Please use this identifier to cite or link to this item: https://doi.org/10.1038/ncomms11792
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dc.titleUbiqutination via K27 and K29 chains signals aggregation and neuronal protection of LRRK2 by WSB1
dc.contributor.authorNucifora F.C.
dc.contributor.authorNucifora L.G.
dc.contributor.authorNg C.-H.
dc.contributor.authorArbez N.
dc.contributor.authorGuo Y.
dc.contributor.authorRoby E.
dc.contributor.authorShani V.
dc.contributor.authorEngelender S.
dc.contributor.authorWei D.
dc.contributor.authorWang X.-F.
dc.contributor.authorLi T.
dc.contributor.authorMoore D.J.
dc.contributor.authorPletnikova O.
dc.contributor.authorTroncoso J.C.
dc.contributor.authorSawa A.
dc.contributor.authorDawson T.M.
dc.contributor.authorSmith W.
dc.contributor.authorLim K.-L.
dc.contributor.authorRoss C.A.
dc.date.accessioned2018-12-20T08:16:31Z
dc.date.available2018-12-20T08:16:31Z
dc.date.issued2016
dc.identifier.citationNucifora 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.issn20411723
dc.identifier.urihttp://scholarbank.nus.edu.sg/handle/10635/150086
dc.description.abstractA 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.publisherNature Publishing Group
dc.sourceScopus
dc.typeArticle
dc.contributor.departmentDEPT OF PHYSIOLOGY
dc.description.doi10.1038/ncomms11792
dc.description.sourcetitleNat. Commun.
dc.description.volume7
dc.description.page11792
dc.published.statepublished
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