Please use this identifier to cite or link to this item:
https://doi.org/10.1038/ncomms11792
DC Field | Value | |
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dc.title | Ubiqutination via K27 and K29 chains signals aggregation and neuronal protection of LRRK2 by WSB1 | |
dc.contributor.author | Nucifora F.C. | |
dc.contributor.author | Nucifora L.G. | |
dc.contributor.author | Ng C.-H. | |
dc.contributor.author | Arbez N. | |
dc.contributor.author | Guo Y. | |
dc.contributor.author | Roby E. | |
dc.contributor.author | Shani V. | |
dc.contributor.author | Engelender S. | |
dc.contributor.author | Wei D. | |
dc.contributor.author | Wang X.-F. | |
dc.contributor.author | Li T. | |
dc.contributor.author | Moore D.J. | |
dc.contributor.author | Pletnikova O. | |
dc.contributor.author | Troncoso J.C. | |
dc.contributor.author | Sawa A. | |
dc.contributor.author | Dawson T.M. | |
dc.contributor.author | Smith W. | |
dc.contributor.author | Lim K.-L. | |
dc.contributor.author | Ross C.A. | |
dc.date.accessioned | 2018-12-20T08:16:31Z | |
dc.date.available | 2018-12-20T08:16:31Z | |
dc.date.issued | 2016 | |
dc.identifier.citation | Nucifora F.C., Nucifora L.G., Ng C.-H., Arbez N., Guo Y., Roby E., Shani V., Engelender S., Wei D., Wang X.-F., Li T., Moore D.J., Pletnikova O., Troncoso J.C., Sawa A., Dawson T.M., Smith W., Lim K.-L., Ross C.A. (2016). Ubiqutination via K27 and K29 chains signals aggregation and neuronal protection of LRRK2 by WSB1. Nat. Commun. 7 : 11792. ScholarBank@NUS Repository. https://doi.org/10.1038/ncomms11792 | |
dc.identifier.issn | 20411723 | |
dc.identifier.uri | http://scholarbank.nus.edu.sg/handle/10635/150086 | |
dc.description.abstract | A common genetic form of Parkinson's disease (PD) is caused by mutations in LRRK2. We identify WSB1 as a LRRK2 interacting protein. WSB1 ubiquitinates LRRK2 through K27 and K29 linkage chains, leading to LRRK2 aggregation and neuronal protection in primary neurons and a Drosophila model of G2019S LRRK2. Knocking down endogenous WSB1 exacerbates mutant LRRK2 neuronal toxicity in neurons and the Drosophila model, indicating a role for endogenous WSB1 in modulating LRRK2 cell toxicity. WSB1 is in Lewy bodies in human PD post-mortem tissue. These data demonstrate a role for WSB1 in mutant LRRK2 pathogenesis, and suggest involvement in Lewy body pathology in sporadic PD. Our data indicate a role in PD for ubiquitin K27 and K29 linkages, and suggest that ubiquitination may be a signal for aggregation and neuronal protection in PD, which may be relevant for other neurodegenerative disorders. Finally, our study identifies a novel therapeutic target for PD. | |
dc.publisher | Nature Publishing Group | |
dc.source | Scopus | |
dc.type | Article | |
dc.contributor.department | PHYSIOLOGY | |
dc.description.doi | 10.1038/ncomms11792 | |
dc.description.sourcetitle | Nat. Commun. | |
dc.description.volume | 7 | |
dc.description.page | 11792 | |
dc.published.state | published | |
Appears in Collections: | Staff Publications Elements |
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