Ubiqutination via K27 and K29 chains signals aggregation and neuronal protection of LRRK2 by WSB1

Mutations in LRRK2 are linked to Parkinson’s Disease. Here, the authors identify WSB1 as a LRRK2 interacting protein and find that it promotes LRRK2 aggregation in primary neurons and drosophila models via ubiquitin K27 and K29 linkages.

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Autores principales:	Frederick C. Nucifora, Leslie G. Nucifora, Chee-Hoe Ng, Nicolas Arbez, Yajuan Guo, Elaine Roby, Vered Shani, Simone Engelender, Dong Wei, Xiao-Fang Wang, Tianxia Li, Darren J. Moore, Olga Pletnikova, Juan C. Troncoso, Akira Sawa, Ted M. Dawson, Wanli Smith, Kah-Leong Lim, Christopher A. Ross
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2016
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/0422154ec8e94aaeacb24bc6f49b8afd
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spelling	oai:doaj.org-article:0422154ec8e94aaeacb24bc6f49b8afd2021-12-02T15:33:48ZUbiqutination via K27 and K29 chains signals aggregation and neuronal protection of LRRK2 by WSB110.1038/ncomms117922041-1723https://doaj.org/article/0422154ec8e94aaeacb24bc6f49b8afd2016-06-01T00:00:00Zhttps://doi.org/10.1038/ncomms11792https://doaj.org/toc/2041-1723Mutations in LRRK2 are linked to Parkinson’s Disease. Here, the authors identify WSB1 as a LRRK2 interacting protein and find that it promotes LRRK2 aggregation in primary neurons and drosophila models via ubiquitin K27 and K29 linkages.Frederick C. NuciforaLeslie G. NuciforaChee-Hoe NgNicolas ArbezYajuan GuoElaine RobyVered ShaniSimone EngelenderDong WeiXiao-Fang WangTianxia LiDarren J. MooreOlga PletnikovaJuan C. TroncosoAkira SawaTed M. DawsonWanli SmithKah-Leong LimChristopher A. RossNature PortfolioarticleScienceQENNature Communications, Vol 7, Iss 1, Pp 1-11 (2016)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Frederick C. Nucifora Leslie G. Nucifora Chee-Hoe Ng Nicolas Arbez Yajuan Guo Elaine Roby Vered Shani Simone Engelender Dong Wei Xiao-Fang Wang Tianxia Li Darren J. Moore Olga Pletnikova Juan C. Troncoso Akira Sawa Ted M. Dawson Wanli Smith Kah-Leong Lim Christopher A. Ross Ubiqutination via K27 and K29 chains signals aggregation and neuronal protection of LRRK2 by WSB1
description	Mutations in LRRK2 are linked to Parkinson’s Disease. Here, the authors identify WSB1 as a LRRK2 interacting protein and find that it promotes LRRK2 aggregation in primary neurons and drosophila models via ubiquitin K27 and K29 linkages.
format	article
author	Frederick C. Nucifora Leslie G. Nucifora Chee-Hoe Ng Nicolas Arbez Yajuan Guo Elaine Roby Vered Shani Simone Engelender Dong Wei Xiao-Fang Wang Tianxia Li Darren J. Moore Olga Pletnikova Juan C. Troncoso Akira Sawa Ted M. Dawson Wanli Smith Kah-Leong Lim Christopher A. Ross
author_facet	Frederick C. Nucifora Leslie G. Nucifora Chee-Hoe Ng Nicolas Arbez Yajuan Guo Elaine Roby Vered Shani Simone Engelender Dong Wei Xiao-Fang Wang Tianxia Li Darren J. Moore Olga Pletnikova Juan C. Troncoso Akira Sawa Ted M. Dawson Wanli Smith Kah-Leong Lim Christopher A. Ross
author_sort	Frederick C. Nucifora
title	Ubiqutination via K27 and K29 chains signals aggregation and neuronal protection of LRRK2 by WSB1
title_short	Ubiqutination via K27 and K29 chains signals aggregation and neuronal protection of LRRK2 by WSB1
title_full	Ubiqutination via K27 and K29 chains signals aggregation and neuronal protection of LRRK2 by WSB1
title_fullStr	Ubiqutination via K27 and K29 chains signals aggregation and neuronal protection of LRRK2 by WSB1
title_full_unstemmed	Ubiqutination via K27 and K29 chains signals aggregation and neuronal protection of LRRK2 by WSB1
title_sort	ubiqutination via k27 and k29 chains signals aggregation and neuronal protection of lrrk2 by wsb1
publisher	Nature Portfolio
publishDate	2016
url	https://doaj.org/article/0422154ec8e94aaeacb24bc6f49b8afd
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Ubiqutination via K27 and K29 chains signals aggregation and neuronal protection of LRRK2 by WSB1

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