The DOI matches its Crossref record; 7 of the 7 references it cites were found in a registry or an index.
Sumoylation inhibits α-synuclein aggregation and toxicity
Open accessAbstract
Posttranslational modification of proteins by attachment of small ubiquitin-related modifier (SUMO) contributes to numerous cellular phenomena. Sumoylation sometimes creates and abolishes binding interfaces, but increasing evidence points to another role for sumoylation in promoting the solubility of aggregation-prone proteins. Using purified α-synuclein, an aggregation-prone protein implicated in Parkinson’s disease that was previously reported to be sumoylated upon overexpression, we compared the aggregation kinetics of unmodified and modified α-synuclein. Whereas unmodified α-synuclein formed fibrils, modified α-synuclein remained soluble. The presence of as little as 10% sumoylated α-synuclein was sufficient to delay aggregation significantly in vitro. We mapped SUMO acceptor sites in α-synuclein and showed that simultaneous mutation of lysines 96 and 102 to arginine significantly impaired α-synuclein sumoylation in vitro and in cells. Importantly, this double mutant showed increased propensity for aggregation and cytotoxicity in a cell-based assay and increased cytotoxicity in dopaminergic neurons of the substantia nigra in vivo. These findings strongly support the model that sumoylation promotes protein solubility and suggest that defects in sumoylation may contribute to aggregation-induced diseases.
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Cites
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Cited by
Cell Biology and Pathophysiology of α-Synuclein
Burré, J., Sharma, M., & Südhof, T. C. (2018) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a024091 · Cited by 579
The Synaptic Function of α-Synuclein
Burré, J. (2015) · Journal of Parkinson's Disease · doi:10.3233/jpd-150642 · Cited by 573
Physicochemical Properties of Cells and Their Effects on Intrinsically Disordered Proteins (IDPs)
Theillet, F.-X., Binolfi, A., Frembgen-Kesner, T., Hingorani, K., Sarkar, M., Kyne, C., Li, C., Crowley, P. B., Gierasch, L., Pielak, G. J., et al. (2014) · Chemical Reviews · doi:10.1021/cr400695p · Cited by 503
Global quantitative analysis of the human brain proteome in Alzheimer’s and Parkinson’s Disease
Ping, L., Duong, D. M., Yin, L., Gearing, M., Lah, J. J., Levey, A. I., & Seyfried, N. T. (2018) · Scientific Data · doi:10.1038/sdata.2018.36 · Cited by 221
Drisaldi, B., Colnaghi, L., Fioriti, L., Rao, N., Myers, C., Snyder, A. M., Metzger, D. J., Tarasoff, J., Konstantinov, E., Fraser, P. E., et al. (2015) · Cell Reports · doi:10.1016/j.celrep.2015.04.061 · Cited by 120
Metadata
- Authors
- Krumova, P., Meulmeester, E., Garrido, M., Tirard, M., Hsiao, H.-H., Bossis, G., Urlaub, H., Zweckstetter, M., Kügler, S., Melchior, F., Bähr, M., & Weishaupt, J. H.
- Venue
- Journal of Cell Biology
- Publisher
- Rockefeller University Press
- Published
- 2011-07-11
- Volume
- 194
- Issue
- 1
- Pages
- 49-60
- ISSN
- 0021-9525 (ISSN-L)
- 1540-8140
- OpenAlex
- W2139180375
- Cited by
- 254
- References
- 7
- FWCI
- 8.41
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Krumova, P., Meulmeester, E., Garrido, M., Tirard, M., Hsiao, H.-H., Bossis, G., Urlaub, H., Zweckstetter, M., Kügler, S., Melchior, F., Bähr, M., & Weishaupt, J. H. (2011). Sumoylation inhibits α-synuclein aggregation and toxicity. Journal of Cell Biology. https://doi.org/10.1083/jcb.201010117
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