA levels of Atg5, Atg7, Beclin1, and GABARAPL2 decrease with age; however, correlated protein level decreases were not assessed (Lipinski et al. 2010, Shibata et al. 2006).”
Background
Autophagy requires endoplasmic reticulum targeting of the PI3-kinase complex via Atg14L
Matsunaga, K., Morita, E., Saitoh, T., Akira, S., Ktistakis, N. T., Izumi, T., Noda, T., & Yoshimori, T. (2010) · Journal of Cell Biology · doi:10.1083/jcb.200911141 · Cited by 456 · cited 1× · see citing works
“In contrast, ATG14 is specifically required for the proper localization of the nucleation complex to the forming autophagosome (Matsunaga et al. 2010); ATG14 also recruits other autophagosome biogenesis components to the initial autophagosome membrane, termed the isolation membrane in mammals.”
Background
FINE STRUCTURE OF NERVE FIBERS AND GROWTH CONES OF ISOLATED SYMPATHETIC NEURONS IN CULTURE
Bunge, M. (1973) · Journal of Cell Biology · doi:10.1083/jcb.56.3.713 · Cited by 452 · cited 1× · see citing works
“This work was consistent with electron microscopy studies of primary rat sympathetic motor neurons identifying autophagic vesicles in distal growth cones (Bunge 1973).”
Result
Contacts between the endoplasmic reticulum and other membranes in neurons
Wu, Y.-M., Whiteus, C., Xu, S. C., Hayworth, K. J., Weinberg, R., Hess, H. F., & Camilli, P. D. (2017) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.1701078114 · Cited by 449 · cited 1× · see citing works
“Three-dimensional reconstructions of the ER in mouse brain show the dramatic extension of ER tubules throughout the soma, dendrites and axon of neurons in vivo (Wu et al. 2017).”
Background
Translocon component Sec62 acts in endoplasmic reticulum turnover during stress recovery
Fumagalli, F., Noack, J., Bergmann, T., Cebollero, E., Pisoni, G. B., Fasana, E., Fregno, I., Galli, C., Loi, M., Soldà, T., et al. (2016) · Nature Cell Biology · doi:10.1038/ncb3423 · Cited by 438 · cited 1× · see citing works
“…multiple ER-associated proteins with LIR motifs that mediate binding to LC3-family proteins, including FAM134B/RETREG1 (reticulophagy regulator 1), reticulon 3L (RTN3), and CCPG1 (cell cycle progression 1) (Fumagalli et al. 2016, Grumati et al. 2018, Khaminets et al. 2015, Smith et al. 2018).”
Background
C. elegans Screen Identifies Autophagy Genes Specific to Multicellular Organisms
Tian, Y., Li, Z., Hu, W., Ren, H., Tian, E., Zhao, Y., Lu, Q., Huang, X., Yang, P., Li, X., et al. (2010) · Cell · doi:10.1016/j.cell.2010.04.034 · Cited by 434 · see citing works
Huntingtin functions as a scaffold for selective macroautophagy
Rui, Y.-N., Xu, Z., Patel, B., Chen, Z., Chen, D., Tito, A., David, G., Sun, Y., Stimming, E. F., Bellen, H. J., et al. (2015) · Nature Cell Biology · doi:10.1038/ncb3101 · Cited by 423 · cited 1× · see citing works
“…have demonstrated aging or disease-associated deficits at multiple points in the pathway, including autophagosome biogenesis (De Pace et al. 2018, Rui et al. 2015, Stavoe & Holzbaur 2018), cargo-loading (Martinez-Vicente et al. 2010, Rudnick et al. 2017), intracellular transport (Nicolas et al.…”
Background
Genome-wide Analyses Identify KIF5A as a Novel ALS Gene
Nicolas, A., Kenna, K., Renton, A., Ticozzi, N., Faghri, F., Chia, R., Dominov, J., Kenna, B. J., Nalls, M., Keagle, P., et al. (2018) · Neuron · doi:10.2139/ssrn.3155776 · Cited by 417 · cited 1×
“…et al. 2018, Rui et al. 2015, Stavoe & Holzbaur 2018), cargo-loading (Martinez-Vicente et al. 2010, Rudnick et al. 2017), intracellular transport (Nicolas et al. 2018, Wong & Holzbaur 2014b), and autophagosomelysosome fusion or acidification (Lie & Nixon 2018, Nixon et al. 2005) across disease…”
Background
CCPG1 Is a Non-canonical Autophagy Cargo Receptor Essential for ER-Phagy and Pancreatic ER Proteostasis
Smith, M. D., Harley, M., Kemp, A. J., Wills, J., Lee, M., Arends, M., von Kriegsheim, A., Behrends, C., & Wilkinson, S. (2017) · Developmental Cell · doi:10.1016/j.devcel.2017.11.024 · Cited by 416 · see citing works
Massive accumulation of luminal protease-deficient axonal lysosomes at Alzheimer’s disease amyloid plaques
Gowrishankar, S., Yuan, P., Wu, Y., Schrag, M., Paradise, S., Grutzendler, J., De Camilli, P., & Ferguson, S. M. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1510329112 · Cited by 406 · cited 1× · see citing works
“While there are lysosomes present in the axon, they lack the full complement of degradative enzymes found in somal lysosomes (Cheng et al. 2018, Gowrishankar et al. 2015).”
Background
HsAtg4B/HsApg4B/Autophagin-1 Cleaves the Carboxyl Termini of Three Human Atg8 Homologues and Delipidates Microtubule-associated Protein Light Chain 3- and GABAA Receptor-associated Protein-Phospholipid Conjugates*
Tanida, I., Sou, Y., Ezaki, J., Minematsu-Ikeguchi, N., Ueno, T., & Kominami, E. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m401461200 · Cited by 396 · cited 1× · see citing works
“ATG4 also acts at the end of autophagy to cleave mATG8s from the cytosolic face of the completed autophagosome (Kauffman et al. 2018, Tanida et al. 2004).”
Background
The Regulation of Autophagosome Dynamics by Huntingtin and HAP1 Is Disrupted by Expression of Mutant Huntingtin, Leading to Defective Cargo Degradation
Wong, Y., & Holzbaur, E. (2014) · Journal of Neuroscience · doi:10.1523/jneurosci.1870-13.2014 · Cited by 380 · see citing works
Self-citation
Autophagosome Biogenesis in Primary Neurons Follows an Ordered and Spatially Regulated Pathway
Maday, S., & Holzbaur, E. L. F. (2014) · Developmental Cell · doi:10.1016/j.devcel.2014.06.001 · Cited by 372 · see citing works
Self-citation
Selective autophagy as a potential therapeutic target for neurodegenerative disorders
Scrivo, A., Bourdenx, M., Pampliega, O., & Cuervo, A. M. (2018) · The Lancet Neurology · doi:10.1016/s1474-4422(18)30238-2 · Cited by 355 · cited 1× · see citing works
“Deficits in intersecting pathways such as the ubiquitin-proteasome pathway and lysosomal degradation via chaperone-mediated autophagy are also likely to contribute to neurodegenerative disease (Scrivo et al. 2018).”
Background
p62 filaments capture and present ubiquitinated cargos for autophagy
Zaffagnini, G., Savova, A., Danieli, A., Romanov, J., Tremel, S., Ebner, M., Peterbauer, T., Sztacho, M., Trapannone, R., Tarafder, A., et al. (2018) · EMBO Journal · doi:10.15252/embj.201798308 · Cited by 349 · cited 1× · see citing works
“In vitro studies indicate that p62 is sufficient to induce the clustering of ubiquitinated proteins, known as cargo nucleation, into aggregates that can be targeted by autophagy (Zaffagnini et al. 2018).”
Background
Regulation of presynaptic neurotransmission by macroautophagy
Hernandez, D., Torres, C. A., Setlik, W., Cebrián, C., Mosharov, E., Tang, G.-M., Cheng, H.-C., Kholodilov, N., Yarygina, O., Burke, R., et al. (2012) · Neuron · doi:10.1016/j.neuron.2012.02.020 · Cited by 346 · cited 1× · see citing works
“Thus, these data suggest that autophagy acts in dopamine neurons to restrict synaptic transmission (Hernandez et al. 2012).”
Background
Spatial Parkin Translocation and Degradation of Damaged Mitochondria via Mitophagy in Live Cortical Neurons
Cai, Q., Zakaria, H. M., Simone, A., & Sheng, Z. (2012) · Current Biology · doi:10.1016/j.cub.2012.02.005 · Cited by 345 · cited 1× · see citing works
“Conversely, GFP-LC3 was rarely observed associated with axonal mitochondria in these experiments (Cai et al. 2012).”
Dynamic recruitment and activation of ALS-associated TBK1 with its target optineurin are required for efficient mitophagy
Moore, A. S., & Holzbaur, E. (2016) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.1523810113 · Cited by 329 · see citing works
Self-citation
Compartment-Specific Regulation of Autophagy in Primary Neurons
Maday, S., & Holzbaur, E. L. F. (2016) · The Journal of Neuroscience · doi:10.1523/jneurosci.4401-15.2016 · Cited by 309 · see citing works
Self-citation
Disrupted Autophagy Leads to Dopaminergic Axon and Dendrite Degeneration and Promotes Presynaptic Accumulation of α-Synuclein and LRRK2 in the Brain
Friedman, L. G., Lachenmayer, M. L., Wang, J., He, L., Poulose, S. M., Komatsu, M., Holstein, G. R., & Yue, Z. (2012) · The Journal of Neuroscience · doi:10.1523/jneurosci.5809-11.2012 · Cited by 303 · cited 1× · see citing works
“These swellings contained ubiquitinated filamentous inclusions that were also observed in cell bodies (Friedman et al. 2012).”
Background
MUL1 acts in parallel to the PINK1/parkin pathway in regulating mitofusin and compensates for loss of PINK1/parkin
Yun, J.-N., Puri, R., Yang, H., Lizzio, M. A., Wu, C.-L., Sheng, Z.-H., & Guo, M. (2014) · eLife · doi:10.7554/elife.01958 · Cited by 298 · cited 1× · see citing works
“For example, mitochondrial ubiquitin ligase 1 (MUL1 or Mulan) has been proposed to function in a parallel pathway to Parkin in the clearance of damaged mitochondria (Yun et al. 2014).”
Background
Products of endocytosis and autophagy are retrieved from axons by regulated retrograde organelle transport
Hollenbeck, P. (1993) · Journal of Cell Biology · doi:10.1083/jcb.121.2.305 · Cited by 292 · cited 2× · see citing works
“Virtually every possible membrane source, including plasma membrane (Hollenbeck 1993; Ravikumar 2010), mitochondria (Hailey et al. 2010), Golgi (van der Vaart et al. 2010), ER (Hamasaki et al. 2013, Hayashi-Nishino et al. 2009, Ylä-Anttila et al. 2009), and recycling endosomes (Puri et al. 2018),…”
Background
Neuronal stimulation induces autophagy in hippocampal neurons that is involved in AMPA receptor degradation after chemical long-term depression
Shehata, M., Matsumura, H., Okubo-Suzuki, R., Ohkawa, N., & Inokuchi, K. (2012) · The Journal of Neuroscience · doi:10.1523/jneurosci.4533-11.2012 · Cited by 285 · cited 5× · see citing works
“Upon stimulation with low-dose NMDA, dendritic spines displayed an increase in GFP-LC3 puncta.”
BackgroundInfluential
Deconstruction for Reconstruction: The Role of Proteolysis in Neural Plasticity and Disease
Bingol, B., & Sheng, M. (2011) · Neuron · doi:10.1016/j.neuron.2010.11.006 · Cited by 275 · cited 1× · see citing works
“Multiple degradative pathways are at work in neurons, such as the degradation of misfolded proteins via the ubiquitin-proteasome pathway (Bingol & Sheng 2011).”
Background
Mutations in FAM134B, encoding a newly identified Golgi protein, cause severe sensory and autonomic neuropathy
Kurth, I., Pamminger, T., Hennings, J. C., Soehendra, D., Huebner, A. K., Rotthier, A., Baets, J., Senderek, J., Topaloglu, H., Farrell, S. A., et al. (2009) · Nature Genetics · doi:10.1038/ng.464 · Cited by 260 · cited 1× · see citing works
“Genetic studies indicate that FAM134B, an ERphagy receptor, is required to maintain neuronal homeostasis, as mutations cause a sensory and autonomic neuropathy known as HSAN-II (Kurth et al. 2009).”
Background
A LRRK2-Dependent EndophilinA Phosphoswitch Is Critical for Macroautophagy at Presynaptic Terminals.
Soukup, S.-F., Kuenen, S., Vanhauwaert, R., Manetsberger, J., Hernández-Díaz, S., Swerts, J., Schoovaerts, N., Vilain, S., Gounko, N. V., Vints, K., et al. (2016) · Neuron · doi:10.1016/j.neuron.2016.09.037 · Cited by 260 · cited 3× · see citing works
“In Drosophila, autophagosome biogenesis also occurred at the neuromuscular junction (NMJ) in the distal axon of motor neurons (Neisch et al. 2017, Soukup et al. 2016).”
Background
Autophagy Is Required for Memory Formation and Reverses Age-Related Memory Decline
Glatigny, M., Moriceau, S., Rivagorda, M., Ramos-Brossier, M., Nascimbeni, A. C., Lante, F., Shanley, M. R., Boudarene, N., Rousseaud, A., Friedman, A. K., et al. (2019) · Current Biology · doi:10.1016/j.cub.2018.12.021 · Cited by 257 · cited 3× · see citing works
“The LC3-II/LC3-I ratio also decreased with age (Glatigny et al. 2019).”
BackgroundResultInfluential
Autophagy promotes synapse development in Drosophila
Shen, W., & Ganetzky, B. (2009) · Journal of Cell Biology · doi:10.1083/jcb.200907109 · Cited by 252 · cited 1× · see citing works
“Additionally, overexpression of Atg1 increased NMJ synaptic bouton number in an autophagy-dependent manner (Shen & Ganetzky 2009).”
Background
Assortment of phosphatidylinositol 3-kinase complexes--Atg14p directs association of complex I to the pre-autophagosomal structure in Saccharomyces cerevisiae.
Obara, K., Sekito, T., & Ohsumi, Y. (2006) · Molecular Biology of the Cell · doi:10.1091/mbc.e05-09-0841 · Cited by 247 · cited 1× · see citing works
“The nucleation complex generates PI3P, an important component of the autophagosome membrane during biogenesis (Kihara et al. 2001, Obara et al. 2006).”
Background
Lysosome trafficking and signaling in health and neurodegenerative diseases
Lie, P., & Nixon, R. (2018) · Neurobiology of Disease · doi:10.1016/j.nbd.2018.05.015 · Cited by 242 · see citing works
Spatiotemporal regulation of autophagy during Caenorhabditis elegans aging
Chang, J. T., Kumsta, C., Hellman, A. B., Adams, L. M., & Hansen, M. (2017) · eLife · doi:10.7554/elife.18459 · Cited by 241 · cited 1× · see citing works
“However, age appears to affect neuronal autophagy more variably than other tissues (Chang et al. 2017).”
Background
Characterization of LAMP1-labeled nondegradative lysosomal and endocytic compartments in neurons
Cheng, X.-T., Xie, Y.-X., Zhou, B., Huang, N., Farfel-Becker, T., & Sheng, Z.-H. (2018) · Journal of Cell Biology · doi:10.1083/jcb.201711083 · Cited by 240 · cited 1× · see citing works
“While there are lysosomes present in the axon, they lack the full complement of degradative enzymes found in somal lysosomes (Cheng et al. 2018, Gowrishankar et al. 2015).”
Background
Dual roles of Atg8−PE deconjugation by Atg4 in autophagy
Yu, Z.-Q., Ni, T., Hong, B., Wang, H., Jiang, F.-J., Zou, S.-S., Chen, Y., Zheng, X.-L., Klionsky, D., Liang, Y.-H., et al. (2012) · Autophagy · doi:10.4161/auto.19652 · Cited by 240 · cited 1× · see citing works
“…outer membrane by PI3P phosphatases (Cebollero et al. 2012) and mATG8s are removed from the outer membrane by ATG4 (Kauffman et al. 2018, Nair et al. 2012, Yu et al. 2012), possibly destabilizing the association of other autophagy components with the cytosolic face of the autophagosomal membrane.”
Background
Deficiency of parkin and PINK1 impairs age-dependent mitophagy in Drosophila
Cornelissen, T., Vilain, S., Vints, K., Gounko, N., Verstreken, P., & Vandenberghe, W. (2018) · eLife · doi:10.7554/elife.35878 · Cited by 239 · cited 2× · see citing works
“For example, non-selective axonal autophagy is differentially regulated than the selective removal of damaged mitochondria from the soma (Cornelissen et al. 2018, Devireddy et al. 2015, McWilliams et al. 2016, Sung et al. 2016).”
Background
A role for Atg8–PE deconjugation in autophagosome biogenesis
Nair, U., Yen, W.-L., Mari, M., Cao, Y., Xie, Z.-P., Baba, M., Reggiori, F., & Klionsky, D. (2012) · Autophagy · doi:10.4161/auto.19385 · Cited by 237 · cited 1× · see citing works
“Of note, a loss-of-function mutation in the Atlastin ATL1 is causal for SPG3A, a hereditary spastic paraplegia (Namekawa et al. 2007).”
Background
Neural-specific Deletion of FIP200 Leads to Cerebellar Degeneration Caused by Increased Neuronal Death and Axon Degeneration*
Liang, C.-C., Wang, C.-R., Peng, X., Gan, B., & Guan, J.-L. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.072389 · Cited by 236 · cited 2× · see citing works
“Neuron-specific knock-out of FIP200 in mice using the Nestin promoter triggered neuronal loss of Purkinje cells and granular cells, spongiosis in the cerebellar white matter, axonal and dendritic degeneration in Purkinje cells, axonal swelling, and accumulation of ubiquitinpositive aggregates (Liang et al. 2010).”
Background
Axonal autophagosomes recruit dynein for retrograde transport through fusion with late endosomes
Cheng, X.-T., Zhou, B., Lin, M.-Y., Cai, Q., & Sheng, Z.-H. (2015) · Journal of Cell Biology · doi:10.1083/jcb.201412046 · Cited by 227 · cited 4× · see citing works
“One significant difference is that axonal autophagosomes form constitutively under fed conditions (Cheng et al. 2015, Lee et al. 2011, Maday & Holzbaur 2014, 2016; Maday et al. 2012, Stavoe et al. 2016), in contrast, to the induction of autophagy in nutrient-limiting conditions observed in many…”
BackgroundInfluential
Temporal analysis of recruitment of mammalian ATG proteins to the autophagosome formation site
Koyama-Honda, I., Itakura, E., Fujiwara, T., & Mizushima, N. (2013) · Autophagy · doi:10.4161/auto.25529 · Cited by 227 · cited 1× · see citing works
“The step-wise autophagosome biogenesis pathway elucidated in yeast and mammalian cell culture (Itakura & Mizushima 2010, Koyama-Honda et al. 2013) appears to be consistent with the pathway for biogenesis in the distal axon (Maday & Holzbaur 2014).”
Result
Mechanisms of selective autophagy and mitophagy: Implications for neurodegenerative diseases
Chu, C. T. (2019) · Neurobiology of Disease · doi:10.1016/j.nbd.2018.07.015 · Cited by 218 · cited 2× · see citing works
“Observations from both experimental models and post-mortem analysis of human tissues suggest that dysfunction of autophagy may be a common contributor to the pathogenic process across these diseases (recently reviewed by (Boland et al. 2018, Chu 2018)).”
Background
The RAB11A-Positive Compartment Is a Primary Platform for Autophagosome Assembly Mediated by WIPI2 Recognition of PI3P-RAB11A
Puri, C., Vicinanza, M., Ashkenazi, A., Gratian, M. J., Zhang, Q., Bento, C. F., Renna, M., Menzies, F. M., & Rubinsztein, D. C. (2018) · Developmental Cell · doi:10.1016/j.devcel.2018.03.008 · Cited by 213 · cited 2× · see citing works
“2009), and recycling endosomes (Puri et al. 2018), has been implicated in autophagy at some point.”
Background
KIF1A/UNC-104 Transports ATG-9 to Regulate Neurodevelopment and Autophagy at Synapses
Stavoe, A. K. H., Kargbo-Hill, S. E., Hall, D. H., & Colón-Ramos, D. A. (2016) · Developmental Cell · doi:10.1016/j.devcel.2016.06.012 · Cited by 211 · see citing works
Self-citation
Cholesterol and ORP1L-mediated ER contact sites control autophagosome transport and fusion with the endocytic pathway
Wijdeven, R., Janssen, H., Nahidiazar, L., Janssen, L., Jalink, K., Berlin, I., & Neefjes, J. (2016) · Nature Communications · doi:10.1038/ncomms11808 · Cited by 209 · cited 1× · see citing works
“Dynein is recruited to autophagosomes by RAB7 and RILP (Cheng et al. 2015, Jordens et al. 2001, Wijdeven et al. 2016).”
Background
The SAC1 domain in synaptojanin is required for autophagosome maturation at presynaptic terminals
Vanhauwaert, R., Kuenen, S., Masius, R., Bademosi, A. T., Manetsberger, J., Schoovaerts, N., Bounti, L., Gontcharenko, S., Swerts, J., Vilain, S., et al. (2017) · EMBO Journal · doi:10.15252/embj.201695773 · Cited by 206 · see citing works
LC3 Binding to the Scaffolding Protein JIP1 Regulates Processive Dynein-Driven Transport of Autophagosomes
Fu, M.-M., Nirschl, J. J., & Holzbaur, E. (2014) · Developmental Cell · doi:10.1016/j.devcel.2014.04.015 · Cited by 202 · see citing works
Self-citation
Regulation of mATG9 trafficking by Src- and ULK1-mediated phosphorylation in basal and starvation-induced autophagy
Zhou, C.-Q., Ma, K., Gao, R., Mu, C.-L., Chen, L.-B., Liu, Q.-Q., Luo, Q., Feng, D., Zhu, Y.-S., & Chen, Q. (2016) · Cell Research · doi:10.1038/cr.2016.146 · Cited by 201 · see citing works
Integrated Transcriptome and Proteome Analyses Reveal Organ-Specific Proteome Deterioration in Old Rats
Ori, A., Toyama, B. H., Harris, M. S., Bock, T., Iskar, M., Bork, P., Ingolia, N. T., Hetzer, M. W., & Beck, M. (2015) · Cell Systems · doi:10.1016/j.cels.2015.08.012 · Cited by 201 · cited 1× · see citing works
“Conversely, transcriptome and proteome analysis in rat brain did not detect significant changes in autophagy pathway components between six months and 24 months (Ori et al. 2015).”
Background
KIF1A/UNC-104 transports ATG-9 to regulate neurodevelopment and autophagy at synapses
Stavoe, A. K. H., Hill, S. E., Hall, D. H., & Colón-Ramos, D. (2016) · bioRxiv · doi:10.1101/057166 · Cited by 199 · cited 8×
“This robust retrograde trafficking of autophagosomes has been confirmed in vivo in C. elegans (Stavoe et al. 2016) and Drosophila (Neisch et al. 2017), where the STRIPAK complex was implicated as a key regulatory factor.”
BackgroundInfluentialSelf-citation
Bassoon Controls Presynaptic Autophagy through Atg5.
Okerlund, N. D., Schneider, K. S., Leal-Ortiz, S. A., Montenegro-Venegas, C., Kim, S., Garner, L. C., Waites, C., Gundelfinger, E., Reimer, R., & Garner, C. (2017) · Neuron · doi:10.1016/j.neuron.2017.01.026 · Cited by 191 · cited 1× · see citing works
“Conversely, transcriptome and proteome analysis in rat brain did not detect significant changes in autophagy pathway components between six months and 24 months (Ori et al. 2015).”
Background
Exit from the Golgi Is Required for the Expansion of the Autophagosomal Phagophore in Yeast Saccharomyces cerevisiae
van der Vaart, A., Griffith, J. M., & Reggiori, F. (2010) · Autophagy · doi:10.1091/mbc.e09-04-0345 · Cited by 191 · cited 1× · see citing works
“…every possible membrane source, including plasma membrane (Hollenbeck 1993; Ravikumar 2010), mitochondria (Hailey et al. 2010), Golgi (van der Vaart et al. 2010), ER (Hamasaki et al. 2013, Hayashi-Nishino et al. 2009, Ylä-Anttila et al. 2009), and recycling endosomes (Puri et al. 2018), has…”
Background
Genome-wide CRISPR screen identifies TMEM41B as a gene required for autophagosome formation
Morita, K., Hama, Y., Izume, T., Tamura, N., Ueno, T., Yamashita, Y., Sakamaki, Y., Mimura, K., Morishita, H., Shihoya, W., et al. (2018) · Journal of Cell Biology · doi:10.1083/jcb.201804132 · Cited by 190 · cited 1× · see citing works
“Several accessory transmembrane proteins have recently been discovered, such as VMP1 and TMEM41B (Moretti et al. 2018, Morita et al. 2018), which primarily localize to the ER.”
Background
GABAA Receptor-Associated Protein Traffics GABAA Receptors to the Plasma Membrane in Neurons
Leil, T., Chen, Z.-W., Chang, C., & Olsen, R. (2004) · Journal of Neuroscience · doi:10.1523/jneurosci.3355-04.2004 · Cited by 190 · cited 1× · see citing works
“GABARAP was then subsequently found to be important for GABAA receptor intracellular trafficking (Leil 2004), but the cellular mechanism of GABARAP regulation of GABAA receptor trafficking remains unclear.”
Background
Distinct roles for motor neuron autophagy early and late in the SOD1 G93A mouse model of ALS
Rudnick, N. D., Griffey, C. J., Guarnieri, P., Gerbino, V., Wang, X., Piersaint, J. A., Tapia, J. C., Rich, M. M., & Maniatis, T. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1704294114 · Cited by 189 · cited 1× · see citing works
“…including autophagosome biogenesis (De Pace et al. 2018, Rui et al. 2015, Stavoe & Holzbaur 2018), cargo-loading (Martinez-Vicente et al. 2010, Rudnick et al. 2017), intracellular transport (Nicolas et al. 2018, Wong & Holzbaur 2014b), and autophagosomelysosome fusion or acidification (Lie &…”
Background
ER-phagy at a glance
Grumati, P., Dikič, I., & Stolz, A. (2018) · Journal of Cell Science · doi:10.1242/jcs.217364 · Cited by 184 · cited 3× · see citing works
“One mechanism for turnover is ERphagy (also referred to as reticulophagy), the selective removal of ER segments by autophagy (Grumati et al. 2018).”
Background
Releasing Syntaphilin Removes Stressed Mitochondria from Axons Independent of Mitophagy under Pathophysiological Conditions
Lin, M.-Y., Cheng, X., Tammineni, P., Xie, Y., Zhou, B., Cai, Q., & Sheng, Z. (2017) · Neuron · doi:10.1016/j.neuron.2017.04.004 · Cited by 184 · cited 1× · see citing works
“Additionally, mitochondrial anchoring protein syntaphilin (SNPH) is released from axonal mitochondria upon stress, allowing their retrograde transport out of the axon (Lin et al. 2017).”
Background
TMEM41B is a novel regulator of autophagy and lipid mobilization
Moretti, F., Bergman, P., Dodgson, S., Marcellin, D., Claerr, I., Goodwin, J. M., deJesus, R., Kang, Z. B., Antczak, C., Begue, D., et al. (2018) · EMBO Reports · doi:10.15252/embr.201845889 · Cited by 161 · cited 3× · see citing works
“Sci 113(24):E3349–58 [PubMed: 27247382] Moretti F, Bergman P, Dodgson S, Marcellin D, Claerr I, et al. 2018 TMEM41B is a novel regulator of autophagy and lipid mobilization.”
Background
Presynaptic Terminals Independently Regulate Synaptic Clustering and Autophagy of GABAAReceptors inCaenorhabditis elegans
Rowland, A. M., Richmond, J. E., Olsen, J. G., Hall, D. H., & Bamber, B. A. (2006) · The Journal of Neuroscience · doi:10.1523/jneurosci.2279-05.2006 · Cited by 159 · cited 1× · see citing works
“These data indicate that autophagy selectively regulates surface expression of GABAA receptors, suggesting that autophagy could modulate neuronal excitation and inhibition (Rowland 2006).”
Background
Atlastins remodel the endoplasmic reticulum for selective autophagy
Liang, J. R., Lingeman, E., Ahmed, S., & Corn, J. E. (2018) · Journal of Cell Biology · doi:10.1083/jcb.201804185 · Cited by 158 · cited 7× · see citing works
“Genetic studies indicate that FAM134B, an ERphagy receptor, is required to maintain neuronal homeostasis, as mutations cause a sensory and autonomic neuropathy known as HSAN-II (Kurth et al. 2009).”
BackgroundInfluential
Metabolic Activity Determines Efficacy of Macroautophagic Clearance of Pathological Oligomeric α-Synuclein
Yu, W. H., Dorado, B., Figueroa, H. Y., Wang, L., Planel, E., Cookson, M. R., Clark, L. N., & Duff, K. E. (2009) · The American Journal of Pathology · doi:10.2353/ajpath.2009.080928 · Cited by 155 · cited 2× · see citing works
“Analogously, knockdown of Beclin1 in M17 human neuroblastoma cells resulted in increased aggregations of α-synuclein oligomers (Yu et al. 2009).”
Background
Phosphatidylinositol-3-Phosphate Clearance Plays a Key Role in Autophagosome Completion
Cebollero, E., van der Vaart, A., Zhao, M.-T., Rieter, E., Klionsky, D., Helms, J., & Reggiori, F. (2012) · Current Biology · doi:10.1016/j.cub.2012.06.029 · Cited by 151 · cited 2× · see citing works
“After autophagosome closure, PI3P is removed from the outer membrane by PI3P phosphatases (Cebollero et al. 2012) and mATG8s are removed from the outer membrane by ATG4 (Kauffman et al.”
Background
Development and Characterization of a New Parkinson's Disease Model Resulting from Impaired Autophagy
Ahmed, I., Liang, Y., Schools, S., Dawson, V. L., Dawson, T. M., & Savitt, J. M. (2012) · The Journal of Neuroscience · doi:10.1523/jneurosci.0209-12.2012 · Cited by 144 · cited 1× · see citing works
“Additionally, conditional knock-out of Atg7 in dopaminergic neurons using the DAT, EN, or TH promoters produced neuron loss, loss of striatal dopamine, accumulation of ubiquitin- and p62-containing inclusions, and accumulation of α-synuclein in vivo (Ahmed et al. 2012, Sato et al. 2018).”
Background
Mice deficient in Epg5 exhibit selective neuronal vulnerability to degeneration
Zhao, H.-Y., Zhao, Y. G., Wang, X., Xu, L.-J., Miao, L., Feng, D., Chen, Q., Kovács, A. L., Fan, D.-S., & Zhang, H. (2013) · Journal of Cell Biology · doi:10.1083/jcb.201211014 · Cited by 139 · cited 2× · see citing works
“…acts downstream from known Atg genes (Lu et al. 2011, Tian et al. 2010), yielded p62 aggregations and ubiquitin-positive inclusions in brain and spinal cord extracts, a reduction of pyramidal and motor neurons, axonal degeneration, and accumulation of TDP43 aggregates in neurons (Zhao et al. 2013).”
Background
Control of Autophagosome Axonal Retrograde Flux by Presynaptic Activity Unveiled Using Botulinum Neurotoxin Type A
Wang, T., Martin, S., Papadopulos, A., Harper, C. B., Mavlyutov, T., Niranjan, D., Glass, N., Cooper-White, J., Sibarita, J., Choquet, D., et al. (2015) · Journal of Neuroscience · doi:10.1523/jneurosci.3757-14.2015 · Cited by 137 · cited 1× · see citing works
“Similarly, in rat primary hippocampal neurons, stimulation with KCl or NMDA induced axonal autophagy (Shehata et al. 2012, Wang et al. 2015).”
Background
p62 -mediated phase separation at the intersection of the ubiquitin-proteasome system and autophagy
Danieli, A., & Martens, S. (2018) · Journal of Cell Science · doi:10.1242/jcs.214304 · Cited by 136 · cited 1× · see citing works
“…leads to accumulation of both p62 and ubiquitinated proteins. p62 appears to sit at a crucial juncture between the ubiquitin proteasome and selective autophagy by detecting the buildup of ubiquitinated substrates (Danieli & Martens 2018), suggesting a key role in regulation of protein turnover.”
Background
Loss of autophagy in dopaminergic neurons causes Lewy pathology and motor dysfunction in aged mice
Sato, S., Uchihara, T., Fukuda, T., Noda, S., Kondo, H., Saiki, S., Komatsu, M., Uchiyama, Y., Tanaka, K., & Hattori, N. (2018) · Scientific Reports · doi:10.1038/s41598-018-21325-w · Cited by 125 · see citing works
blue cheese Mutations Define a Novel, Conserved Gene Involved in Progressive Neural Degeneration
Finley, K., Edeen, P. T., Cumming, R. C., Mardahl-Dumesnil, M., Taylor, B. J., Rodriguez, M. H., Hwang, C., Benedetti, M. G., & McKeown, M. (2003) · Journal of Neuroscience · doi:10.1523/jneurosci.23-04-01254.2003 · Cited by 122 · cited 1× · see citing works
“In vivo studies support a role for ALFY in aggrephagy, as the Drosophila mutant blue cheese demonstrates accumulation of ubiquitin-positive inclusions, neurodegeneration, and shortened lifespan (Finley et al. 2003).”
Background
Absence of the Autophagy Adaptor SQSTM1/p62 Causes Childhood-Onset Neurodegeneration with Ataxia, Dystonia, and Gaze Palsy.
Haack, T., Ignatius, E., Calvo-Garrido, J., Iuso, A., Isohanni, P., Maffezzini, C., Lönnqvist, T., Suomalainen, A., Gorza, M., Kremer, L., et al. (2016) · American Journal of Human Genetics · doi:10.1016/j.ajhg.2016.06.026 · Cited by 121 · cited 1× · see citing works
“Supporting the importance of p62 in neurons, mutations in p62/SQSTM1 are implicated in ALS/FTD (frontotemporal dementia) and ataxia (Fecto et al. 2011, Haack et al. 2016).”
Background
hVps15, but not Ca2+/CaM, is required for the activity and regulation of hVps34 in mammalian cells
Yan, Y., Flinn, R., Wu, H., Schnur, R. S., & Backer, J. (2008) · Biochemical Journal · doi:10.1042/bj20081865 · Cited by 121 · cited 1× · see citing works
“A uthor M anuscript A uthor M anuscript A uthor M anuscript A uthor M anuscript Matsunaga et al. 2009, Yan et al. 2009, Zhong et al. 2009).”
Background
Altered distribution of ATG9A and accumulation of axonal aggregates in neurons from a mouse model of AP-4 deficiency syndrome
Pace, R. D., Skirzewski, M., Damme, M., Mattera, R., Mercurio, J., Foster, A. M., Cuitino, L., Jarnik, M., Hoffmann, V., Morris, H. D., et al. (2018) · PLoS Genetics · doi:10.1371/journal.pgen.1007363 · Cited by 111 · cited 1× · see citing works
“Studies to date have demonstrated aging or disease-associated deficits at multiple points in the pathway, including autophagosome biogenesis (De Pace et al. 2018, Rui et al. 2015, Stavoe & Holzbaur 2018), cargo-loading (Martinez-Vicente et al. 2010, Rudnick et al. 2017), intracellular transport…”
Background
Structural determinants in GABARAP required for the selective binding and recruitment of ALFY to LC3B‐positive structures
Lystad, A. H., Ichimura, Y., Takagi, K., Yang, Y., Pankiv, S., Kanegae, Y., Kageyama, S., Suzuki, M., Saito, I., Mizushima, T., et al. (2014) · EMBO Reports · doi:10.1002/embr.201338003 · Cited by 106 · cited 1× · see citing works
“ALFY (autophagy-linked FYVE protein, also known as WDFY3 for WD repeat and FYVE domain-containing protein) is a large scaffolding molecule that binds to p62, the ATG8 proteins LC3C and the GABARAPs, and ATG5, a component of the core autophagy machinery (Lystad et al. 2014).”
Background
Delipidation of mammalian Atg8-family proteins by each of the four ATG4 proteases
Kauffman, K. J., Yu, S., Jin, J.-X., Mugo, B., Nguyen, N., O'Brien, A., Nag, S., Lystad, A. H., & Melia, T. (2018) · Autophagy · doi:10.1080/15548627.2018.1437341 · Cited by 99 · cited 5× · see citing works
“After autophagosome closure, PI3P is removed from the outer membrane by PI3P phosphatases (Cebollero et al. 2012) and mATG8s are removed from the outer membrane by ATG4 (Kauffman et al. 2018, Nair et al. 2012, Yu et al. 2012), possibly destabilizing the association of other autophagy components with the cytosolic face…”
BackgroundInfluential
Neuronal inhibition of the autophagy nucleation complex extends life span in post-reproductive C. elegansPreprint
Wilhelm, T., Byrne, J., Medina, R., Kolundžić, E., Geisinger, J., Hajdůšková, M., Tursun, B., & Richly, H. (2017) · Genes & Development · doi:10.1101/gad.301648.117 · Cited by 98 · see citing works
The Endolysosomal System and Proteostasis: From Development to Degeneration
Winckler, B., Faundez, V., Maday, S., Cai, Q., Almeida, C. G., & Zhang, H.-Y. (2018) · Journal of Neuroscience · doi:10.1523/jneurosci.1665-18.2018 · Cited by 96 · see citing works
Rapidly transported organelles containing membrane and cytoskeletal components: their relation to axonal growth
Hollenbeck, P., & Bray, D. (1987) · Journal of Cell Biology · doi:10.1083/jcb.105.6.2827 · Cited by 95 · cited 1× · see citing works
“In the converse experiment in chick embryonic DRG neurons, when axon outgrowth was blocked with cytochalasin-E, retrograde transport of axonal autophagosomes increased threefold (Hollenbeck & Bray 1987).”
Background
Autophagy linked FYVE (Alfy/WDFY3) is required for establishing neuronal connectivity in the mammalian brain
Dragich, J., Kuwajima, T., Hirose-Ikeda, M., Yoon, M., Eenjes, E., Bosco, J. R., Fox, L., Lystad, A. H., Oo, T., Yarygina, O., et al. (2016) · eLife · doi:10.7554/elife.14810 · Cited by 93 · cited 1× · see citing works
“Baseline defects in autophagy were not observed, but an exogenous aggregation-prone substrate accumulated more rapidly in Alfy knockout MEFs (Dragich et al. 2016).”
Background
Autophagy Negatively Regulates Early Axon Growth in Cortical Neurons
Ban, B.-K., Jun, M.-H., Ryu, H.-H., Jang, D.-J., Ahmad, S. T., & Lee, J.-A. (2013) · Molecular and Cellular Biology · doi:10.1128/mcb.00627-13 · Cited by 92 · see citing works
Homozygosity mapping and targeted genomic sequencing reveal the gene responsible for cerebellar hypoplasia and quadrupedal locomotion in a consanguineous kindred.Preprint
Gulsuner, S., Tekinay, A. B., Doerschner, K., Boyaci, H., Bilguvar, K., Unal, H., Ors, A., Onat, O., Atalar, E., Başak, A., et al. (2011) · Genome Research · doi:10.1101/gr.126110.111 · Cited by 89 · cited 1× · see citing works
“In humans, a missense mutation in WDR81 is associated with the rare neurodevelopmental condition known as CAMRQ for cerebellar ataxia, mental retardation, and disequilibrium syndrome (Gulsuner et al. 2011).”
Background
A STRIPAK complex mediates axonal transport of autophagosomes and dense core vesicles through PP2A regulation
Neisch, A. L., Neufeld, T. P., & Hays, T. (2017) · Journal of Cell Biology · doi:10.1083/jcb.201606082 · Cited by 87 · cited 3× · see citing works
“In Drosophila, autophagosome biogenesis also occurred at the neuromuscular junction (NMJ) in the distal axon of motor neurons (Neisch et al. 2017, Soukup et al. 2016).”
Background
Dynein- and activity-dependent retrograde transport of autophagosomes in neuronal axons
Katsumata, K., Nishiyama, J., Inoue, T., Mizushima, N., Takeda, J., & Yuzaki, M. (2010) · Autophagy · doi:10.4161/auto.6.3.11262 · Cited by 84 · cited 1× · see citing works
“Although the number of autophagosomes increased in the axon, NMDA treatment did not appear to affect retrograde transport of autophagosomes (Katsumata et al. 2010).”
Background
Expression of WIPI2B counteracts age-related decline in autophagosome biogenesis in neurons
Stavoe, A. K., Gopal, P. P., Gubas, A., Tooze, S. A., & Holzbaur, E. L. (2019) · eLife · doi:10.7554/elife.44219 · Cited by 82 · see citing works
Self-citation
The Organization of Mitochondrial Quality Control and Life Cycle in the Nervous System In Vivo in the Absence of PINK1
Devireddy, S., Liu, A., Lampe, T., & Hollenbeck, P. (2015) · Journal of Neuroscience · doi:10.1523/jneurosci.1198-15.2015 · Cited by 79 · cited 2× · see citing works
“For example, non-selective axonal autophagy is differentially regulated than the selective removal of damaged mitochondria from the soma (Cornelissen et al. 2018, Devireddy et al. 2015, McWilliams et al. 2016, Sung et al. 2016).”
Background
Mutations in the SPG3A gene encoding the GTPase atlastin interfere with vesicle trafficking in the ER/Golgi interface and Golgi morphogenesis.
Namekawa, M., Muriel, M., Janer, A., Latouche, M., Dauphin, A., Debeir, T., Martin, E., Duyckaerts, C., Prigent, A., Depienne, C., et al. (2007) · Molecular and cellular neurosciences · doi:10.1016/j.mcn.2007.01.012 · Cited by 79 · cited 1× · see citing works
“Of note, a loss-of-function mutation in the Atlastin ATL1 is causal for SPG3A, a hereditary spastic paraplegia (Namekawa et al. 2007).”
Background
Faculty of 1000 evaluation for Cytosolic proteostasis through importing of misfolded proteins into mitochondria.
Jackson, S. (2017) · doi:10.3410/f.727347900.793530068 · Cited by 78 · cited 1×
“Recently identified pathways may also contribute to the clearance of misfolded or aggregated proteins in neurons, such as the MAGIC (mitochondria as guardian in cytosol) pathway involving import of misfolded proteins into mitochondria (Ruan et al. 2017).”
Background
Compartmentalized Regulation of Parkin-Mediated Mitochondrial Quality Control in the Drosophila Nervous System In Vivo
Sung, H., Tandarich, L. C., Nguyen, K., & Hollenbeck, P. (2016) · Journal of Neuroscience · doi:10.1523/jneurosci.0633-16.2016 · Cited by 78 · cited 2× · see citing works
“For example, non-selective axonal autophagy is differentially regulated than the selective removal of damaged mitochondria from the soma (Cornelissen et al. 2018, Devireddy et al. 2015, McWilliams et al. 2016, Sung et al. 2016).”
Background
Unc-51 Controls Active Zone Density and Protein Composition by Downregulating ERK Signaling
Wairkar, Y. P., Toda, H., Mochizuki, H., Furukubo-Tokunaga, K., Tomoda, T., & DiAntonio, A. (2009) · The Journal of Neuroscience · doi:10.1523/jneurosci.3848-08.2009 · Cited by 73 · cited 1× · see citing works
“As in worms, these defects in autophagy mutants were due to incorrect synaptic formation, not precocious degeneration or synaptic retraction (Wairkar et al. 2009).”
Background
Arf6 and the 5’phosphatase of Synaptojanin 1 regulate autophagy in cone photoreceptors
George, A. A., Hayden, S., Stanton, G. R., & Brockerhoff, S. E. (2016) · Bioessays · doi:10.1002/bies.201670913 · Cited by 73 · cited 1× · see citing works
“Similarly, in the Zebrafish photoreceptor, synaptojanin, a lipid phosphatase and EndophilinA interactor, is necessary for autophagy (George et al. 2016).”
Background
The BEACH-containing protein WDR81 coordinates p62 and LC3C to promote aggrephagy
Liu, X.-Z., Li, Y., Wang, X., Xing, R., Liu, K., Gan, Q.-W., Tang, C., Gao, Z.-Y., Jian, Y., Luo, S.-Q., et al. (2017) · Journal of Cell Biology · doi:10.1083/jcb.201608039 · Cited by 70 · cited 2× · see citing works
“WDR81 (WD repeat domain 81) can bind directly to LC3, but also interacts with p62, and has been proposed to facilitate the ability of p62 to bind to aggregated and ubiqutinated proteins (Liu et al. 2017).”
Background
MTOR controls genesis and autophagy of GABAergic interneurons during brain development
Ka, M., Smith, A. L., & Kim, W.-Y. (2017) · Autophagy · doi:10.1080/15548627.2017.1327927 · Cited by 65 · cited 1× · see citing works
“Conditionally knocking out mTOR in GABAergic precursors increased autophagy in those cells and suppressed their proliferation, leading to a reduction in cortical interneurons (Ka et al. 2017).”
Background
C-Terminal Modification Is Required for GABARAP-Mediated GABAA Receptor Trafficking
Chen, Z.-W., Chang, C., Leil, T., & Olsen, R. (2007) · Journal of Neuroscience · doi:10.1523/jneurosci.0919-07.2007 · Cited by 59 · cited 1× · see citing works
“In PC12 cells, primary hippocampal neurons, and Xenopus oocytes, GABARAP lipidation was required for increased surface expression of GABAA receptors (Chen et al. 2007).”
Background
Induction of autophagy by TOCP in differentiated human neuroblastoma cells lead to degradation of cytoskeletal components and inhibition of neurite outgrowth.
Chen, J.-X., Sun, Y.-J., Wang, P., Long, D.-X., Li, W., Li, L., & Wu, Y.-J. (2013) · Toxicology · doi:10.1016/j.tox.2013.05.012 · Cited by 57 · cited 1× · see citing works
“In SH-SY5Y cells, an in vitro cell line model of neurons, induction of autophagy with Tri-ortho-cresyl phosphate (TOCP) also inhibited neurite outgrowth (Chen et al. 2013).”
Method
WDR81 Is Necessary for Purkinje and Photoreceptor Cell Survival
Traka, M., Millen, K., Collins, D., Elbaz, B., Kidd, G., Gomez, C. M., & Popko, B. (2013) · Journal of Neuroscience · doi:10.1523/jneurosci.2394-12.2013 · Cited by 37 · cited 1× · see citing works
“Similarly, mice carrying a homozygous missense mutation in WDR81 exhibited Purkinje cell and photoreceptor cell death (Traka et al. 2013).”
Background
Basal autophagy is required for promoting dendritic terminal branching in Drosophila sensory neurons
Clark, S. G., Graybeal, L. L., Bhattacharjee, S., Thomas, C., Bhattacharya, S., & Cox, D. (2018) · PLoS ONE · doi:10.1371/journal.pone.0206743 · Cited by 35 · cited 1× · see citing works
“In Drosophila, knockdown of autophagy genes reduced dendritic arbor growth and terminal branching in multidendritic sensory neurons in vivo (Clark et al. 2018).”
Background
Autophagy in childhood neurological disorders
Zhu, Y., Runwal, G., Obrocki, P., & Rubinsztein, D. (2018) · Developmental Medicine & Child Neurology · doi:10.1111/dmcn.14092 · Cited by 11 · cited 2× · see citing works
“This hypothesis is further supported by the observation that mutations in many of the proteins involved in autophagy are sufficient to cause neurodevelopmental or neurodegenerative disease, including PINK1, Parkin, OPTN, TBK1, ATL1, SQSTM1, and WDR81 as discussed above, as well as ATG5, AP4, HTT, WIPI4, and DYNC1H1 (r…”
Background

Flagged first, then by citations

2 of the 157 references couldn’t be matched to a known paper.

Research works printed but not linked: 10

Chano T, Okabe H, Hulette CM. 2007 RB1CC1 insufficiency causes neuronal atrophy through mTOR signaling alteration and involved in the pathology of Alzheimer’s diseases. Brain Res. 1168: 97– 105 17706618
Fecto F, Yan J, Vemula SP, Liu E, Yang Y, 2011 SQSTM1 mutations in familial and sporadic amyotrophic lateral sclerosis. Arch. Neurol 68(11): 1440– 46 22084127
Haidar M, Asselbergh B, Adriaenssens E, De Winter V, Timmermans J-P, 2019 Neuropathy-causing mutations in HSPB1 impair autophagy by disturbing the formation of p62/SQSTM1 bodies. Autophagy. 00(00): 1– 18 PMC6526868 30669930
Hamasaki M, Furuta N, Matsuda A, Nezu A, Yamamoto A, 2013 Autophagosomes form at ER-mitochondria contact sites. Nature. 495(7441): 389– 93 23455425
Lu Q, Yang P, Huang X, Hu W, Guo B, 2011 The WD40 Repeat PtdIns(3)P-Binding Protein EPG-6 Regulates Progression of Omegasomes to Autophagosomes. Dev. Cell 21(2): 343– 57 21802374
Rowland AM. 2006 Presynaptic Terminals Independently Regulate Synaptic Clustering and Autophagy of GABAA Receptors in Caenorhabditis elegans. J. Neurosci 26(6): 1711– 20 16467519 PMC6793639
Ruan L, Zhou C, Jin E, Kucharavy A, Zhang Y, 2017 Cytosolic proteostasis through importing of misfolded proteins into mitochondria. Nature. 543(7645): 443– 46 28241148 PMC5793917
Sliter DA, Martinez J, Hao L, Chen X, Sun N, 2018 Parkin and PINK1 mitigate STING-induced inflammation. Nature. 561(7722): 258– 62 30135585 PMC7362342
Smith MD, Harley ME, Kemp AJ, Wills J, Lee M, 2018 CCPG1 Is a Non-canonical Autophagy CargoReceptor Essential for ER-Phagyand Pancreatic ER Proteostasis. Dev. Cell 44(2): 217– 32 29290589 PMC5791736
Tekirdag K, Cuervo AM. 2018 Chaperone-mediated autophagy and endosomal microautophagy: Joint by a chaperone. J. Biol. Chem 293(15): 5414– 24 29247007 PMC5900761

Sorted by citations

The different autophagy degradation pathways and neurodegeneration
Fleming, A., Bourdenx, M., Fujimaki, M., Karabiyik, C., Krause, G. J., Lopez, A., Martín‐Segura, A., Puri, C., Scrivo, A., Skidmore, J., et al. (2022) · Neuron · doi:10.1016/j.neuron.2022.01.017 · Cited by 499 · see citing works
Interactions between reactive oxygen species and autophagy special issue: Death mechanisms in cellular homeostasis.
Redza-Dutordoir, M., & Averill-Bates, D. (2021) · Biochimica et biophysica acta. Molecular cell research · doi:10.1016/j.bbamcr.2021.119041 · Cited by 194 · see citing works
Toxic Effects of Glyphosate on the Nervous System: A Systematic Review
Costas-Ferreira, C., Durán, R., & Faro, L. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23094605 · Cited by 185 · see citing works
Neuronal Autophagy Regulates Presynaptic Neurotransmission by Controlling the Axonal Endoplasmic Reticulum
Kuijpers, M., Kochlamazashvili, G., Stumpf, A., Puchkov, D., Swaminathan, A., Lucht, M. T., Krause, E., Maritzen, T., Schmitz, D., & Haucke, V. (2021) · Neuron · doi:10.1016/j.neuron.2020.10.005 · Cited by 170 · see citing works
Mutant HTT (huntingtin) impairs mitophagy in a cellular model of Huntington disease
Franco-Iborra, S., Plaza-Zabala, A., Montpeyo, M., Sebastián, D., Vila, M., & Martínez-Vicente, M. (2020) · Autophagy · doi:10.1080/15548627.2020.1728096 · Cited by 172 · see citing works
Neuronal Autophagy Regulates Presynaptic Neurotransmission by Controlling the Axonal Endoplasmic ReticulumPreprint
Kuijpers, M., Kochlamazashvili, G., Stumpf, A., Puchkov, D., Swaminathan, A., Lucht, M. T., Krause, E., Maritzen, T., Schmitz, D., & Haucke, V. (2020) · bioRxiv · doi:10.1101/2020.07.06.189522 · Cited by 167 · see citing works
Increased LRRK2 kinase activity alters neuronal autophagy by disrupting the axonal transport of autophagosomes
Boecker, C., Goldsmith, J., Dou, D., Cajka, G. G., & Holzbaur, E. (2021) · Current Biology · doi:10.1016/j.cub.2021.02.061 · Cited by 153 · see citing works
“In particular, axonal transport of autophagic vesicles (AVs) in neurons is tightly regulated and vital to neuronal homeostasis.(20,21) AVs are preferentially formed at the distal tip of the axon and then transported retrogradely toward the cell soma, maturing en route by fusion with late endosomes/lysosomes.”
Self-citation
Cellular rejuvenation: molecular mechanisms and potential therapeutic interventions for diseases
Ji, S., Xiong, M., Chen, H., Liu, Y., Zhou, L., Hong, Y., Wang, M., Wang, C., Fu, X., & Sun, X. (2023) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-023-01343-5 · Cited by 170 · see citing works
“The activity of autophagy and the autophagy gene transcription by specific transcription factors, epigenetic changes, and microRNAs have emerged as crucially conserved pathways for promoting lifespan.(238) In autophagy pathways, multiple points with age including autophagosome biogenesis, cargo loading, intracellular…”
Background
Piezoelectric Scaffolds as Smart Materials for Neural Tissue Engineering
Zaszczyńska, A., Sajkiewicz, P., & Gradys, A. (2020) · Polymers · doi:10.3390/polym12010161 · Cited by 140 · see citing works
“The basic functional units in the nervous system having specific electrical properties are neurons and neuroglia (Figure 3), which enable effective transmission of the signals [63,64].”
Background
Macroautophagy in CNS health and disease
Griffey, C. J., & Yamamoto, A. (2022) · Nature Reviews Neuroscience · doi:10.1038/s41583-022-00588-3 · Cited by 120 · see citing works
The Multiple Roles of Autophagy in Neural Function and Diseases
Li, Y., Qin, Z., & Sheng, R. (2023) · Neuroscience Bulletin · doi:10.1007/s12264-023-01120-y · Cited by 108 · see citing works
“Autophagy in neurons includes constitutive and stress-induced autophagy, which are involved in the renewal of damaged or aging endoplasmic reticulum, mitochondria, other organelles, and aggregate proteins [81, 82].”
Background
Presynaptic autophagy is coupled to the synaptic vesicle cycle via ATG-9
Yang, S., Park, D., Manning, L., Hill, S. E., Cao, M., Xuan, Z., Gonzalez, I., Dong, Y.-M., Clark, B., Shao, L., et al. (2020) · bioRxiv · doi:10.1016/j.neuron.2021.12.031 · Cited by 99 · see citing works
“Neurons are particularly vulnerable to dysfunctional organelles and damaged proteins due to their post-mitotic nature, polarized morphology, and high metabolic activity states during neuronal stimulation (Son et al., 2012; Stavoe and Holzbaur, 2019; Menzies et al., 2017).”
Autophagy in Neuronal Development and Plasticity
Fleming, A., & Rubinsztein, D. C. (2020) · Trends in Neurosciences · doi:10.1016/j.tins.2020.07.003 · Cited by 93 · see citing works
Targeting Brain Renin-Angiotensin System for the prevention and treatment of Alzheimer's disease: past, present and future.
Gouveia, F., Camins, A., Ettcheto, M., Bicker, J., Falcão, A., Cruz, M., & Fortuna, A. (2022) · Ageing Research Reviews · doi:10.1016/j.arr.2022.101612 · Cited by 90 · see citing works
Enhancing autophagy in Alzheimer's disease through drug repositioning
Eshraghi, M., Ahmadi, M., Afshar, S., Lorzadeh, S., Adlimoghaddam, A., Rezvani Jalal, N., West, R., Dastghaib, S., Igder, S., Torshizi, S. R. N., et al. (2022) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2022.108171 · Cited by 89 · see citing works
Deubiquitinating enzymes (DUBs): decipher underlying basis of neurodegenerative diseases
Liu, B.-H., Ruan, J., Chen, M., Li, Z.-D., Manjengwa, G. M., Schlüter, D., Song, W., & Wang, X. (2021) · Molecular Psychiatry · doi:10.1038/s41380-021-01233-8 · Cited by 87 · see citing works
Ubiquitin signaling in neurodegenerative diseases: an autophagy and proteasome perspective
Guerroué, F. L., & Youle, R. (2020) · Cell Death and Differentiation · doi:10.1038/s41418-020-00667-x · Cited by 85 · see citing works
“When formed in the axon, acidified vesicles are subsequently retrogradely transported toward the soma [15].”
Background
Mitochondrial Dysfunction in Neurodegenerative Diseases: Mechanisms and Corresponding Therapeutic Strategies
Meng, K., Jia, H., Hou, X., Zhu, Z., Lu, Y., Feng, Y., Feng, J., Xia, Y., Tan, R., Cui, F., et al. (2025) · Biomedicines · doi:10.3390/biomedicines13020327 · Cited by 82 · see citing works
“Mitophagy defects can lead to impaired mitochondrial function and reduced ATP production, thereby affecting cell energy metabolism and normal function and participating in the development of ND [27].”
The Journey of the Synaptic Autophagosome: A Cell Biological Perspective
Kargbo-Hill, S. E., & Colón-Ramos, D. A. (2020) · Neuron · doi:10.1016/j.neuron.2020.01.018 · Cited by 72 · see citing works
The NRF2-Dependent Transcriptional Regulation of Antioxidant Defense Pathways: Relevance for Cell Type-Specific Vulnerability to Neurodegeneration and Therapeutic Intervention
Boas, S., Joyce, K. L., & Cowell, R. (2021) · Antioxidants · doi:10.3390/antiox11010008 · Cited by 64 · see citing works
The Role of PGC-1α-Mediated Mitochondrial Biogenesis in Neurons
Chen, M., Yan, R.-Y., Luo, J.-S., Ning, J.-Q., Zhou, R., & Ding, L.-L. (2023) · Neurochemical Research · doi:10.1007/s11064-023-03934-8 · Cited by 60 · see citing works
Structural basis for membrane recruitment of ATG16L1 by WIPI2 in autophagy
Strong, L. M., Chang, C.-M., Riley, J. F., Boecker, C. A., Flower, T., Buffalo, C., Ren, X.-F., Stavoe, A. K. H., Holzbaur, E., & Hurley, J. (2021) · bioRxiv · doi:10.1101/2021.05.14.444175 · Cited by 57
Self-citation
The contribution of altered neuronal autophagy to neurodegeneration
Filippone, A., Esposito, E., Mannino, D., Lyssenko, N., & Praticò, D. (2022) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2022.108178 · Cited by 55 · see citing works
The contribution of altered neuronal autophagy to neurodegeneration
Filippone, A., Esposito, E., Mannino, D., Lyssenko, N., & Praticò, D. (2022) · Pharmacology and Therapeutics · doi:10.2139/ssrn.4035507 · Cited by 54
Autophagy in Multiple Sclerosis: Two Sides of the Same Coin
Misrielal, C., Mauthe, M., Reggiori, F., & Eggen, B. (2020) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2020.603710 · Cited by 54 · see citing works
“It is known that basal autophagy in neurons is essential for protein quality control, pruning, development, and neuronal survival (Hara et al., 2006; Komatsu et al., 2006; Wong and Cuervo, 2010; Feng et al., 2017; Plaza-Zabala et al., 2017; Stavoe and Holzbaur, 2019).”
BackgroundInfluential
Interaction between autophagy and the NLRP3 inflammasome in Alzheimer’s and Parkinson’s disease
Lu, R., Zhang, L., & Yang, X. (2022) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2022.1018848 · Cited by 58 · see citing works
“Unlike other cells, neurons are non-regenerating and irreplaceable and must regulate autophagy to maintain cell survival (Muller et al., 2017; Stavoe and Holzbaur, 2019).”
Background
Aging membranes: unexplored functions for lipids in the lifespan of the central nervous system
Skowronska-Krawczyk, D., & Budin, I. (2019) · Experimental Gerontology · doi:10.1016/j.exger.2019.110817 · Cited by 52 · see citing works
Resveratrol Attenuates Chronic Unpredictable Mild Stress-Induced Alterations in the SIRT1/PGC1α/SIRT3 Pathway and Associated Mitochondrial Dysfunction in Mice
Tabassum, S., Misrani, A., Huang, H., Zhang, Z.-Y., Li, Q.-W., & Long, C. (2023) · Molecular Neurobiology · doi:10.1007/s12035-023-03395-8 · Cited by 51 · see citing works
The Complex Mechanisms by Which Neurons Die Following DNA Damage in Neurodegenerative Diseases
Shadfar, S., Brocardo, M. G., & Atkin, J. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23052484 · Cited by 50 · see citing works
“The specific ablation of autophagy in neurons leads to neurodegeneration, demonstrating the existence of a specific relationship between autophagy and neuronal viability [88].”
Background
New insights into the role of autophagy in retinal and eye diseases.
Villarejo-Zori, B., Jiménez-Loygorri, J. I., Zapata-Muñoz, J., Bell, K., & Boya, P. (2021) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2021.101038 · Cited by 50 · see citing works
Peroxisomal Dysfunction in Neurological Diseases and Brain Aging
Uzor, N.-E., McCullough, L., & Tsvetkov, A. S. (2020) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2020.00044 · Cited by 49 · see citing works
Axonal transport of autophagosomes is regulated by dynein activators JIP3/JIP4 and ARF/RAB GTPasesPreprint
Cason, S. E., & Holzbaur, E. (2023) · bioRxiv · doi:10.1101/2023.01.28.526044 · Cited by 47 · see citing works
“Autophagy is a process by which 20 these components can be broken down and recycled (Stavoe and Holzbaur, 2019).”
BackgroundSelf-citation
Autophagy-dependent filopodial kinetics restrict synaptic partner choice during Drosophila brain wiring
Kiral, F. R., Linneweber, G., Mathejczyk, T., Georgiev, S. V., Wernet, M. F., Hassan, B. A., von Kleist, M., & Hiesinger, P. (2019) · Nature Communications · doi:10.1038/s41467-020-14781-4 · Cited by 44 · see citing works
Regulation of α-synuclein homeostasis and inflammasome activation by microglial autophagy
Choi, I., Heaton, G. R., Lee, Y.-K., & Yue, Z. (2022) · Science Advances · doi:10.1126/sciadv.abn1298 · Cited by 43 · see citing works
Absence of Sac2/INPP5F enhances the phenotype of a Parkinson’s disease mutation of synaptojanin 1
Cao, M., Park, D., Wu, Y.-M., & Camilli, P. D. (2020) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.2004335117 · Cited by 43 · see citing works
Neuronal autophagy in the control of synapse function.
Karpova, A., Hiesinger, P., Kuijpers, M., Albrecht, A., Kirstein, J., Andres‐Alonso, M., Biermeier, A., Eickholt, B., Mikhaylova, M., Maglione, M., et al. (2025) · Neuron · doi:10.1016/j.neuron.2025.01.019 · Cited by 42 · see citing works
Aggrephagy at a glance.
Bauer, B., Martens, S., & Ferrari, L. (2023) · Journal of Cell Science · doi:10.1242/jcs.260888 · Cited by 42 · see citing works
From Metabolic Syndrome to Neurological Diseases: Role of Autophagy
Maiuolo, J., Gliozzi, M., Musolino, V., Carresi, C., Scarano, F., Nucera, S., Scicchitano, M., Bosco, F., Ruga, S., Zito, M. C., et al. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.651021 · Cited by 42 · see citing works
“For this reason, autophagy can perform this function in each neuronal compartment (Stavoe and Holzbaur, 2019).”
Background
Bidirectional Regulation of Neuronal Autophagy in Ischemic Stroke: Mechanisms and Therapeutic Potential.
Wu, Y.-G., Li, Z., Ding, T., Yang, Y.-Q., Wei, C.-M., Zhang, S.-S., & Fan, X. (2025) · Ageing Research Reviews · doi:10.1016/j.arr.2025.102842 · Cited by 41 · see citing works
NAD depletion mediates cytotoxicity in human neurons with autophagy deficiency
Sun, C., Seranova, E., Cohen, M. A., Chipara, M., Roberts, J., Astuti, D., Palhegyi, A., Acharjee, A., Sedlackova, L., Kataura, T., et al. (2023) · Cell Reports · doi:10.1016/j.celrep.2023.112372 · Cited by 41 · see citing works
The emerging role of autophagy and mitophagy in tauopathies: From pathogenesis to translational implications in Alzheimer’s disease
Liu, X., Ye, M., & Ma, L. (2022) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2022.1022821 · Cited by 51 · see citing works
“In neurons, autophagy is essential for the maintenance of cellular homeostasis and participates in multiple neuron-specific functions, such as axon guidance, synaptic transmission, proper neuronal connectivity, and neural stem cell development (Menzies et al., 2017; Stavoe and Holzbaur, 2019).”
Background
Autophagy-Lysosomal Pathway as Potential Therapeutic Target in Parkinson’s Disease
Bonam, S. R., Tranchant, C., & Muller, S. (2021) · Cells · doi:10.3390/cells10123547 · Cited by 41 · see citing works
Drp1-mediated mitochondrial fission contributes to mitophagy in paraquat-induced neuronal cell damage.
Chen, N.-Z., Guo, Z.-K., Luo, Z.-S., Zheng, F.-L., Shao, W.-Y., Yu, G.-X., Cai, P., Wu, S.-Y., & Li, H.-Y. (2020) · Environmental Pollution · doi:10.1016/j.envpol.2020.116413 · Cited by 41 · see citing works
Cylindromatosis Drives Synapse Pruning and Weakening by Promoting Macroautophagy through Akt-mTOR Signaling
Zajicek, A. S., Ruan, H., Dai, H., Skolfield, M. C., Phillips, H., Burnette, W. J., Javidfar, B., Sun, S.-C., Akbarian, S., & Yao, W.-D. (2021) · bioRxiv · doi:10.1038/s41380-022-01571-1 · Cited by 40 · see citing works
“Indeed, autophagy plays essential roles in neuron viability and development [23, 24] and is implicated in numerous neurodegenerative and psychiatric diseases [25-29].”
Background
The needs of a synapse—How local organelles serve synaptic proteostasis
Grochowska, K. M., Andres‐Alonso, M., Karpova, A., & Kreutz, M. R. (2022) · The EMBO Journal · doi:10.15252/embj.2021110057 · Cited by 38 · see citing works
E3 Ubiquitin Ligases in Neurological Diseases: Focus on Gigaxonin and Autophagy
Lescouzères, L., & Bomont, P. (2020) · Frontiers in Physiology · doi:10.3389/fphys.2020.01022 · Cited by 38 · see citing works
“Still, autophagosome biogenesis has also been evidenced in the soma (Maday and Holzbaur, 2016; Stavoe and Holzbaur, 2019) and GAN might constitute a powerful biological system to study its process and function.”
Background
Mitophagy in neurodegenerative disease pathogenesis
Yang, K., Yan, Y., Yu, A., Zhang, R., Zhang, Y., Qiu, Z., Li, Z., Zhang, Q., Wu, S., & Li, F. (2023) · Neural Regeneration Research · doi:10.4103/1673-5374.385281 · Cited by 44 · see citing works
“Depending on the cargo type, selective autophagy pathways include ERphagy, aggrephagy, and mitophagy (Stavoe and Holzbaur, 2019), among which mitophagy is the most familiar pathway (Chu, 2019; Garcia-Macia et al., 2019).”
Background
Autophagy regulates inflammation in intracerebral hemorrhage: Enemy or friend?
Fu, K.-Y., Xu, W., Lenahan, C., Mo, Y., Wen, J., Deng, T., Huang, Q.-R., Guo, F.-Z., Mo, L.-G., & Yan, J. (2023) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2022.1036313 · Cited by 37 · see citing works
“Under physiological conditions, autophagy in the neuron is maintained at a low level, but when stimulated, autophagy is enhanced (Stavoe and Holzbaur, 2019).”
BackgroundInfluential
Mitophagy in Neurons: Mechanisms Regulating Mitochondrial Turnover and Neuronal Homeostasis
Basak, B., & Holzbaur, E. L. F. (2025) · Journal of Molecular Biology · doi:10.1016/j.jmb.2025.169161 · Cited by 44 · see citing works
Self-citation
Molecular Mechanism and Regulation of Autophagy and Its Potential Role in Epilepsy
Zhu, H.-X., Wang, W., & Li, Y. (2022) · Cells · doi:10.3390/cells11172621 · Cited by 35 · see citing works
Renal denervation improves vascular endothelial dysfunction by inducing autophagy via AMPK/mTOR signaling activation in a rat model of type 2 diabetes mellitus with insulin resistance
Wang, Y., Rijal, B., Xu, M., Li, Z., An, Y., Zhang, F., & Lu, C. (2020) · Acta Diabetologica · doi:10.1007/s00592-020-01532-6 · Cited by 37 · see citing works
Role of mitophagy in the neurodegenerative diseases and its pharmacological advances: A review
Wang, Q., Xue, H., Yue, Y., Hao, S., Huang, S., & Zhang, Z. (2022) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2022.1014251 · Cited by 38 · see citing works
“Besides, the strict control of mitochondrial size, number, and distribution is crucial for neurons (Millecamps and Julien, 2013; Schönfeld and Reiser, 2013; Stavoe and Holzbaur, 2019).”
Background
Autophagy in Spinocerebellar ataxia type 2, a dysregulated pathway, and a target for therapy
Marcelo, A., Afonso, I. T., Afonso-Reis, R., Brito, D. V. C., Costa, R. G., Rosa, A., Alves-Cruzeiro, J., Ferreira, B., Henriques, C., Nobre, R., et al. (2021) · Cell Death and Disease · doi:10.1038/s41419-021-04404-1 · Cited by 34 · see citing works
Pharmacological c-Jun NH2-Terminal Kinase (JNK) Pathway Inhibition Reduces Severity of Spinal Muscular Atrophy Disease in Mice
Schellino, R., Boido, M., Borsello, T., & Vercelli, A. (2018) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2018.00308 · Cited by 34 · see citing works
“Moreover, the in vitro inactivation of the JNK3 is able to reduce the degeneration of SMN-deficient neurons and to provide neuroprotection (Yamasaki et al., 2012; Genabai et al., 2015).”
Background
Role of Mitochondria–ER Contact Sites in Mitophagy
Rühmkorf, A., & Harbauer, A. (2023) · Biomolecules · doi:10.3390/biom13081198 · Cited by 32 · see citing works
“Alternatively, the local fusion of mitophagosomes with axonal lysosomes has been observed [51], but the exact site of neuronal autophagosome–lysosome fusion is still a matter of discussion [52].”
Background
Role of the Endoplasmic Reticulum in Synaptic Transmission
Chanaday, N. L., & Kavalali, E. (2022) · Current Opinion in Neurobiology · doi:10.1016/j.conb.2022.102538 · Cited by 32 · see citing works
REST/NRSF deficiency impairs autophagy and leads to cellular senescence in neurons
Rocchi, A., Carminati, E., Fusco, A. D., Kowalska, J. A., Floß, T., & Benfenati, F. (2021) · Aging Cell · doi:10.1111/acel.13471 · Cited by 42 · see citing works
The axonal endolysosomal and autophagic systems
Kuijpers, M., Tehran, D. A., Haucke, V., & Soykan, T. (2020) · Journal of Neurochemistry · doi:10.1111/jnc.15287 · Cited by 32 · see citing works
“…recruitment of downstream components such as Atg5, a core component of the Atg12-Atg5:Atg16L ligase complex that conjugates LC3- and LC3-related proteins to phosphatidylethanolamine to promote phagophore elongation and autophagosome assembly (Maday & Holzbaur, 2014; Stavoe & Holzbaur, 2019).”
Background
Combinatorial selective ER-phagy remodels the ER during neurogenesis
Hoyer, M. J., Smith, I. R., Paoli, J. C., Jiang, Y.-Z., Paulo, J. A., & Harper, J. W. (2023) · bioRxiv · doi:10.1101/2023.06.26.546565 · Cited by 31
Common Principles and Specific Mechanisms of Mitophagy from Yeast to Humans
Kumar, R., & Reichert, A. S. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22094363 · Cited by 33 · see citing works
“p62 (SQSTM1), the best-characterized and the first identified autophagy cargo receptor, has both a ubiquitin-associated (UBA) domain to interact with ubiquitinated protein substrates and an LIR motif for binding to LC3/GABARAP-positive autophagosomes [89].”
Background
The HERC proteins and the nervous system.
Pérez-Villegas, E. M., Ruiz, R., Bachiller, S., Ventura, F., Armengol, J., & Rosa, J. L. (2021) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2021.11.017 · Cited by 30 · see citing works
Heavy metal-induced disruption of the autophagy-lysosomal pathway: implications for aging and neurodegenerative disorders
Das, S., Murumulla, L., Ghosh, P., & Challa, S. (2025) · Biometals · doi:10.1007/s10534-025-00665-x · Cited by 29 · see citing works
“Since neurons are long-lived and do not divide, effective waste clearance through autophagy is critical for their proper function and survival (Stavoe and Holzbaur 2019).”
ATG9 resides on a unique population of small vesicles in presynaptic nerve terminals
Binotti, B., Ninov, M., Cepeda, A. P., Ganzella, M., Matti, U., Riedel, D., Urlaub, H., Sambandan, S., & Jahn, R. (2023) · Autophagy · doi:10.1080/15548627.2023.2274204 · Cited by 29 · see citing works
Potential benefits of medium chain fatty acids in aging and neurodegenerative disease
Dunn, E., Zhang, B., Sahota, V., & Augustin, H. (2023) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2023.1230467 · Cited by 29 · see citing works
“In addition, MCFAs have been shown to improve mitochondrial function and promote autophagy, both of which are known to be dysregulated in aging and NDs (Rangaraju et al., 2019; Stavoe and Holzbaur, 2019).”
Background
Lost in traffic: consequences of altered palmitoylation in neurodegeneration
Ramzan, F., Abrar, F., Mishra, G., Liao, L. M. Q., & Martin, D. D. (2023) · Frontiers in Physiology · doi:10.3389/fphys.2023.1166125 · Cited by 29 · see citing works
“Since neurons are terminally differentiated postmitotic cells that cannot replenish via cell division, autophagy plays an integral role in ensuring the removal of toxic cargo to maintain cellular homeostasis (reviewed in (Kulkarni and Maday, 2018; Stavoe and Holzbaur, 2019)).”
Background
Autophagy and neurodegeneration: Unraveling the role of C9ORF72 in the regulation of autophagy and its relationship to ALS-FTD pathology
Diab, R., Pilotto, F., & Saxena, S. (2023) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2023.1086895 · Cited by 29 · see citing works
“Frequently, loss of function mutations are coupled with gain of toxic function of the genes that promote toxic protein aggregation, thereby contributing to the disruption of physiological cellular function and leading to neuronal death (Stavoe and Holzbaur, 2019; Monaco and Fraldi, 2020).”
Background
The Potential Role of Voltage-Dependent Anion Channel in the Treatment of Parkinson's Disease
He, Y., Wang, W.-J., Yang, T., Thomas, E. R., Dai, R., & Li, X. (2022) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2022/4665530 · Cited by 29 · see citing works
“Mitochondria participate in many biological cell processes such as apoptosis [33], autophagy [34], ferroptosis [32], pyroptosis [35], and cellular senescence [36].”
Current Knowledge of Endolysosomal and Autophagy Defects in Hereditary Spastic Paraplegia
Marchesi, L. T., Leblanc, M., & Stevanin, G. (2021) · Cells · doi:10.3390/cells10071678 · Cited by 29 · see citing works
Emerging roles of ATG9/ATG9A in autophagy: implications for cell and neurobiology
Choi, J., Jang, H., Xuan, Z., & Park, D. (2024) · Autophagy · doi:10.1080/15548627.2024.2384349 · Cited by 28 · see citing works
Neuronal endoplasmic reticulum architecture and roles in axonal physiology.
Yperman, K., & Kuijpers, M. (2023) · Molecular and cellular neurosciences · doi:10.1016/j.mcn.2023.103822 · Cited by 28 · see citing works
Dopaminergic Axons: Key Recitalists in Parkinson’s Disease
Mishra, A., & Dixit, A. (2021) · Neurochemical Research · doi:10.1007/s11064-021-03464-1 · Cited by 28 · see citing works
Pentraxin 3 Promotes Glioblastoma Progression by Negative Regulating Cells Autophagy
Wang, Z.-Y., Wang, X., Zhang, N., Zhang, H., Dai, Z.-Y., Zhang, M.-Y., Feng, S.-S., & Cheng, Q. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.00795 · Cited by 28 · see citing works
“Cells autophagy is a programmed cell death and act as a response to unfavorable factors like hypoxia and nutrient deficiency (Stavoe and Holzbaur, 2019).”
Background
Irisin attenuates acute glaucoma-induced neuroinflammation by activating microglia-integrin αVβ5/AMPK and promoting autophagy.
Zhang, Q.-X., Xiang, S., Chen, X., Rong, Y., Huang, L., Chen, Z.-Q., Yao, K., Chen, W., Deng, C.-H., & Wang, J.-M. (2024) · International Immunopharmacology · doi:10.1016/j.intimp.2024.112545 · Cited by 27 · see citing works
Spatiotemporal analysis of axonal autophagosome–lysosome dynamics reveals limited fusion events and slow maturation
Cason, S. E., Mogre, S. S., Holzbaur, E., & Koslover, E. F. (2022) · Molecular Biology of the Cell · doi:10.1091/mbc.e22-03-0111 · Cited by 27 · see citing works
“the axon, up to 1 m in humans, to recycle their cargo (Maday and Holzbaur, 2014; Stavoe and Holzbaur, 2019).”
BackgroundSelf-citation
Does propofol definitely improve postoperative cognitive dysfunction?—a review of propofol-related cognitive impairment
Liu, P.-F., Zhao, S., Qiao, H., Li, T.-Z., Mi, W., Xu, Z.-P., & Xue, X. (2022) · Acta Biochimica et Biophysica Sinica · doi:10.3724/abbs.2022067 · Cited by 27
“When autophagy function is impaired, the clearing ability decreases, leading to cognitive dysfunction [67].”
Background
Autophagy in Rare (NonLysosomal) Neurodegenerative Diseases
Zatyka, M., Sarkar, S., & Barrett, T. (2020) · Journal of Molecular Biology · doi:10.1016/j.jmb.2020.02.012 · Cited by 27 · see citing works
“Autophagy is also an important regulator of neurodevelopment by negatively regulating axon outgrowth and positively regulating synaptic formation [33,34].”
Towards a better understanding of the neuro-developmental role of autophagy in sickness and in health
Zapata-Muñoz, J., Villarejo-Zori, B., Largo-Barrientos, P., & Boya, P. (2021) · Cell Stress · doi:10.15698/cst2021.07.253 · Cited by 26 · see citing works
Impaired neuronal macroautophagy in the prelimbic cortex contributes to comorbid anxiety-like behaviors in rats with chronic neuropathic pain
Fu, S., Sun, H., Wang, J., Gao, S., Zhu, L., Cui, K., Liu, S., Qi, X., Guan, R.-Q., Fan, X., et al. (2024) · Autophagy · doi:10.1080/15548627.2024.2330038 · Cited by 25 · see citing works
The influence of NQO2 on the dysfunctional autophagy and oxidative stress induced in the hippocampus of rats and in SH‐SY5Y cells by fluoride
Ran, L.-Y., Xiang, J., Zeng, X.-X., He, W., Dong, Y.-T., Yu, W.-F., Qi, X.-L., Xiao, Y., Cao, K., Zou, J., et al. (2023) · CNS Neuroscience & Therapeutics · doi:10.1111/cns.14090 · Cited by 25 · see citing works
Programmed cell death in cerebellar Purkinje neurons.
Erekat, N. (2022) · Journal of Integrative Neuroscience · doi:10.31083/j.jin2101030 · Cited by 25 · see citing works
“Autophagy occurs in neurons in physiological processes, such as regulation of metabolism through removal of particular enzymes, morphogenesis, and tissue remodeling due to differentiation [54, 55].”
Background
Targeting Autophagy, Ferroptosis, and Neuroinflammation: Polyphenol-Mediated Modulation of Emerging Signaling Pathways in Neurodegeneration
Jindal, A., & Rai, S. N. (2026) · Molecular Neurobiology · doi:10.1007/s12035-026-05760-9 · Cited by 24 · see citing works
“Effective autophagy is essential for preserving proteostasis, regulating mitochondrial quality, and averting toxicity in neurons, which are post-mitotic, long-lived cells [8].”
MAPK Signaling in the Interplay Between Oxidative Stress and Autophagy
Desideri, E., Castelli, S., & Ciriolo, M. (2025) · Antioxidants · doi:10.3390/antiox14060662 · Cited by 24 · see citing works
Inhibiting Microglia-Derived NLRP3 Alleviates Subependymal Edema and Cognitive Dysfunction in Posthemorrhagic Hydrocephalus after Intracerebral Hemorrhage via AMPK/Beclin-1 Pathway
Zhang, Z.-R., Guo, P.-W., Huang, S.-N., Jia, Z.-C., Chen, T.-N., Liu, X., Feng, H., & Chen, Y.-J. (2022) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2022/4177317 · Cited by 24 · see citing works
“As the terminally di ﬀ erentiated cells, neurons did not divide and replicate themselves, which was the main reason a severe brain injury was often di ﬃ cult to recover [47].”
Axonal Organelles as Molecular Platforms for Axon Growth and Regeneration after Injury
Petrova, V., Nieuwenhuis, B., Fawcett, J., & Eva, R. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22041798 · Cited by 24 · see citing works
“Autophagosomes participate in degradation through gathering cellular material and mitochondria then fusing with lysosomes, but are also an important part of the recycling machinery (reviewed in [184,185]).”
Background
Bisphenol S impairs mitochondrial function by targeting Myo19/oxidative phosphorylation pathway contributing to axonal and dendritic injury.
Zhang, X., Gong, H.-Y., Zhao, Y., Wu, Y.-J., Cheng, J., Song, Y., Wang, B.-Q., Qin, Y.-F., & Sun, M.-K. (2024) · Environment International · doi:10.1016/j.envint.2024.108643 · Cited by 23 · see citing works
Latest advances in mechanisms of epileptic activity in Alzheimer’s disease and dementia with Lewy Bodies
Vicente, M., Addo-Osafo, K., & Vossel, K. (2024) · Frontiers in Neurology · doi:10.3389/fneur.2024.1277613 · Cited by 23 · see citing works
“Another crucial role function of mTOR signaling is autophagy, the process of degrading and recycling components of dysfunctional cells and proteins (164).”
Background
Melatonin Attenuates Ropivacaine-Induced Apoptosis by Inhibiting Excessive Mitophagy Through the Parkin/PINK1 Pathway in PC12 and HT22 Cells
Zeng, L., He, J.-F., Liu, C.-G., Zhang, F., Zhang, Z., Chen, H.-X., Wang, Q., Ding, X.-D., & Luo, H.-Y. (2021) · Inflammation · doi:10.1007/s10753-021-01579-9 · Cited by 23 · see citing works
“It stabilizes the intercellular environment in most cells including neurons [29, 30].”
Background
Autophagy mediated targeting degradation, a promising strategy in drug development.
Zhang, J., Pan, X., Ji, W.-S., & Zhou, J.-M. (2024) · Bioorganic chemistry (Print) · doi:10.1016/j.bioorg.2024.107466 · Cited by 22 · see citing works
Logistics of neuronal protein turnover: Numbers and mechanisms.
Sun, C., & Schuman, E. (2022) · Molecular and cellular neurosciences · doi:10.1016/j.mcn.2022.103793 · Cited by 22 · see citing works
Acute central nervous system toxicity during treatment of pediatric acute lymphoblastic leukemia: phenotypes, risk factors and genotypes
Anastasopoulou, S., Nielsen, R. L., Als-Nielsen, B., Banerjee, J., Eriksson, M. A., Helenius, M., Heyman, M., Johannsdottir, I. M., Jónsson, Ó., Macgregor, S., et al. (2022) · Haematologica · doi:10.3324/haematol.2021.280016 · Cited by 22 · see citing works
Lipin1 Alleviates Autophagy Disorder in Sciatic Nerve and Improves Diabetic Peripheral Neuropathy
Wang, M.-J., Xie, M., Yu, S.-Y., Shang, P., Zhang, C., Han, X., Fan, C., Chen, L., Zhuang, X.-H., & Chen, S.-H. (2021) · Molecular Neurobiology · doi:10.1007/s12035-021-02540-5 · Cited by 22 · see citing works
Intermittent Hypoxic Conditioning Rescues Cognition and Mitochondrial Bioenergetic Profile in the Triple Transgenic Mouse Model of Alzheimer’s Disease
Correia, S., Machado, N. J., Alves, M., Oliveira, P., & Moreira, P. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22010461 · Cited by 22 · see citing works
“Subsequently, active Parkin leads to the ubiquitination of mitochondrial proteins which serves as a distinct molecular code required for the selective recruitment of autophagy machinery and the completion of mitophagy [26,27].”
Background
Valproic acid affects neuronal fate and microglial function via enhancing autophagic flux in mice after traumatic brain injury
Zheng, Z., Wu, Y.-Q., Li, Z., Ye, L.-X., Lu, Q., Zhou, Y., Yuan, Y., Jiang, T., Xie, L., Liu, Y.-L., et al. (2020) · Journal of Neurochemistry · doi:10.1111/jnc.14892 · Cited by 21 · see citing works
Exploiting Natural Niches with Neuroprotective Properties: A Comprehensive Review
Moukham, H., Lambiase, A., Barone, G. D., Tripodi, F., & Coccetti, P. (2024) · Nutrients · doi:10.3390/nu16091298 · Cited by 20 · see citing works
“Autophagy is particularly important in neurons since it is involved in neurodevelopment as well as in the maintenance of neuronal homeostasis, and basal beneficial autophagy is necessary to maintain lifespan and prolong longevity [100].”
Background
Neurotropic virus infection and neurodegenerative diseases: Potential roles of autophagy pathway
Zhao, Y.-J., Xu, K., Shu, F.-X., & Zhang, F. (2023) · CNS Neuroscience & Therapeutics · doi:10.1111/cns.14548 · Cited by 20 · see citing works
Kaempferol improves Pb-induced cognitive impairments via inhibiting autophagy.
Wang, M., Xia, Y., Ai, S., Gu, X.-Z., & Wang, H.-L. (2023) · Journal of Nutritional Biochemistry · doi:10.1016/j.jnutbio.2023.109556 · Cited by 20
Activating transcription factor 6 regulates cystathionine to increase autophagy and restore memory in Alzheimer' s disease model mice.
Zhang, J.-Y., Ma, S., Liu, X.-L., Du, Y., Zhu, X.-L., Liu, Y., & Wu, X.-P. (2022) · Biochemical and Biophysical Research Communications - BBRC · doi:10.1016/j.bbrc.2022.05.053 · Cited by 20 · see citing works
The active zone protein Clarinet regulates synaptic sorting of ATG-9 and presynaptic autophagy
Zhao, X., Yang, S., Kargbo-Hill, S. E., Clark, B., Manning, L., & Colón‐Ramos, D. A. (2023) · PLoS Biology · doi:10.1371/journal.pbio.3002030 · Cited by 24 · see citing works
Autophagy–Lysosome Pathway Dysfunction in Neurodegeneration and Cancer: Mechanisms and Therapeutic Opportunities
Du, M., Yu, Y., Wang, J.-C., & Ji, C.-C. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms27010366 · Cited by 18 · see citing works
“While basal autophagy is essential for cellular homeostasis, its dysregulation—either deficiency or hyperactivation—can be pathogenic [25–27].”
Autophagic stress activates distinct compensatory secretory pathways in neurons
Palumbos, S. D., Popolow, J., Goldsmith, J., & Holzbaur, E. (2024) · bioRxiv · doi:10.1101/2024.11.07.621551 · Cited by 18
“Macroautophagy, hereafter referred to as autophagy, is a fundamental cellular process by which aggregated proteins and dysfunctional organelles are degraded (1).”
Self-citation

Authors: Stavoe, A. K. H., & Holzbaur, E. L. F.
Affiliations: University of Pennsylvania (US)
ORCID: Stavoe, Andrea K.H.
Holzbaur, Erika L.F.
Venue: Annual Review of Cell and Developmental Biology
Publisher: Annual Reviews
Published: 2019-10-06
Volume: 35
Issue: 1
Pages: 477-500
ISSN: 1081-0706 (ISSN-L)
1530-8995
DOI: 10.1146/annurev-cellbio-100818-125242
PMC: PMC6996145
OpenAlex: W2963539474
Cited by: 328
References: 157
Citations by year: 2026: 41 · 2025: 56 · 2024: 59 · 2023: 61 · 2022: 58 · 2021: 28 · 2020: 21 · 2019: 3 · 2018: 1
FWCI: 4.01
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Locations: Annual Review of Cell and Developmental Biology (publishedVersion)
PubMed (publishedVersion)
PubMed Central (acceptedVersion)
Funders: National Institutes of Health
National Institute of Neurological Disorders and Stroke (K99NS109286, R37NS060698)
Topics: Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
Life Sciences › Biochemistry, Genetics and Molecular Biology › Aging › Genetics, Aging, and Longevity in Model Organisms
Keywords: autophagy, neurons, autophagosome formation, selective autophagy, bulk autophagy, mitochondrial turnover, protein aggregation, brain development, neuronal homeostasis, aging, neurodegeneration, endoplasmic reticulum, organelle degradation
MeSH terms: Autophagosomes, Animals, Autophagy, Axons, Dendrites, Endoplasmic Reticulum, Homeostasis, Humans, Memory, Mitochondria, Neurons, Synapses, Neurodegenerative Diseases, Proteasome Endopeptidase Complex, Ubiquitination, Unfolded Protein Response

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

Autophagy in neurons

Abstract

Integrity signals

Claims the paper makes

Claims other papers make about this one

Self-check

Cites

Cited by

Record

About these checks