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Autophagy and Neurodegeneration: Pathogenic Mechanisms and Therapeutic Opportunities
Open accessAbstract
Autophagy is a conserved pathway that delivers cytoplasmic contents to the lysosome for degradation. Here we consider its roles in neuronal health and disease. We review evidence from mouse knockout studies demonstrating the normal functions of autophagy as a protective factor against neurodegeneration associated with intracytoplasmic aggregate-prone protein accumulation as well as other roles, including in neuronal stem cell differentiation. We then describe how autophagy may be affected in a range of neurodegenerative diseases. Finally, we describe how autophagy upregulation may be a therapeutic strategy in a wide range of neurodegenerative conditions and consider possible pathways and druggable targets that may be suitable for this objective.
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“and permanent or transient endogenous defects in autophagy have been associated with embryonic lethality, developmental defects, and multiple pathological disorders, including (but not limited to) neurodegeneration, cancer, and cardiovascular disorders [812–817].”
From Molecular mechanisms of cell death: recommendations of the nomenclature committee on cell death 2018. (2018) · cites this paper as [813]
In the citing paper
“Molecular and histopathologic analyses of patient tissues demonstrate mislocalized or accumulated autophagy machinery, pathogenic mutations underlying familial neurodegenerative diseases disable known autophagy-related factors, and genetically ablating autophagy effectors produce neurodegeneration in cell and animal model systems [74–81], supporting a role for autophagy dysfunction in the devel”
From Autophagy and ALS: mechanistic insights and therapeutic implications (2022) · cites this paper as [80]
In the citing paper
“The autophagic process is essential in preserving the homeostatic requirements of post‐mitotic neurons, both at the central and at the peripheral nervous system levels (Menzies et al, 2017; Scrivo et al, 2018; Mallucci et al, 2020)”
From Autophagy in major human diseases (2021) · cites this paper as Menzies et al, 2017
In the citing paper
“By analogy, a comparable phenotype has been described in Atg16l1 hypomorphic mice (Lv et al, 2014; Wu et al, 2016; Menzies et al, 2017).”
From Autophagy in major human diseases (2021) · cites this paper as Menzies et al, 2017
In the citing paper
“Aβ is targeted for autophagy‐dependent degradation within the lysosome, explaining why activation of autophagy reduces the burden of Aβ plaques in rodents (Boland et al, 2008; Menzies et al, 2017; Meng et al, 2019).”
From Autophagy in major human diseases (2021) · cites this paper as Menzies et al, 2017
In the citing paper
“However, autophagy appears to be causally implicated in the PSEN1 (presenilin 1)‐mediated conversion of APP (amyloid beta precursor protein) into Aβ (Yu et al, 2005), as well as in the non‐canonical secretion of Aβ into the extracellular space (Nilsson et al, 2013; Menzies et al, 2017).”
From Autophagy in major human diseases (2021) · cites this paper as Menzies et al, 2017
In the citing paper
“While autophagy proteins have been shown to impact the clearance of protein aggregates in neurons, most likely by the canonical autophagic process of aggrephagy (Frake et al., 2015; Menzies et al., 2017; Qaisiya et al., 2017; Sarkar et al., 2007; Sarkar et al., 2009; Webb et al., 2003; Yamamoto and Simonsen, 2011), effects in microglia of the CNS are more likely due to LANDO.”
From LC3-Associated Endocytosis Facilitates β-Amyloid Clearance and Mitigates Neurodegeneration in Murine Alzheimer’s Disease (2019) · cites this paper as Menzies et al., 2017
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“In addition, one of these specializations targets protein aggregates (aggrephagy) with direct relevance to neurodegeneration [81].”
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BackgroundPathways to healing: Plants with therapeutic potential for neurodegenerative diseases
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BackgroundTFEB-dependent induction of thermogenesis by the hepatocyte SLC2A inhibitor trehalose
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“Autophagy is the primary clearance mechanism for several aggregation-prone proteins, such as amyloid-β, α-synuclein and huntingtin, associated with Alzheimer’s, Parkinson’s and Huntington’s disease, respectively (Nixon, 2013; Menzies et al., 2017); a process termed aggrephagy (Gatica et al.”
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“Autophagy plays a vital role in neuronal regulation, and its impairment has been shown to lead to neuronal pathologies such as Alzheimer, Parkinson and Huntington diseases, amyotrophic lateral sclerosis, Vici syndrome, HSP, and others [26–28].”
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BackgroundAging Differentially Affects Axonal Autophagosome Formation and Maturation
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“Many studies have linked defects in autophagy to age-related neurodegenerative diseases [4–6].”
BackgroundTMEM175: A lysosomal ion channel associated with neurological diseases
Wu, L., Lin, Y., Song, J., Li, L., Rao, X., Wan, W., Wei, G., Hua, F., & Ying, J. (2023) · Neurobiology of Disease · doi:10.1016/j.nbd.2023.106244 · Cited by 31
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Self-citationAmino Acids in Autophagy: Regulation and Function
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“Mammalian target of rapamycin complex 1 (mTORC1) and AMP-dependent protein kinase (AMPK) can be activated by nutrients, growth factors, and AMP/ATP respectively, which, regulate the ULK1/2 complex through a series of phosphorylation events, 55 thereby in response to the autophagy activation.”
BackgroundStaufen Impairs Autophagy in Neurodegeneration
Paul, S., Dansithong, W., Gandelman, M., Figueroa, K. P., Zu, T., Ranum, L. P. W., Scoles, D. R., & Pulst, S. M. (2022) · Annals of Neurology · doi:10.1002/ana.26515 · Cited by 32
“Current understanding of autophagy emphasizes regulation by kinase cascades and by transcriptional changes in key genes involved in autophagy.(1,2,51) A number of RBPs other than autophagy-signaling pathway components like mTOR are involved in regulating autophagy-related mRNA metabolism, such as maintaining their sta…”
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“It was reported that A (cid:2) may be degraded by autophagy, and upregulation of autophagy has been shown to reduce A (cid:2) levels in a number of systems [36].”
Fu, Y., Zhang, J., Qin, R., Ren, Y., Zhou, T., Han, B., & Liu, B. (2025) · Pharmacological Reviews · doi:10.1016/j.pharmr.2025.100053 · Cited by 29
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Propofol Attenuates α-Synuclein Aggregation and Neuronal Damage in a Mouse Model of Ischemic Stroke
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Self-citationModulation of O-GlcNAcylation Regulates Autophagy in Cortical Astrocytes
Rahman, M. A., Hwang, H., Cho, Y., & Rhim, H. (2019) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2019/6279313 · Cited by 26
“In conclusion, it has been well studied that the stimulation of autophagy acts with beneficial effects in a number of neurodegenerative diseases [38, 39].”
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The pROS of Autophagy in Neuronal Health
Sedlackova, L., Kelly, G., & Korolchuk, V. I. (2020) · Journal of Molecular Biology · doi:10.1016/j.jmb.2020.01.020 · Cited by 28
Wang, H., Dou, S., Zhu, J., Shao, Z., Wang, C., & Cheng, B. (2020) · Neuropeptides · doi:10.1016/j.npep.2020.102112 · Cited by 27
Haddad, M. E., Eid, S., Harb, F., Massry, M. E., Azar, S. T., Sauleau, E., & Eid, A. A. (2022) · Journal of Pain · doi:10.1016/j.jpain.2022.02.011 · Cited by 28
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“Genetic anomalies in FTD are closely related to a deficient autophagic lysosomal network (ALN), and like ALS, the disease is characterized by aggregates containing tau, TDP43, RNAbinding protein FUS and other ubiquitylated proteins insufficiently cleared by the ALN [39].”
BackgroundIntermittent Fasting: Myths, Fakes and Truth on This Dietary Regimen Approach
Brogi, S., Tabanelli, R., Puca, S., & Calderone, V. (2024) · Foods · doi:10.3390/foods13131960 · Cited by 26
“…which involves the build-up of dangerous free radicals and is a condition that worsens with age and the progression of neurodegenerative disorders [155]. oxidative stress, which involves the build-up of dangerous free radicals and is a condition that worsens with age and the progression of…”
Yang, H., Niu, S., Guo, M., & Xue, Y. (2024) · Environmental Pollution · doi:10.1016/j.envpol.2024.124934 · Cited by 26
The interplay between probiotics and host autophagy: mechanisms of action and emerging insights
Sadeghloo, Z., Nabavi-Rad, A., Zali, M. R., Klionsky, D. J., & Yadegar, A. (2024) · Autophagy · doi:10.1080/15548627.2024.2403277 · Cited by 26
“Endoplasmic reticulum stress and irregular autophagy are linked to deposition of damaged misfolded proteins (e.g., MAPT/tau, TARDBP/TDP-43, SOD1, SNCA/α-synuclein, and those containing polyglutamine [polyQ]) [153,154].”
Lin, M., Chen, Y., Yang, H.-B., Lin, C., & Hung, S. (2019) · Neurotherapeutics · doi:10.1007/s13311-019-00803-7 · Cited by 27
Jang, K.-H., Hwang, Y., & Kim, E. (2020) · PubMed Central · doi:10.14348/molcells.2020.0078 · Cited by 25
“Such differential blocking mechanisms against autophagy process depending on the stress characteristics have been also shown in neurodegenerative disease (Menzies et al., 2017).”
Mitochondria-ER Tethering in Neurodegenerative Diseases
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Running to save sight: The effects of exercise on retinal health and function
Chu‐Tan, J. A., Kirkby, M., & Natoli, R. (2021) · Clinical and Experimental Ophthalmology · doi:10.1111/ceo.14023 · Cited by 27
Proteomics analysis of N-methyl-d-aspartate-induced cell death in retinal and optic nerves
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Akwa, Y., Malta, C. D., Zallo, F., Gondard, E., Lunati, A., Diaz-de-Grenu, L. Z., Zampelli, A., Boiret, A., Santamaria, S., Martinez-Preciado, M., et al. (2022) · Autophagy · doi:10.1080/15548627.2022.2095791 · Cited by 27
“Since TFEB coordinately regulates both processes, manipulation of its activation could achieve such a goal [19,52].”
BackgroundThe Role of Ferroptosis in Nervous System Disorders
Du, L., Wu, Y., Fan, Z., Li, Y., Guo, X., Fang, Z., & Zhang, X. (2023) · Journal of Integrative Neuroscience · doi:10.31083/j.jin2201019 · Cited by 26
“Neurodegenerative diseases are caused by the accumulation of oligomers and the aggregation of misfolded proteins [86,87].”
Intermittent Fasting: Myths, Fakes and Truth on this Dietary Regimen Approach
Brogi, S., Tabanelli, R., Puca, S., & Calderone, V. (2024) · doi:10.20944/preprints202405.1820.v1 · Cited by 26
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“Macroautophagy is an evolutionarily conserved process that delivers diverse cellular contents to lysosomes for degradation, and a broadly used homeostatic mechanism essential for brain physiology [29,30].”
Backgroundde Calbiac, H., Renault, S., Haouy, G., Jung, V. A., Roger, K., Zhou, Q., Campanari, M., Chentout, L., Demy, D. L., Marian, A., et al. (2024) · Autophagy · doi:10.1080/15548627.2024.2358736 · Cited by 23
“It is becoming clear that autophagy deficiency is a relevant factor contributing to C9orf72 /ALS pathogenesis, thus supporting the relevance of autophagy as a major therapeutic strategy to protect neurons from degeneration [84–86].”
Vishnumukkala, T., Nassir, C. M. N. C. M., Hein, Z. M., Gopalakrishna, P. K., Karikalan, B., Alkatiri, A., Jagadeesan, S., Naik, V. R., Thomas, W., Moklas, M. A. M., et al. (2025) · Cells · doi:10.3390/cells14191497 · Cited by 30
Assessment of mammalian endosomal microautophagy
Krause, G. J., & Cuervo, A. M. (2020) · Methods in cell biology · doi:10.1016/bs.mcb.2020.10.009 · Cited by 25
Rahman, M. A., Cho, Y., Hwang, H., & Rhim, H. (2020) · Brain Sciences · doi:10.3390/brainsci10120958 · Cited by 25
“Considering that autophagy is involved in the degradation of abnormal protein aggregates and the clearance of misfolded proteins [6,73–75], the stimulation of autophagic activity may serve as an effective approach in treating neurodegenerative disorders [18,76,77].”
BackgroundDeubiquitylating enzymes in neuronal health and disease
Amer‐Sarsour, F., Kordonsky, A., Berdichevsky, Y., Prag, G., & Ashkenazi, A. (2021) · Cell Death and Disease · doi:10.1038/s41419-020-03361-5 · Cited by 27
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Zhang, Z., Li, H., Su, Y., Ma, J., Yuan, Y., Yu, Z., Shi, M., Shao, S., Zhang, Z., & Hölscher, C. (2022) · Frontiers in Neuroscience · doi:10.3389/fnins.2022.814430 · Cited by 26
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“As a result, a major focus has been spent on identifying safe and effective pharmacological agents that can induce autophagy to effectively target key aspects of the molecular pathology in AD and other neurodegenerative diseases (Rubinsztein et al., 2012; Rubinsztein et al., 2015; Galluzzi et al., 2017; Menzies et al.…”
BackgroundXia, J., Wan, Y., Wu, J., Yang, Y., Xu, J., Zhang, L., Liu, D., Chen, L., Tang, F., Ao, H., et al. (2022) · Critical Reviews in Food Science and Nutrition · doi:10.1080/10408398.2022.2115457 · Cited by 25
“The accumulation of Aβ also impairs the autophagosomes and lysosome fusion, reducing the degradation of Aβ by auto-phagy (Menzies et al. 2017; Ułamek-Kozioł et al. 2013).”
BackgroundMolecular understanding of ER-MT communication dysfunction during neurodegeneration
Sammeta, S. S., Banarase, T. A., Rahangdale, S. R., Wankhede, N. L., Aglawe, M. M., Taksande, B. G., Mangrulkar, S. V., Upaganlawar, A. B., Koppula, S., Kopalli, S. R., et al. (2023) · Mitochondrion · doi:10.1016/j.mito.2023.07.005 · Cited by 26
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“In AD, besides the inhibited autophagy activity, the imbalance of autophagosome formation and degradation which is attributed to lysosomal impairment is also a prominent feature of autophagy dysfunction 10 .”
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Autophagy Intertwines with Different Diseases—Recent Strategies for Therapeutic Approaches
Ramesh, J., Ronsard, L., Gao, A., & Venugopal, B. (2019) · Diseases · doi:10.3390/diseases7010015 · Cited by 26
“HIV-Tat has been found to cause a decrease in Beclin-1, LC3II, and p62 levels in neurons, suggesting that Tat may induce autophagic degradation by inducing the fusion of autophagosomes and lysosomes [153,154].”
BackgroundAutophagy-associated signal pathways of functional foods for chronic diseases
Xie, J., Liang, J., & Chen, N. (2019) · Food Science and Human Wellness · doi:10.1016/j.fshw.2019.03.002 · Cited by 26
Metadata
- Authors
- Menzies, F. M., Fleming, A., Caricasole, A., Bento, C. F., Andrews, S. P., Ashkenazi, A., Füllgrabe, J., Jackson, A., Jimenez Sanchez, M., Karabiyik, C., Licitra, F., Lopez Ramirez, A., Pavel, M., Puri, C., Renna, M., Ricketts, T., Schlotawa, L., Vicinanza, M., Won, H., Zhu, Y., Skidmore, J., & Rubinsztein, D. C.
- Affiliations
- University of Cambridge (GB)
- Corresponding author
- Rubinsztein, David C.
- ORCID
- Venue
- Neuron
- Publisher
- Elsevier BV
- Published
- 2017-03
- Volume
- 93
- Issue
- 5
- Pages
- 1015-1034
- ISSN
- 0896-6273 (ISSN-L)
- OpenAlex
- W2592067246
- Cited by
- 1,134
- References
- 288
- Citations by year
- 2026: 68 · 2025: 96 · 2024: 107 · 2023: 119 · 2022: 153 · 2021: 138 · 2020: 145 · 2019: 159 · 2018: 108 · 2017: 39
- FWCI
- 16.37
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Neuron (publishedVersion)
- PubMed (publishedVersion)
- DIGITAL.CSIC (Spanish National Research Council (CSIC)) (acceptedVersion, other-oa)
- Research Portal (King's College London) (submittedVersion, other-oa)
- Apollo (University of Cambridge) (submittedVersion, cc-by-nc-nd)
- Apollo
- Funders
- Tau Consortium
- Alzheimer’s Research UK
- Wellcome Trust (095317/Z/11/Z)
- Cambridge Institute for Medical Research (100140/Z/12/Z)
- NIHR Biomedical Research Unit in Dementia at Addenbrooke’s Hospital
- The Rosetrees Trust
- FEBS
- Addenbrooke’s Charitable Trust
- Sims Scholarship
- James Baird Fund
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Keywords
- autophagy, neurodegeneration, lysosomal degradation, protein aggregation, neurodegenerative diseases, therapeutic target, druggable targets, mouse knockout models
- MeSH terms
- Animals, Autophagy, Humans, Lysosomes, Motor Neurons, Proteins, Signal Transduction, Neurodegenerative Diseases
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