The DOI matches its Crossref record; 36 of the 36 references it cites were found in a registry or an index.
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 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
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Autophagy as a Regulated Pathway of Cellular Degradation
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The role of autophagy during the early neonatal starvation period
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Impairment of starvation-induced and constitutive autophagy in Atg7 -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
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Homeostatic levels of p62 control cytoplasmic inclusion body formation in autophagy-deficient mice.
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Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death
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Krols, M., Asselbergh, B., De Rycke, R., De Winter, V., Seyer, A., Müller, F.-J., Kurth, I., Bultynck, G., Timmerman, V., & Janssens, S. (2019) · Human Molecular Genetics · doi:10.1093/hmg/ddy352 · Cited by 40
Metadata
- 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
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › 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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