The DOI matches its Crossref record; 17 of the 17 references it cites were found in a registry or an index.
Ubiquitin accumulation in autophagy-deficient mice is dependent on the Nrf2-mediated stress response pathway: a potential role for protein aggregation in autophagic substrate selection
Open accessAbstract
Genetic ablation of autophagy in mice leads to liver and brain degeneration accompanied by the appearance of ubiquitin (Ub) inclusions, which has been considered to support the hypothesis that ubiquitination serves as a cis-acting signal for selective autophagy. We show that tissue-specific disruption of the essential autophagy genes Atg5 and Atg7 leads to the accumulation of all detectable Ub–Ub topologies, arguing against the hypothesis that any particular Ub linkage serves as a specific autophagy signal. The increase in Ub conjugates in Atg7−/− liver and brain is completely suppressed by simultaneous knockout of either p62 or Nrf2. We exploit a novel assay for selective autophagy in cell culture, which shows that inactivation of Atg5 leads to the selective accumulation of aggregation-prone proteins, and this does not correlate with an increase in substrate ubiquitination. We propose that protein oligomerization drives autophagic substrate selection and that the accumulation of poly-Ub chains in autophagy-deficient circumstances is an indirect consequence of activation of Nrf2-dependent stress response pathways.
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Cites
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“Thus, the presence of both the LC3 recognition sequence and UBA domains in p62 has suggested a model in which p62 serves as an adaptor that recruits ubiquitinated proteins to autophagosomes (Bjørkøy et al., 2005; Pankiv et al., 2007; Kirkin et al., 2009a; Lamark et al., 2009).”
BackgroundSuppression 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
Self-citationLoss 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
Self-citationProtein aggregation and neurodegenerative disease
Ross, C. A., & Poirier, M. A. (2004) · Nature Medicine · doi:10.1038/nm1066 · Cited by 3,454
Absolute quantification of proteins and phosphoproteins from cell lysates by tandem MS
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A multiubiquitin chain is confined to specific lysine in a targeted short-lived protein
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Cited by
The KEAP1-NRF2 system: a thiol-based sensor-effector apparatus for maintaining redox homeostasis
Yamamoto, M., Kensler, T. W., & Motohashi, H. (2018) · Physiological Reviews · doi:10.1152/physrev.00023.2017 · Cited by 1,968
Self-citationAutophagy, mitochondria and oxidative stress: cross-talk and redox signalling.
Lee, J., Giordano, S., & Zhang, J. (2012) · Biochemical Journal · doi:10.1042/bj20111451 · Cited by 1,438
Degradation of misfolded proteins in neurodegenerative diseases: Therapeutic targets and strategies
Ciechanover, A., & Kwon, Y. T. (2015) · Experimental & Molecular Medicine · doi:10.1038/emm.2014.117 · Cited by 898
ROS and Autophagy: Interactions and Molecular Regulatory Mechanisms
Li, L., Tan, J., Miao, Y., Lei, P., & Zhang, Q. (2015) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-015-0166-x · Cited by 876
Stimulation of autophagy reduces neurodegeneration in a mouse model of human tauopathy
Schaeffer, V., Lavenir, I., Ozcelik, S., Tolnay, M., Winkler, D. T., & Goedert, M. (2012) · Brain · doi:10.1093/brain/aws143 · Cited by 343
Metadata
- Authors
- Riley, B. E., Kaiser, S. E., Shaler, T. A., Ng, A. C. Y., Hara, T., Hipp, M. S., Lage, K., Xavier, R. J., Ryu, K.-Y., Taguchi, K., Yamamoto, M., Tanaka, K., Mizushima, N., Komatsu, M., & Kopito, R. R.
- Venue
- Journal of Cell Biology
- Publisher
- Rockefeller University Press
- Published
- 2010-11-01
- Volume
- 191
- Issue
- 3
- Pages
- 537-552
- ISSN
- 0021-9525 (ISSN-L)
- 1540-8140
- OpenAlex
- W2126118460
- Cited by
- 161
- References
- 17
- FWCI
- 10.69
- Type
- journal article
- Language
- en
- Open access
- bronze
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- CoChat. (2026). Citation check: Ubiquitin accumulation in autophagy-deficient mice is dependent on the Nrf2-mediated stress response pathway: a potential role for protein aggregation in autophagic substrate selection. https://app.cochat.ai/papers/10.1083/jcb.201005012
- The paper
- Riley, B. E., Kaiser, S. E., Shaler, T. A., Ng, A. C. Y., Hara, T., Hipp, M. S., Lage, K., Xavier, R. J., Ryu, K.-Y., Taguchi, K., Yamamoto, M., Tanaka, K., Mizushima, N., Komatsu, M., & Kopito, R. R. (2010). Ubiquitin accumulation in autophagy-deficient mice is dependent on the Nrf2-mediated stress response pathway: a potential role for protein aggregation in autophagic substrate selection. Journal of Cell Biology. https://doi.org/10.1083/jcb.201005012
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
