The ataxin-1 interactome reveals direct connection with multiple disrupted nuclear transport pathways

Patients with spinocerebellar ataxia type 1 express ataxin-1 with an extended polyglutamine (polyQ) tract that forms distinctive nuclear bodies. Here, the authors characterize the cellular pathways affected by polyQ-ataxin-1, showing that it disrupts multiple nuclear transport processes.

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Autores principales:	Sunyuan Zhang, Nicholas A. Williamson, Lisa Duvick, Alexander Lee, Harry T. Orr, Austin Korlin-Downs, Praseuth Yang, Yee-Foong Mok, David A. Jans, Marie A. Bogoyevitch
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2020
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/b2b32690cddc4b05a5d62aa6d6b893b2
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id	oai:doaj.org-article:b2b32690cddc4b05a5d62aa6d6b893b2
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spelling	oai:doaj.org-article:b2b32690cddc4b05a5d62aa6d6b893b22021-12-02T16:13:39ZThe ataxin-1 interactome reveals direct connection with multiple disrupted nuclear transport pathways10.1038/s41467-020-17145-02041-1723https://doaj.org/article/b2b32690cddc4b05a5d62aa6d6b893b22020-07-01T00:00:00Zhttps://doi.org/10.1038/s41467-020-17145-0https://doaj.org/toc/2041-1723Patients with spinocerebellar ataxia type 1 express ataxin-1 with an extended polyglutamine (polyQ) tract that forms distinctive nuclear bodies. Here, the authors characterize the cellular pathways affected by polyQ-ataxin-1, showing that it disrupts multiple nuclear transport processes.Sunyuan ZhangNicholas A. WilliamsonLisa DuvickAlexander LeeHarry T. OrrAustin Korlin-DownsPraseuth YangYee-Foong MokDavid A. JansMarie A. BogoyevitchNature PortfolioarticleScienceQENNature Communications, Vol 11, Iss 1, Pp 1-16 (2020)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Sunyuan Zhang Nicholas A. Williamson Lisa Duvick Alexander Lee Harry T. Orr Austin Korlin-Downs Praseuth Yang Yee-Foong Mok David A. Jans Marie A. Bogoyevitch The ataxin-1 interactome reveals direct connection with multiple disrupted nuclear transport pathways
description	Patients with spinocerebellar ataxia type 1 express ataxin-1 with an extended polyglutamine (polyQ) tract that forms distinctive nuclear bodies. Here, the authors characterize the cellular pathways affected by polyQ-ataxin-1, showing that it disrupts multiple nuclear transport processes.
format	article
author	Sunyuan Zhang Nicholas A. Williamson Lisa Duvick Alexander Lee Harry T. Orr Austin Korlin-Downs Praseuth Yang Yee-Foong Mok David A. Jans Marie A. Bogoyevitch
author_facet	Sunyuan Zhang Nicholas A. Williamson Lisa Duvick Alexander Lee Harry T. Orr Austin Korlin-Downs Praseuth Yang Yee-Foong Mok David A. Jans Marie A. Bogoyevitch
author_sort	Sunyuan Zhang
title	The ataxin-1 interactome reveals direct connection with multiple disrupted nuclear transport pathways
title_short	The ataxin-1 interactome reveals direct connection with multiple disrupted nuclear transport pathways
title_full	The ataxin-1 interactome reveals direct connection with multiple disrupted nuclear transport pathways
title_fullStr	The ataxin-1 interactome reveals direct connection with multiple disrupted nuclear transport pathways
title_full_unstemmed	The ataxin-1 interactome reveals direct connection with multiple disrupted nuclear transport pathways
title_sort	ataxin-1 interactome reveals direct connection with multiple disrupted nuclear transport pathways
publisher	Nature Portfolio
publishDate	2020
url	https://doaj.org/article/b2b32690cddc4b05a5d62aa6d6b893b2
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The ataxin-1 interactome reveals direct connection with multiple disrupted nuclear transport pathways

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