The DOI matches its Crossref record; 7 of the 7 references it cites were found in a registry or an index.
Aggregate formation inhibits proteasomal degradation of polyglutamine proteins
Abstract
Insoluble protein aggregates are consistently found in neurodegenerative disorders caused by expanded polyglutamine [poly(Q)] repeats. The aggregates contain various components of the ubiquitin/proteasome system, suggesting an attempt of the cell to clear the aberrant substrate. To investigate the effect of expanded poly(Q) repeats on ubiquitin/proteasome-dependent proteolysis, we targeted these proteins for proteasomal degradation by the introduction of an N-end rule degradation signal. While soluble poly(Q) proteins were degraded, they resisted proteasomal degradation once present in the aggregates. Stabilization was also observed for proteins that are co-aggregated via interaction with the expanded poly(Q) domain. Introduction of a degradation signal in ataxin-1/Q92 reduced the incidence of nuclear inclusions and the cellular toxicity, conceivably by accelerating the clearance of the soluble substrate.
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Cites
Sakamoto, K. M., Kim, K. B., Kumagai, A., Mercurio, F., Crews, C. M., & Deshaies, R. J. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.141230798 · Cited by 2,609
Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases
Bucciantini, M., Giannoni, E., Chiti, F., Baroni, F., Formigli, L., Zurdo, J., Taddei, N., Ramponi, G., Dobson, C. M., & Stefani, M. (2002) · Nature · doi:10.1038/416507a · Cited by 2,434
Aggresomes: A Cellular Response to Misfolded Proteins
Johnston, J. A., Ward, C. L., & Kopito, R. R. (1998) · The Journal of Cell Biology · doi:10.1083/jcb.143.7.1883 · Cited by 2,148
Histone deacetylase inhibitors arrest polyglutamine-dependent neurodegeneration in Drosophila
Steffan, J. S., Bodai, L., Pallos, J., Poelman, M., McCampbell, A., Apostol, B. L., Kazantsev, A., Schmidt, E., Zhu, Y.-Z., Greenwald, M., et al. (2001) · Nature · doi:10.1038/35099568 · Cited by 1,228 · cited 1×
“Among these are important regulators such as the CREB-binding protein (31) and the TATA-binding protein (42), which have been proposed as mediators of the neuronal toxicity observed in aggregate-containing cells ( 43 ).”
BackgroundThe N-end rule: functions, mysteries, uses
Varshavsky, A. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.22.12142 · Cited by 859
Cause of neural death in neurodegenerative diseases attributable to expansion of glutamine repeats
Perutz, M. F., & Windle, A. H. (2001) · Nature · doi:10.1038/35084141 · Cited by 199
Harnessing the Ubiquitination Machinery to Target the Degradation of Specific Cellular Proteins
Zhou, P., Bogacki, R., McReynolds, L., & Howley, P. M. (2000) · Molecular Cell · doi:10.1016/s1097-2765(00)00074-5 · Cited by 164
Cited by
Protein aggregation and neurodegenerative disease
Ross, C. A., & Poirier, M. A. (2004) · Nature Medicine · doi:10.1038/nm1066 · Cited by 3,454
The roles of intracellular protein-degradation pathways in neurodegeneration
Rubinsztein, D. C. (2006) · Nature · doi:10.1038/nature05291 · Cited by 1,625
α-Synuclein Is Degraded by Both Autophagy and the Proteasome
Webb, J. L., Ravikumar, B., Atkins, J., Skepper, J. N., & Rubinsztein, D. C. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m300227200 · Cited by 1,429
Cargo recognition and degradation by selective autophagy
Gatica, D., Lahiri, V., & Klionsky, D. J. (2018) · Nature Cell Biology · doi:10.1038/s41556-018-0037-z · Cited by 1,067
The Ubiquitin Proteasome System in Neurodegenerative Diseases
Ciechanover, A., & Brundin, P. (2003) · Neuron · doi:10.1016/s0896-6273(03)00606-8 · Cited by 982
Metadata
- Authors
- Verhoef, L. G. G. C.
- Venue
- Human Molecular Genetics
- Publisher
- Oxford University Press (OUP)
- Published
- 2002-10-15
- Volume
- 11
- Issue
- 22
- Pages
- 2689-2700
- ISSN
- 0964-6906 (ISSN-L)
- 1460-2083
- OpenAlex
- W2141871877
- Cited by
- 292
- References
- 7
- FWCI
- 5.52
- Type
- journal article
- Language
- en
- Open access
- closed
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- Verhoef, L. G. G. C. (2002). Aggregate formation inhibits proteasomal degradation of polyglutamine proteins. Human Molecular Genetics. https://doi.org/10.1093/hmg/11.22.2689
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
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.
