PLIC proteins or ubiquilins regulate autophagy‐dependent cell survival during nutrient starvation
Open accessAbstract
Ubiquilins (UBQLNs) are adaptor proteins thought to deliver ubiquitinated substrates to proteasomes. Here, we show a role for UBQLN in autophagy: enforced expression of UBQLN protects cells from starvation-induced death, whereas depletion of UBQLN renders cells more susceptible. The UBQLN protective effect requires the autophagy-related genes ATG5 and ATG7, two essential components of autophagy. The ubiquitin-associated domain of UBQLN mediates both its association with autophagosomes and its protective effect against starvation. Depletion of UBQLN delays the delivery of autophagosomes to lysosomes. This study identifies a new role for UBQLN in regulating the maturation of autophagy, expanding the involvement of ubiquitin-related proteins in this process.
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UBQLN2 can act as an autophagy receptor by directly interacting with LC3 in autophagosomes.
“UBQLN2 can also act as an autophagy receptor by directly interacting with LC3 in autophagosomes [219,220].”
From Autophagy and ALS: mechanistic insights and therapeutic implications (2022) · cites this paper as [219]
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Repertoires of Autophagy in the Pathogenesis of Ocular Diseases
Li, Y., Jiang, Q. L., Cao, G.-F., Yao, J., & Yan, B. (2015) · Cellular Physiology and Biochemistry · doi:10.1159/000373980 · Cited by 16,351 · see citing works
Cui, C., Cui, J., Jin, F., Cui, Y., Li, R., Jiang, X., Tian, Y., Wang, R. C., Jiang, P., & Gao, J. (2017) · Cellular Physiology and Biochemistry · doi:10.1159/000479571 · Cited by 5,214 · see citing works
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 · see citing works
Autophagy as a regulated pathway of cellular degradation.
Klionsky, D., & Emr, S. (2000) · Science · doi:10.1126/science.290.5497.1717 · Cited by 3,794 · see citing works
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 · see citing works
The role of autophagy during the early neonatal starvation period
Kuma, A., Hatano, M., Matsui, M., Yamamoto, A., Nakaya, H., Yoshimori, T., Ohsumi, Y., Tokuhisa, T., & Mizushima, N. (2004) · Nature · doi:10.1038/nature03029 · Cited by 2,865 · see citing works
Impairment of starvation-induced and constitutive autophagy in <i>Atg7</i> -deficient mice
Komatsu, M., Waguri, S., Ueno, T., Iwata, J., Murata, S., Tanida, I., Ezaki, J., Mizushima, N., Ohsumi, Y., Uchiyama, Y., et al. (2005) · The Journal of Cell Biology · doi:10.1083/jcb.200412022 · Cited by 2,331 · see citing works
Kimura, S., Noda, T., & Yoshimori, T. (2007) · Autophagy · doi:10.4161/auto.4451 · Cited by 2,278 · see citing works
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 · see citing works
Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death
Arrasate, M., Mitra, S., Schweitzer, E. S., Segal, M. R., & Finkbeiner, S. (2004) · Nature · doi:10.1038/nature02998 · Cited by 1,979 · see citing works
Inhibition of Macroautophagy Triggers Apoptosis
Boya, P., González‐Polo, R. A., Casares, N., Perfettini, J., Dessen, P., Larochette, N., Métivier, D., Meley, D., Souquère, S., Yoshimori, T., et al. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.3.1025-1040.2005 · Cited by 1,629 · see citing works
Lemasters, J. J. (2005) · Rejuvenation Research · doi:10.1089/rej.2005.8.3 · Cited by 1,342 · see citing works
Yamamoto, A., Tagawa, Y., Yoshimori, T., Moriyama, Y., Masaki, R., & Tashiro, Y. (1998) · Cell Structure and Function · doi:10.1247/csf.23.33 · Cited by 1,312 · see citing works
Calpain-mediated cleavage of Atg5 switches autophagy to apoptosis
Yousefi, S., Perozzo, R., Schmid, I., Ziemiecki, A., Schaffner, T. J., Scapozza, L., Brunner, T., & Simon, H. (2006) · Nature Cell Biology · doi:10.1038/ncb1482 · Cited by 1,300 · see citing works
Characterization and Dynamics of Aggresome Formation by a Cytosolic Gfp-Chimera✪
García‐Mata, R., Bebők, Z., Sorscher, E. J., & Sztul, E. S. (1999) · The Journal of Cell Biology · doi:10.1083/jcb.146.6.1239 · Cited by 597 · see citing works
Induction of Autophagy during Extracellular Matrix Detachment Promotes Cell Survival
Fung, C., Lock, R., Gao, S., Salas, E., & Debnath, J. (2008) · Molecular Biology of the Cell · doi:10.1091/mbc.e07-10-1092 · Cited by 558 · cited 3× · see citing works
“When stably transfected with control or ATG7 short hairpin RNA (Fung et al, 2008), cells were maintained under 2 mg/ml of puromycin selection.”
BackgroundMethodInfluentialSelf-citationHofmann, K., & Falquet, L. (2001) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(01)01835-7 · Cited by 449 · see citing works
The hPLIC Proteins May Provide a Link between the Ubiquitination Machinery and the Proteasome
Kleijnen, M. F., Shih, A. H., Zhou, P., Kumar, S., Soccio, R. E., Kedersha, N., Gill, G., & Howley, P. M. (2000) · Molecular Cell · doi:10.1016/s1097-2765(00)00040-x · Cited by 352 · see citing works
Tracker Dyes to Probe Mitochondrial Autophagy (Mitophagy) in Rat Hepatocytes
Rodríguez‐Enríquez, S., Kim, I., Currin, R. T., & Lemasters, J. J. (2006) · Autophagy · doi:10.4161/auto.2229 · Cited by 331 · see citing works
Jana, N. R., Dikshit, P., Goswami, A., Kotliarova, S. E., Murata, S., Tanaka, K., & Nukina, N. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m412042200 · Cited by 323 · see citing works
Aggregate‐Prone Proteins Are Cleared from the Cytosol by Autophagy: Therapeutic Implications
Williams, A. J., Jahreiss, L., Sarkar, S., Saiki, S., Menzies, F. M., Ravikumar, B., & Rubinsztein, D. C. (2006) · Current topics in developmental biology/Current Topics in Developmental Biology · doi:10.1016/s0070-2153(06)76003-3 · Cited by 284 · see citing works
Budding yeast Dsk2p is a polyubiquitin-binding protein that can interact with the proteasome
Funakoshi, M., Sasaki, T., Nishimoto, T., & Kobayashi, H. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.012585199 · Cited by 244 · see citing works
Autophagy in Innate and Adaptive Immunity
Xu, Y., & Eissa, N. T. (2010) · Proceedings of the American Thoracic Society · doi:10.1513/pats.200909-103js · Cited by 242 · see citing works
Structural Studies of the Interaction between Ubiquitin Family Proteins and Proteasome Subunit S5a
Walters, K. J., Kleijnen, M. F., Goh, A. M., Wagner, G., & Howley, P. M. (2002) · Biochemistry · doi:10.1021/bi011892y · Cited by 220 · see citing works
Mah, A. L., Perry, G. L., Smith, M. A., & Monteiro, M. J. (2000) · The Journal of Cell Biology · doi:10.1083/jcb.151.4.847 · Cited by 203 · see citing works
Wu, A. L., Wang, J., Zheleznyak, A., & Brown, E. J. (1999) · Molecular Cell · doi:10.1016/s1097-2765(00)80212-9 · Cited by 140 · see citing works
Self-citationWang, H., Lim, P. J., Yin, C., Rieckher, M., Vogel, B. E., & Monteiro, M. J. (2006) · Human Molecular Genetics · doi:10.1093/hmg/ddl017 · Cited by 118 · see citing works
Autophagy and antigen presentation
Münz, C. (2006) · Cellular Microbiology · doi:10.1111/j.1462-5822.2006.00714.x · Cited by 90 · see citing works
Autophagy in innate and adaptive immunity.
Deretic, V. (2005) · Trends in immunology · doi:10.1016/j.it.2005.08.003 · Cited by 89 · see citing works
[29] Localization of GTPases by indirect immunofluorescence and immunoelectron microscopy
McCaffery, J. M., & Farquhar, M. G. (1995) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(95)57031-4 · Cited by 71 · see citing works
Ubiquilin recruits Eps15 into ubiquitin-rich cytoplasmic aggregates via a UIM-UBL interaction
Regan‐Klapisz, E., Sorokina, I., Voortman, J., de Keizer, P. L. J., Roovers, R. C., Verheesen, P., Urbé, S., Fallon, L., Fon, E. A., Verkleij, A. J., et al. (2005) · Journal of Cell Science · doi:10.1242/jcs.02571 · Cited by 64 · see citing works
Characterization of ubiquilin 1, an mTOR-interacting protein
Wu, S., Mikhailov, A. V., Kalloo-Hosein, H., Hara, K., Yonezawa, K., & Avruch, J. (2002) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/s0167-4889(01)00164-1 · Cited by 63 · see citing works
Feng, P., Scott, C. W., Cho, N., Nakamura, H., Chung, Y.-H., Monteiro, M. J., & Jung, J. U. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.9.3938-3948.2004 · Cited by 58 · see citing works
N’Diaye, E.-N., & Brown, E. J. (2003) · The Journal of Cell Biology · doi:10.1083/jcb.200307155 · Cited by 51 · see citing works
Self-citationThe Ubiquitin-like Protein PLIC-2 Is a Negative Regulator of G Protein-coupled Receptor Endocytosis
N’Diaye, E.-N., Hanyaloglu, A. C., Kajihara, K. K., Puthenveedu, M. A., Wu, P., von Zastrow, M., & Brown, E. J. (2008) · Molecular Biology of the Cell · doi:10.1091/mbc.e07-08-0775 · Cited by 36 · see citing works
Self-citationQuantitative monitoring of autophagic degradation
Kawai, A., Takano, S., Nakamura, N., & Ohkuma, S. (2006) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2006.09.168 · Cited by 24 · see citing works
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Guidelines for the use and interpretation of assays for monitoring autophagy (3rd edition).
Klionsky, D. J., Abdelmohsen, K., Abe, A., Abedin, M. J., Abeliovich, H., Acevedo Arozena, A., Adachi, H., Adams, C. M., Adams, P. D., Adeli, K., et al. (2016) · Autophagy · doi:10.1080/15548627.2015.1100356 · Cited by 5,894 · see citing works
Combination of ERK and autophagy inhibition as a treatment approach for pancreatic cancer
Bryant, K. L., Stalnecker, C. A., Zeitouni, D., Klomp, J. E., Peng, S., Tikunov, A. P., Gunda, V., Pierobon, M., Waters, A. M., George, S. D., et al. (2019) · Nature Medicine · doi:10.1038/s41591-019-0368-8 · Cited by 692 · see citing works
Autophagy mediates degradation of nuclear lamina
Dou, Z., Xu, C., Donahue, G., Shimi, T., Pan, J.-A., Zhu, J., Ivanov, A., Capell, B. C., Drake, A. M., Shah, P. P., et al. (2015) · Nature · doi:10.1038/nature15548 · Cited by 655 · see citing works
A Diversity of Selective Autophagy Receptors Determines the Specificity of the Autophagy Pathway
Kirkin, V., & Rogov, V. V. (2019) · Molecular Cell · doi:10.1016/j.molcel.2019.09.005 · Cited by 524 · see citing works
Aggrephagy: Selective Disposal of Protein Aggregates by Macroautophagy
Lamark, T., & Johansen, T. (2012) · International Journal of Cell Biology · doi:10.1155/2012/736905 · Cited by 490 · see citing works
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 485 · see citing works
Autophagic cell death restricts chromosomal instability during replicative crisis
Nassour, J., Radford, R., Correia, A., Fusté, J. M., Schoell, B., Jauch, A., Shaw, R. J., & Karlseder, J. (2019) · Nature · doi:10.1038/s41586-019-0885-0 · Cited by 429 · see citing works
Autophagy and Alzheimer’s Disease: From Molecular Mechanisms to Therapeutic Implications
Uddin, M. S., Stachowiak, A., Mamun, A. A., Tzvetkov, N. T., Takeda, S., Atanasov, A. G., Bergantin, L. B., Abdel‐Daim, M. M., & Stankiewicz, A. M. (2018) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2018.00004 · Cited by 440 · see citing works
Copper is an essential regulator of the autophagic kinases ULK1/2 to drive lung adenocarcinoma
Tsang, T., Posimo, J. M., Gudiel, A. A., Cicchini, M., Feldser, D. M., & Brady, D. C. (2020) · Nature Cell Biology · doi:10.1038/s41556-020-0481-4 · Cited by 373 · see citing works
TDP-43 Proteinopathy and ALS: Insights into Disease Mechanisms and Therapeutic Targets
Scotter, E. L., Chen, H.-J., & Shaw, C. E. (2015) · Neurotherapeutics · doi:10.1007/s13311-015-0338-x · Cited by 356 · see citing works
Dao, T. P., Kolaitis, R.-M., Kim, H.-J., O'Donovan, K., Martyniak, B., Colicino, E., Hehnly, H., Taylor, J. P., & Castañeda, C. A. (2018) · Molecules and Cells · doi:10.1016/j.molcel.2018.02.004 · Cited by 319 · see citing works
Hepatic stellate cell autophagy inhibits extracellular vesicle release to attenuate liver fibrosis
Gao, J., Wei, B., de Assuncao, T. M., Liu, Z., Hu, X., Ibrahim, S., Cooper, S. A., Cao, S., Shah, V. H., & Kostallari, E. (2020) · Journal of Hepatology · doi:10.1016/j.jhep.2020.04.044 · Cited by 288 · see citing works
A comprehensive glossary of autophagy-related molecules and processes (2ndedition)
Klionsky, D. J., Baehrecke, E. H., Brumell, J. H., Chu, C. T., Codogno, P., Cuervo, A. M., Debnath, J., Deretic, V. P., Elazar, Z., Eskelinen, E., et al. (2011) · Autophagy · doi:10.4161/auto.7.11.17661 · Cited by 293 · see citing works
Self-citationZKSCAN3 Is a Master Transcriptional Repressor of Autophagy
Chauhan, S., Jinesh, G. G., Chauhan, S. C., Manyam, G. C., Wang, J., Kamat, A. M., & Boyd, D. D. (2013) · Molecular Cell · doi:10.1016/j.molcel.2013.01.024 · Cited by 276 · see citing works
Exploiting cancer cell vulnerabilities to develop a combination therapy for ras-driven tumors
De Raedt, T., Walton, Z., Yecies, J. L., Li, D., Chen, Y., Malone, C. F., Maertens, O., Jeong, S. M., Bronson, R. T., Lebleu, V., et al. (2011) · Cancer Cell · doi:10.1016/j.ccr.2011.08.014 · Cited by 258 · see citing works
Autophagy Receptors and Neurodegenerative Diseases
Deng, Z., Purtell, K., Lachance, V., Wold, M. S., Chen, S., & Yue, Z. (2017) · Trends in Cell Biology · doi:10.1016/j.tcb.2017.01.001 · Cited by 239 · see citing works
Deng, R., Zhang, H., Huang, J.-H., Cai, R., Wang, Y., Chen, Y., Hu, B., Ye, Z.-P., Li, Z., Mai, J., et al. (2020) · Autophagy · doi:10.1080/15548627.2020.1850609 · Cited by 233 · see citing works
Ubiquilin functions in autophagy and is degraded by chaperone-mediated autophagy
Rothenberg, C., Srinivasan, D., Mah, L., Kaushik, S., Peterhoff, C. M., Ugolino, J., Fang, S., Cuervo, A. M., Nixon, R. A., & Monteiro, M. J. (2010) · Human Molecular Genetics · doi:10.1093/hmg/ddq231 · Cited by 225 · see citing works
Protein aggregation and degradation mechanisms in neurodegenerative diseases.
Takalo, M., Salminen, A., Soininen, H. S., Hiltunen, M. O., & Haapasalo, A. (2013) · Europe PMC (PubMed Central) · Cited by 219 · see citing works
Gao, F., Almeida, S., & Lopez‐Gonzalez, R. (2017) · The EMBO Journal · doi:10.15252/embj.201797568 · Cited by 218 · see citing works
Autophagy in Neurodegenerative Diseases: A Hunter for Aggregates
Park, H., Kang, J., & Lee, S. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21093369 · Cited by 205 · see citing works
Zhang, W., Xu, C., Sun, J., Shen, H., Wang, J., & Yang, C. (2022) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2022.01.008 · Cited by 214 · see citing works
Autophagy and ALS: mechanistic insights and therapeutic implications
Chua, J. P., De Calbiac, H., Kabashi, E., & Barmada, S. J. (2022) · Autophagy · doi:10.1080/15548627.2021.1926656 · Cited by 189 · see citing works
“UBQLN2 can also act as an autophagy receptor by directly interacting with LC3 in autophagosomes [219,220].”
BackgroundThe ubiquitin-proteasome system and autophagy: Coordinated and independent activities
Cohen‐Kaplan, V., Livneh, I., Avni, N., Cohen-Rosenzweig, C., & Ciechanover, A. J. (2016) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2016.07.019 · Cited by 196 · see citing works
Brettschneider, J., Deerlin, V. M. V., Robinson, J. L., Kwong, L. K., Lee, E. B., Ali, Y., Safren, N., Monteiro, M. J., Toledo, J. B., Elman, L. B., et al. (2012) · Acta Neuropathologica · doi:10.1007/s00401-012-0970-z · Cited by 183 · see citing works
A comprehensive glossary of autophagy-related molecules and processes
Klionsky, D. J., Codogno, P., Cuervo, A. M., Deretic, V. P., Elazar, Z., Fueyo-Margareto, J., Gewirtz, D. A., Kroemer, G., Levine, B., Mizushima, N., et al. (2010) · Autophagy · doi:10.4161/auto.6.4.12244 · Cited by 184 · see citing works
iLIR database: A web resource for LIR motif-containing proteins in eukaryotes
Jacomin, A., Samavedam, S., Promponas, V. J., & Nezis, I. P. (2016) · Autophagy · doi:10.1080/15548627.2016.1207016 · Cited by 183 · see citing works
Combination Therapies with CDK4/6 Inhibitors to Treat <i>KRAS-</i> Mutant Pancreatic Cancer
Goodwin, C. M., Waters, A. M., Klomp, J. E., Javaid, S., Bryant, K. L., Stalnecker, C. A., Drizyte-Miller, K., Papke, B., Yang, R., Amparo, A. M., et al. (2023) · Cancer Research · doi:10.1158/0008-5472.can-22-0391 · Cited by 168 · see citing works
The ubiquitin–proteasome system in kidney physiology and disease
Meyer‐Schwesinger, C. (2019) · Nature Reviews Nephrology · doi:10.1038/s41581-019-0148-1 · Cited by 162 · see citing works
Audesse, A. J., Dhakal, S., Hassell, L.-A., Gardell, Z., Nemtsova, Y., & Webb, A. E. (2019) · PLOS Genetics · doi:10.1371/journal.pgen.1008097 · Cited by 155 · see citing works
Ubiquitin-like and ubiquitin-associated domain proteins: significance in proteasomal degradation
Su, V., & Lau, A. F. (2009) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-009-0048-9 · Cited by 147 · see citing works
Schäffner, I., Minakaki, G., Khan, M. A., Balta, E.-A., Schlötzer-Schrehardt, U., Schwarz, T. J., Beckervordersandforth, R., Winner, B., Webb, A. E., DePinho, R. A., et al. (2018) · Neuron · doi:10.1016/j.neuron.2018.08.017 · Cited by 145 · see citing works
“To further validate impaired autophagic flux and the identity of accumulated autophagy-related structures in FoxO cKO cells, we employed a tandem monomeric mCherry-GFP-tagged LC3 reporter (mCherry/GFP/LC3) (N’Diaye et al., 2009; Pankiv et al., 2007), which takes advantage of the differential pH sensitivity of the mChe…”
Nowosad, A., Jeannot, P., Callot, C., Creff, J., Perchey, R. T., Joffre, C., Codogno, P., Manenti, S., & Besson, A. (2020) · Nature Cell Biology · doi:10.1038/s41556-020-0554-4 · Cited by 144 · see citing works
Mitochondrial-derived vesicles compensate for loss of LC3-mediated mitophagy
Towers, C. G., Wodetzki, D., Thorburn, J., Smith, K. R., Caino, M. C., & Thorburn, A. M. (2021) · Developmental Cell · doi:10.1016/j.devcel.2021.06.003 · Cited by 143 · see citing works
Zummo, F. P., Cullen, K. S., Honkanen‐Scott, M., Shaw, J., Lovat, P. E., & Arden, C. (2017) · Diabetes · doi:10.2337/db16-1009 · Cited by 140 · see citing works
Ubiquilins regulate autophagic flux through mTOR signalling and lysosomal acidification
Şentürk, M., Lin, G., Zuo, Z., Mao, D., Watson, E., Mikos, A. G., & Bellen, H. J. (2019) · Nature Cell Biology · doi:10.1038/s41556-019-0281-x · Cited by 124 · see citing works
Ubiquilin Modifies TDP-43 Toxicity in a Drosophila Model of Amyotrophic Lateral Sclerosis (ALS)
Hanson, K. A., Kim, S. H., Wassarman, D. A., & Tibbetts, R. S. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.c109.078527 · Cited by 128 · see citing works
Genome‐wide siRNA screen reveals amino acid starvation‐induced autophagy requires SCOC and WAC
McKnight, N. C., Jefferies, H. B., Alemu, E. A., Saunders, R., Howell, M., Johansen, T., & Tooze, S. A. (2012) · EMBO Journal · doi:10.1038/emboj.2012.36 · Cited by 118 · see citing works
Interleukin-6 Reduces β-Cell Oxidative Stress by Linking Autophagy With the Antioxidant Response
Marasco, M. R., Conteh, A. M., Reissaus, C. A., Cupit, J. E., Appleman, E. M., Mirmira, R. G., & Linnemann, A. K. (2018) · Diabetes · doi:10.2337/db17-1280 · Cited by 127 · see citing works
Autophagy: links with the proteasome
Lamark, T., & Johansen, T. (2009) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2009.11.002 · Cited by 124 · see citing works
Mechanisms of neuronal homeostasis: Autophagy in the axon
Maday, S. (2016) · Brain Research · doi:10.1016/j.brainres.2016.03.047 · Cited by 123 · see citing works
Zientara‐Rytter, K., & Subramani, S. E. (2019) · Cells · doi:10.3390/cells8010040 · Cited by 122 · see citing works
Tavera-Mendoza, L. E., Westerling, T., Libby, E., Marusyk, A., Cato, L., Cassani, R., Cameron, L., Ficarro, S. B., Marto, J. A., Klawitter, J., et al. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1615015114 · Cited by 124 · see citing works
Nowosad, A., Creff, J., Jeannot, P., Culerrier, R. M., Codogno, P., Manenti, S., Nguyen, L., & Besson, A. (2021) · Cell Death and Disease · doi:10.1038/s41419-021-03759-9 · Cited by 125 · see citing works
Key role of UBQLN2 in pathogenesis of amyotrophic lateral sclerosis and frontotemporal dementia
Renaud, L., Picher‐Martel, V., Codron, P., & Julien, J. (2019) · Acta Neuropathologica Communications · doi:10.1186/s40478-019-0758-7 · Cited by 123 · see citing works
Atg5-Independent Sequestration of Ubiquitinated Mycobacteria
Collins, C. A., Mazière, A. M. G. L. D., van Dijk, S., Carlsson, F., Klumperman, J., & Brown, E. J. (2009) · PLoS Pathogens · doi:10.1371/journal.ppat.1000430 · Cited by 122 · see citing works
Self-citationRegulation of liquid–liquid phase separation with focus on post-translational modifications
Luo, Y.-Y., Wu, J., & Li, Y. (2021) · Chemical Communications · doi:10.1039/d1cc05266g · Cited by 117 · see citing works
Autophagy is essential for oligodendrocyte differentiation, survival, and proper myelination
Bankston, A. N., Forston, M. D., Howard, R. M., Andres, K. R., Smith, A. E., Ohri, S. S., Bates, M. L., Bunge, M. B., & Whittemore, S. R. (2019) · Glia · doi:10.1002/glia.23646 · Cited by 112 · see citing works
Nwadike, C., Williamson, L. E., Gallagher, L. E., Guan, J., & Chan, E. Y. W. (2018) · Molecular and Cellular Biology · doi:10.1128/mcb.00023-18 · Cited by 113 · see citing works
Choi, H., Merceron, C., Mangiavini, L., Seifert, E. L., Schipani, E., Shapiro, I. M., & Risbud, M. V. (2016) · Autophagy · doi:10.1080/15548627.2016.1192753 · Cited by 109 · see citing works
Autophagy as a common pathway in amyotrophic lateral sclerosis
Nguyen, D. K. H., Thombre, R., & Wang, J. (2018) · Neuroscience Letters · doi:10.1016/j.neulet.2018.04.006 · Cited by 110 · see citing works
The IAP family member BRUCE regulates autophagosome–lysosome fusion
Ebner, P., Poetsch, I., Deszcz, L., Hoffmann, T., Zuber, J. A., & Ikeda, F. (2018) · Nature Communications · doi:10.1038/s41467-018-02823-x · Cited by 101 · see citing works
Lundquist, M. R., Goncalves, M. D., Loughran, R. M., Possik, E., Vijayaraghavan, T., Yang, A., Pauli, C., Ravi, A., Verma, A., Yang, Z., et al. (2018) · Molecular Cell · doi:10.1016/j.molcel.2018.03.037 · Cited by 106 · see citing works
Guedes-Dias, P., de Proença, J., Soares, T. R., Leitão-Rocha, A., Pinho, B. R., Duchen, M. R., & Oliveira, J. M. A. (2015) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2015.08.012 · Cited by 104 · see citing works
Bustamante, H., González, A. E., Cerda-Troncoso, C., Shaughnessy, R., Otth, C., Soza, A., & Burgos, P. (2018) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2018.00126 · Cited by 87 · see citing works
Vollrath, J. T., Sechi, A. S., Dreser, A., Katona, I., Wiemuth, D., Vervoorts, J., Dohmen, M., Chandrasekar, A., Prause, J. U., Brauers, E., et al. (2014) · Cell Death and Disease · doi:10.1038/cddis.2014.243 · Cited by 100 · see citing works
Defects in optineurin- and myosin VI-mediated cellular trafficking in amyotrophic lateral sclerosis
Sundaramoorthy, V., Walker, A. K., Tan, V. X., Fifita, J. A., McCann, E. P., Williams, K. L., Blair, I. P., Guillemin, G. J., Farg, M. A., & Atkin, J. D. (2015) · Human Molecular Genetics · doi:10.1093/hmg/ddv126 · Cited by 99 · see citing works
Wu, H., Chen, S., Al-Baadani, A., Xu, J., Wu, Q., Pan, K., Zhang, J., & Hong, Y. (2014) · Molecular Neurobiology · doi:10.1007/s12035-014-8933-0 · Cited by 99 · see citing works
Acosta‐Alvear, D., Cho, M. Y., Wild, T., Buchholz, T. J., Lerner, A. G., Šimáková, O., Hahn, J., Korde, N., Landgren, O., Marić, I., et al. (2015) · eLife · doi:10.7554/elife.08153 · Cited by 94 · see citing works
Autophagy receptor defects and ALS-FTLD
Majcher, V., Goode, A., James, V. H., & Layfield, R. (2015) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2015.01.002 · Cited by 91 · see citing works
Wu, J. J., Cai, A., Greenslade, J. E., Higgins, N. R., Fan, C., Le, N. T. T., Tatman, M., Whiteley, A. M., Prado, M. A., Dieriks, B. V., et al. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1917371117 · Cited by 86 · see citing works
Regulation of GPCR signal networks via membrane trafficking
Jean‐Alphonse, F., & Hanyaloglu, A. C. (2010) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2010.07.010 · Cited by 90 · see citing works
Ubiquilin-1 Is a Molecular Chaperone for the Amyloid Precursor Protein*
Stieren, E. S., Ayadi, A. E., Xiao, Y., Siller, E., Landsverk, M., Oberhauser, A., Barral, J., & Boehning, D. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.243147 · Cited by 93 · see citing works
Targeting SQSTM1/p62 Induces Cargo Loading Failure and Converts Autophagy to Apoptosis via NBK/Bik
Chen, S., Zhou, L., Zhang, Y., Leng, Y., Pei, X.-Y., Lin, H., Jones, R., Orlowski, R. Z., Dai, Y., & Grant, S. (2014) · Molecular and Cellular Biology · doi:10.1128/mcb.01383-13 · Cited by 90 · see citing works
Le, N. T. T., Chang, L., Kovlyagina, I., Georgiou, P., Safren, N., Braunstein, K. E., Kvarta, M. D., Dyke, A. M. V., LeGates, T. A., Philips, T., et al. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1608432113 · Cited by 89 · see citing works
Chen, X., Randles, L., Shi, K., Tarasov, S. G., Aihara, H., & Walters, K. J. (2016) · Structure · doi:10.1016/j.str.2016.05.018 · Cited by 83 · see citing works
Autophagy-induced senescence is regulated by p38α signaling
Slobodnyuk, K., Radic, N., Ivanova, S., Lladó, A., Trempolec, N., Zorzano, A., & Nebreda, Á. R. (2019) · Cell Death and Disease · doi:10.1038/s41419-019-1607-0 · Cited by 85 · see citing works
Eps15: a multifunctional adaptor protein regulating intracellular trafficking
Henegouwen, P. M. P. V. B. E. (2009) · Cell Communication and Signaling · doi:10.1186/1478-811x-7-24 · Cited by 85 · see citing works
CYLD is a causative gene for frontotemporal dementia – amyotrophic lateral sclerosis
Dobson‐Stone, C., Hallupp, M., Shahheydari, H., Ragagnin, A., Chatterton, Z., Carew‐Jones, F., Shepherd, C. E., Stefen, H., Parić, E., Fath, T., et al. (2020) · Brain · doi:10.1093/brain/awaa039 · Cited by 82 · see citing works
Wang, K., Liu, X., Liu, Q., Ho, I. H. T., Wei, X., Yin, T., Zhan, Y., Zhang, W., Zhang, W., Chen, B., et al. (2020) · Cell Death and Disease · doi:10.1038/s41419-020-02880-5 · Cited by 86 · see citing works
HSF1 stress response pathway regulates autophagy receptor SQSTM1/p62-associated proteostasis
Watanabe, Y., Tsujimura, A., Taguchi, K., & Tanaka, M. (2016) · Autophagy · doi:10.1080/15548627.2016.1248018 · Cited by 85 · see citing works
The role of ESCRT proteins in fusion events involving lysosomes, endosomes and autophagosomes
Metcalf, D. J., & Isaacs, A. M. (2010) · Biochemical Society Transactions · doi:10.1042/bst0381469 · Cited by 82 · see citing works
Ubiquilin 1 Promotes IFN-γ-Induced Xenophagy of Mycobacterium tuberculosis
Sakowski, E. T., Köster, S., Portal‐Celhay, C., Park, H. S., Shrestha, E., Hetzenecker, S. E. G., Maurer, K., Cadwell, K., & Philips, J. A. (2015) · PLoS Pathogens · doi:10.1371/journal.ppat.1005076 · Cited by 80 · see citing works
Brohée, L., Peulen, O., Nusgens, B., Castronovo, V., Thiry, M., Colige, A., & Deroanne, C. (2018) · Scientific Reports · doi:10.1038/s41598-018-25340-9 · Cited by 81 · see citing works
Kinsey, C. G., Balakrishnan, V., O’Dell, M. R., Huang, J. L., Newman, L. A., Whitney‐Miller, C. L., Hezel, A. F., & Land, H. (2014) · Cell Reports · doi:10.1016/j.celrep.2014.03.061 · Cited by 80 · see citing works
Lipin-1 regulates cancer cell phenotype and is a potential target to potentiate rapamycin treatment
Brohée, L., Demine, S., Willems, J., Arnould, T., Colige, A., & Deroanne, C. (2015) · Oncotarget · doi:10.18632/oncotarget.3595 · Cited by 77 · see citing works
Autophagy induced during apoptosis degrades mitochondria and inhibits type I interferon secretion
Lindqvist, L., Frank, D. O., McArthur, K., Dite, T. A., Lazarou, M., Oakhill, J. S., Kile, B. T., & Vaux, D. L. (2017) · Cell Death and Differentiation · doi:10.1038/s41418-017-0017-z · Cited by 78 · see citing works
Maurel, C., Dangoumau, A., Marouillat, S., Brulard, C., Chami, A. A., Hergesheimer, R. C., Corcia, P., Blasco, H., Andres, C. R., & Vourc’h, P. (2018) · Molecular Neurobiology · doi:10.1007/s12035-017-0856-0 · Cited by 76 · see citing works
Impairment of Lysosome Function and Autophagy in Rare Neurodegenerative Diseases
Darios, F. D., & Stévanin, G. (2020) · Journal of Molecular Biology · doi:10.1016/j.jmb.2020.02.033 · Cited by 77 · see citing works
Ubiquilin4 is an adaptor protein that recruits Ubiquilin1 to the autophagy machinery
Lee, D. Y., Arnott, D. P., & Brown, E. J. (2013) · EMBO Reports · doi:10.1038/embor.2013.22 · Cited by 78 · see citing works
Self-citationRAD51AP1 Is an Essential Mediator of Alternative Lengthening of Telomeres
González, J. B., García-Expósito, L., Hoang, S. M., Lynskey, M. L., Roncaioli, J. L., Ghosh, A., Wallace, C. T., de Vitis, M., Modesti, M., Bernstein, K. A., et al. (2019) · Molecular Cell · doi:10.1016/j.molcel.2019.06.043 · Cited by 77 · see citing works
Chang, L., & Monteiro, M. J. (2015) · PLoS ONE · doi:10.1371/journal.pone.0130162 · Cited by 77 · see citing works
Selective Autophagy Receptors in Neuronal Health and Disease
Conway, O., Akpinar, H. A., Rogov, V. V., & Kirkin, V. (2020) · Journal of Molecular Biology · doi:10.1016/j.jmb.2019.10.013 · Cited by 75 · see citing works
TBC1D20 mediates autophagy as a key regulator of autophagosome maturation
Sidjanin, D. J., Park, A. K., Ronchetti, A., Martins, J., & Jackson, W. T. (2016) · Autophagy · doi:10.1080/15548627.2016.1199300 · Cited by 76 · see citing works
A nonapoptotic role for CASP2/caspase 2
Tiwari, M., Sharma, L. K., Vanegas, D., Callaway, D. A., Bai, Y., Lechleiter, J. D., & Herman, B. A. (2014) · Autophagy · doi:10.4161/auto.28528 · Cited by 75 · see citing works
Pathogenic Ubqln2 gains toxic properties to induce neuron death
Wu, Q., Liu, M., Huang, C., Liu, X., Huang, B., Li, N., Zhou, H., & Xia, X. (2014) · Acta Neuropathologica · doi:10.1007/s00401-014-1367-y · Cited by 75 · see citing works
Leelamine Mediates Cancer Cell Death through Inhibition of Intracellular Cholesterol Transport
Kuzu, O. F., Gowda, R., Sharma, A. K., & Robertson, G. P. (2014) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-13-0868 · Cited by 75 · see citing works
Ubiquitin receptors and protein quality control
Wang, X., & Terpstra, E. J. M. (2012) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2012.09.012 · Cited by 74 · see citing works
Impaired protein degradation in FTLD and related disorders
Götzl, J. K., Lang, C. M., Haass, C., & Capell, A. (2016) · Ageing Research Reviews · doi:10.1016/j.arr.2016.04.008 · Cited by 70 · see citing works
Modulating cancer cell survival by targeting intracellular cholesterol transport
Kuzu, O. F., Gowda, R., Noory, M. A., & Robertson, G. P. (2017) · British Journal of Cancer · doi:10.1038/bjc.2017.200 · Cited by 73 · see citing works
The ubiquilin gene family: evolutionary patterns and functional insights
Marı́n, I. (2014) · BMC Evolutionary Biology · doi:10.1186/1471-2148-14-63 · Cited by 72 · see citing works
Viswanathan, J., Haapasalo, A., Böttcher, C., Miettinen, R. A., Kurkinen, K. M. A., Lu, A., Thomas, A., Maynard, C. J., Romano, D., Hyman, B. T., et al. (2010) · Traffic · doi:10.1111/j.1600-0854.2010.01149.x · Cited by 70 · see citing works
ALS-associated mutant FUS inhibits macroautophagy which is restored by overexpression of Rab1
Soo, K. Y., Sultana, J. M., King, A. E., Atkinson, R., Warraich, S. T., Sundaramoorthy, V., Blair, I. P., Farg, M. A., & Atkin, J. D. (2015) · Cell Death Discovery · doi:10.1038/cddiscovery.2015.30 · Cited by 71 · see citing works
Activated MLKL attenuates autophagy following its translocation to intracellular membranes
Frank, D. O., Vaux, D. L., Murphy, J. M., Vince, J. E., & Lindqvist, L. (2019) · Journal of Cell Science · doi:10.1242/jcs.220996 · Cited by 69 · see citing works
Beverly, L. J., Lockwood, W. W., Shah, P. P., Erdjument‐Bromage, H., & VARMUS, H. E. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1119167109 · Cited by 70 · see citing works
Guidelines for the use and interpretation of assays for monitoring autophagy (3rd edition)
Klionsky, D. J., Abdelmohsen, K., Abe, A., Abedin, J., Abeliovich, H., Acevedo‐Arozena, A., Adachi, H., Adams, C. M., Adams, P. D., Adeli, K., et al. (2016) · Kölner Universitäts PublikationsServer (Universität zu Köln) · doi:10.5167/uzh-131237 · Cited by 69 · see citing works
Teyssou, E., Chartier, L., Amador, M. D. M., Lam, R., Lautrette, G., Nicol, M., Machat, S., da Barroca, S., Moigneu, C., Mairey, M., et al. (2017) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2017.06.018 · Cited by 67 · see citing works
Li, L., Wang, Y., Jiao, L., Lin, C., Lu, C., Zhang, K., Hu, C., Ye, J., Zhang, D., Wu, H., et al. (2019) · Cancer Letters · doi:10.1016/j.canlet.2019.03.027 · Cited by 67 · see citing works
Cassel, J. A., & Reitz, A. B. (2013) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2013.03.020 · Cited by 65 · see citing works
RNA‐binding proteins in neurodegenerative disease: TDP‐43 and beyond
Hanson, K. A., Kim, S. H., & Tibbetts, R. S. (2011) · Wiley Interdisciplinary Reviews - RNA · doi:10.1002/wrna.111 · Cited by 65 · see citing works
- Authors
- N'Diaye, E., Kajihara, K. K., Hsieh, I., Morisaki, H., Debnath, J., & Brown, E. J.
- Affiliations
- Genentech (US)
- Venue
- The EMBO Reports
- Published
- 2009-01-16
- Volume
- 10
- Issue
- 2
- Pages
- 173-179
- ISSN
- 1469-221X (ISSN-L)
- 1469-3178
- PMC
- PMC2637314
- OpenAlex
- W2144022982
- Cited by
- 323
- References
- 36
- Citations by year
- 2026: 11 · 2025: 14 · 2024: 16 · 2023: 25 · 2022: 20 · 2021: 22 · 2020: 39 · 2019: 25 · 2018: 30 · 2017: 31 · 2016: 22 · 2015: 18 · 2014: 12 · 2013: 12 · 2012: 5
- FWCI
- 5.85
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- EMBO Reports (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Washington University in St. Louis
- National Institutes of Health
- University of California, San Francisco
- 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 › Physiology › Calcium signaling and nucleotide metabolism
- Keywords
- ubiquilin, autophagy, nutrient deprivation, ATG5, ATG7, ubiquitin-associated domain, autophagosome maturation, autophagosome-lysosome fusion, cell survival
- MeSH terms
- Autophagy-Related Proteins, Autophagy-Related Protein 5, Autophagy-Related Protein 7, Animals, Autophagy, Carrier Proteins, Culture Media, HeLa Cells, Humans, Microtubule-Associated Proteins, Phagosomes, Recombinant Fusion Proteins, Ubiquitins, Microscopy, Immunoelectron, Protein Structure, Tertiary, Cell Cycle Proteins, Protein Interaction Mapping, Adaptor Proteins, Vesicular Transport, RNA Interference, RNA, Small Interfering, Ubiquitin-Activating Enzymes, Adaptor Proteins, Signal Transducing, Mice
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