She1 affects dynein through direct interactions with the microtubule and the dynein microtubule-binding domain

Dynein is a microtubule motor the motility of which is affected by the microtubule-associated protein She1. Here, the authors show that She1 alters dynein stepping behavior and increases its microtubule affinity through simultaneous interactions with the microtubule and dynein microtubule binding do...

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Autores principales:	Kari H. Ecklund, Tatsuya Morisaki, Lindsay G. Lammers, Matthew G. Marzo, Timothy J. Stasevich, Steven M. Markus
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/913bdefabfaa49f98b3f7aa602394933
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spelling	oai:doaj.org-article:913bdefabfaa49f98b3f7aa6023949332021-12-02T15:39:06ZShe1 affects dynein through direct interactions with the microtubule and the dynein microtubule-binding domain10.1038/s41467-017-02004-22041-1723https://doaj.org/article/913bdefabfaa49f98b3f7aa6023949332017-12-01T00:00:00Zhttps://doi.org/10.1038/s41467-017-02004-2https://doaj.org/toc/2041-1723Dynein is a microtubule motor the motility of which is affected by the microtubule-associated protein She1. Here, the authors show that She1 alters dynein stepping behavior and increases its microtubule affinity through simultaneous interactions with the microtubule and dynein microtubule binding domain.Kari H. EcklundTatsuya MorisakiLindsay G. LammersMatthew G. MarzoTimothy J. StasevichSteven M. MarkusNature PortfolioarticleScienceQENNature Communications, Vol 8, Iss 1, Pp 1-16 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Kari H. Ecklund Tatsuya Morisaki Lindsay G. Lammers Matthew G. Marzo Timothy J. Stasevich Steven M. Markus She1 affects dynein through direct interactions with the microtubule and the dynein microtubule-binding domain
description	Dynein is a microtubule motor the motility of which is affected by the microtubule-associated protein She1. Here, the authors show that She1 alters dynein stepping behavior and increases its microtubule affinity through simultaneous interactions with the microtubule and dynein microtubule binding domain.
format	article
author	Kari H. Ecklund Tatsuya Morisaki Lindsay G. Lammers Matthew G. Marzo Timothy J. Stasevich Steven M. Markus
author_facet	Kari H. Ecklund Tatsuya Morisaki Lindsay G. Lammers Matthew G. Marzo Timothy J. Stasevich Steven M. Markus
author_sort	Kari H. Ecklund
title	She1 affects dynein through direct interactions with the microtubule and the dynein microtubule-binding domain
title_short	She1 affects dynein through direct interactions with the microtubule and the dynein microtubule-binding domain
title_full	She1 affects dynein through direct interactions with the microtubule and the dynein microtubule-binding domain
title_fullStr	She1 affects dynein through direct interactions with the microtubule and the dynein microtubule-binding domain
title_full_unstemmed	She1 affects dynein through direct interactions with the microtubule and the dynein microtubule-binding domain
title_sort	she1 affects dynein through direct interactions with the microtubule and the dynein microtubule-binding domain
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/913bdefabfaa49f98b3f7aa602394933
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She1 affects dynein through direct interactions with the microtubule and the dynein microtubule-binding domain

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