The DOI matches its Crossref record; 7 of the 7 references it cites were found in a registry or an index.
Parkin Facilitates the Elimination of Expanded Polyglutamine Proteins and Leads to Preservation of Proteasome Function
Open accessAbstract
Parkin, the most commonly mutated gene in familial Parkinson's disease, encodes an E3 ubiquitin ligase. A number of candidate substrates have been identified for parkin ubiquitin ligase action including CDCrel-1, o-glycosylated alpha-synuclein, Pael-R, and synphilin-1. We now show that parkin promotes the ubiquitination and degradation of an expanded polyglutamine protein. Overexpression of parkin reduces aggregation and cytotoxicity of an expanded polyglutamine ataxin-3 fragment. Using a cellular proteasome indicator system based on a destabilized form of green fluorescent protein, we demonstrate that parkin reduces proteasome impairment and caspase-12 activation induced by an expanded polyglutamine protein. Parkin forms a complex with the expanded polyglutamine protein, heat shock protein 70 (Hsp70) and the proteasome, which may be important for the elimination of the expanded polyglutamine protein. Hsp70 enhances parkin binding and ubiquitination of expanded polyglutamine protein in vitro suggesting that Hsp70 may help to recruit misfolded proteins as substrates for parkin E3 ubiquitin ligase activity. We speculate that parkin may function to relieve endoplasmic reticulum stress by preserving proteasome activity in the presence of misfolded proteins. Loss of parkin function and the resulting proteasomal impairment may contribute to the accumulation of toxic aberrant proteins in neurodegenerative diseases including Parkinson's disease.
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Cites
Familial Parkinson disease gene product, parkin, is a ubiquitin-protein ligase
Shimura, H., Hattori, N., Kubo, S.-I., Mizuno, Y., Asakawa, S., Minoshima, S., Shimizu, N., Iwai, K., Chiba, T., Tanaka, K., et al. (2000) · Nature Genetics · doi:10.1038/77060 · Cited by 2,024
Chaperone Suppression of α-Synuclein Toxicity in a Drosophila Model for Parkinson's Disease
Auluck, P. K., Chan, H. Y. E., Trojanowski, J. Q., Lee, V. M.-Y., & Bonini, N. M. (2002) · Science · doi:10.1126/science.1067389 · Cited by 1,227
Shimura, H., Schlossmacher, M. G., Hattori, N., Frosch, M. P., Trockenbacher, A., Schneider, R., Mizuno, Y., Kosik, K. S., & Selkoe, D. J. (2001) · Science · doi:10.1126/science.1060627 · Cited by 1,053
Zhang, Y., Gao, J., Chung, K. K. K., Huang, H., Dawson, V. L., & Dawson, T. M. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.240347797 · Cited by 982
Chung, K. K. K., Zhang, Y., Lim, K. L., Tanaka, Y., Huang, H., Gao, J., Ross, C. A., Dawson, V. L., & Dawson, T. M. (2001) · Nature Medicine · doi:10.1038/nm1001-1144 · Cited by 750
Proteasomal function is impaired in substantia nigra in Parkinson’s disease
McNaught, K. S. P., & Jenner, P. (2001) · Neuroscience Letters · doi:10.1016/s0304-3940(00)01701-8 · Cited by 653
CHIP is a chaperone‐dependent E3 ligase that ubiquitylates unfolded protein
Murata, S., Minami, Y., Minami, M., Chiba, T., & Tanaka, K. (2001) · The EMBO Reports · doi:10.1093/embo-reports/kve246 · Cited by 574
Cited by
The Ubiquitin Proteasome System in Neurodegenerative Diseases
Ciechanover, A., & Brundin, P. (2003) · Neuron · doi:10.1016/s0896-6273(03)00606-8 · Cited by 982
Molecular pathways to neurodegeneration
Bossy-Wetzel, E., Schwarzenbacher, R., & Lipton, S. A. (2004) · Nature Medicine · doi:10.1038/nm1067 · Cited by 740
Seibenhener, M. L., Babu, J. R., Geetha, T., Wong, H. C., Krishna, N. R., & Wooten, M. W. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.18.8055-8068.2004 · Cited by 710
Huntington's disease: from pathology and genetics to potential therapies
Imarisio, S., Carmichael, J., Korolchuk, V., Chen, C.-W., Saiki, S., Rose, C., Krishna, G., Davies, J. E., Ttofi, E., Underwood, B. R., et al. (2008) · Biochemical Journal · doi:10.1042/bj20071619 · Cited by 409
Autoregulation of Parkin activity through its ubiquitin‐like domain
Chaugule, V. K., Burchell, L., Barber, K. R., Sidhu, A., Leslie, S. J., Shaw, G. S., & Walden, H. (2011) · The EMBO Journal · doi:10.1038/emboj.2011.204 · Cited by 339
Metadata
- Authors
- Tsai, Y. C., Fishman, P. S., Thakor, N. V., & Oyler, G. A.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2003-06
- Volume
- 278
- Issue
- 24
- Pages
- 22044-22055
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2068806054
- Cited by
- 283
- References
- 7
- FWCI
- 12.84
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Tsai, Y. C., Fishman, P. S., Thakor, N. V., & Oyler, G. A. (2003). Parkin Facilitates the Elimination of Expanded Polyglutamine Proteins and Leads to Preservation of Proteasome Function. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.m212235200
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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