Structural basis for two-way communication between dynein and microtubules

The movement of cytoplasmic dynein on microtubule tracks is coordinated by the microtubule-binding domain (MTBD) and the ATPase domain via a coiled-coil stalk. Here authors use NMR and cryo-EM and suggest that the communication between the ATPase-domain and MTBD is achieved by sliding of the stalk α...

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Auteurs principaux:	Noritaka Nishida, Yuta Komori, Osamu Takarada, Atsushi Watanabe, Satoko Tamura, Satoshi Kubo, Ichio Shimada, Masahide Kikkawa
Format:	article
Langue:	EN
Publié:	Nature Portfolio 2020
Sujets:	Science Q
Accès en ligne:	https://doaj.org/article/d1ea81cf3f6d4a4f9f1f0bbb49e57455
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spelling	oai:doaj.org-article:d1ea81cf3f6d4a4f9f1f0bbb49e574552021-12-02T14:42:46ZStructural basis for two-way communication between dynein and microtubules10.1038/s41467-020-14842-82041-1723https://doaj.org/article/d1ea81cf3f6d4a4f9f1f0bbb49e574552020-02-01T00:00:00Zhttps://doi.org/10.1038/s41467-020-14842-8https://doaj.org/toc/2041-1723The movement of cytoplasmic dynein on microtubule tracks is coordinated by the microtubule-binding domain (MTBD) and the ATPase domain via a coiled-coil stalk. Here authors use NMR and cryo-EM and suggest that the communication between the ATPase-domain and MTBD is achieved by sliding of the stalk α-helix by a half-turn or one-turn.Noritaka NishidaYuta KomoriOsamu TakaradaAtsushi WatanabeSatoko TamuraSatoshi KuboIchio ShimadaMasahide KikkawaNature PortfolioarticleScienceQENNature Communications, Vol 11, Iss 1, Pp 1-11 (2020)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Noritaka Nishida Yuta Komori Osamu Takarada Atsushi Watanabe Satoko Tamura Satoshi Kubo Ichio Shimada Masahide Kikkawa Structural basis for two-way communication between dynein and microtubules
description	The movement of cytoplasmic dynein on microtubule tracks is coordinated by the microtubule-binding domain (MTBD) and the ATPase domain via a coiled-coil stalk. Here authors use NMR and cryo-EM and suggest that the communication between the ATPase-domain and MTBD is achieved by sliding of the stalk α-helix by a half-turn or one-turn.
format	article
author	Noritaka Nishida Yuta Komori Osamu Takarada Atsushi Watanabe Satoko Tamura Satoshi Kubo Ichio Shimada Masahide Kikkawa
author_facet	Noritaka Nishida Yuta Komori Osamu Takarada Atsushi Watanabe Satoko Tamura Satoshi Kubo Ichio Shimada Masahide Kikkawa
author_sort	Noritaka Nishida
title	Structural basis for two-way communication between dynein and microtubules
title_short	Structural basis for two-way communication between dynein and microtubules
title_full	Structural basis for two-way communication between dynein and microtubules
title_fullStr	Structural basis for two-way communication between dynein and microtubules
title_full_unstemmed	Structural basis for two-way communication between dynein and microtubules
title_sort	structural basis for two-way communication between dynein and microtubules
publisher	Nature Portfolio
publishDate	2020
url	https://doaj.org/article/d1ea81cf3f6d4a4f9f1f0bbb49e57455
work_keys_str_mv	AT noritakanishida structuralbasisfortwowaycommunicationbetweendyneinandmicrotubules AT yutakomori structuralbasisfortwowaycommunicationbetweendyneinandmicrotubules AT osamutakarada structuralbasisfortwowaycommunicationbetweendyneinandmicrotubules AT atsushiwatanabe structuralbasisfortwowaycommunicationbetweendyneinandmicrotubules AT satokotamura structuralbasisfortwowaycommunicationbetweendyneinandmicrotubules AT satoshikubo structuralbasisfortwowaycommunicationbetweendyneinandmicrotubules AT ichioshimada structuralbasisfortwowaycommunicationbetweendyneinandmicrotubules AT masahidekikkawa structuralbasisfortwowaycommunicationbetweendyneinandmicrotubules
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Structural basis for two-way communication between dynein and microtubules

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