Subnanometre-resolution structure of the doublet microtubule reveals new classes of microtubule-associated proteins

Cilia are hair-like appendages involved in cell motility and sensory reception. Here, the authors report a high resolution cryo-EM structure of the microtubule doublet from motile cilia and identify microtubule inner proteins (MIPs) bound to the inner surface of the doublet that appear to stabilize...

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Autores principales: Muneyoshi Ichikawa, Dinan Liu, Panagiotis L. Kastritis, Kaustuv Basu, Tzu Chin Hsu, Shunkai Yang, Khanh Huy Bui
Formato: article
Lenguaje:EN
Publicado: Nature Portfolio 2017
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Acceso en línea:https://doaj.org/article/c6bf466253ae4a448f152879a69ac15a
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spelling oai:doaj.org-article:c6bf466253ae4a448f152879a69ac15a2021-12-02T14:42:26ZSubnanometre-resolution structure of the doublet microtubule reveals new classes of microtubule-associated proteins10.1038/ncomms150352041-1723https://doaj.org/article/c6bf466253ae4a448f152879a69ac15a2017-05-01T00:00:00Zhttps://doi.org/10.1038/ncomms15035https://doaj.org/toc/2041-1723Cilia are hair-like appendages involved in cell motility and sensory reception. Here, the authors report a high resolution cryo-EM structure of the microtubule doublet from motile cilia and identify microtubule inner proteins (MIPs) bound to the inner surface of the doublet that appear to stabilize its structure.Muneyoshi IchikawaDinan LiuPanagiotis L. KastritisKaustuv BasuTzu Chin HsuShunkai YangKhanh Huy BuiNature PortfolioarticleScienceQENNature Communications, Vol 8, Iss 1, Pp 1-12 (2017)
institution DOAJ
collection DOAJ
language EN
topic Science
Q
spellingShingle Science
Q
Muneyoshi Ichikawa
Dinan Liu
Panagiotis L. Kastritis
Kaustuv Basu
Tzu Chin Hsu
Shunkai Yang
Khanh Huy Bui
Subnanometre-resolution structure of the doublet microtubule reveals new classes of microtubule-associated proteins
description Cilia are hair-like appendages involved in cell motility and sensory reception. Here, the authors report a high resolution cryo-EM structure of the microtubule doublet from motile cilia and identify microtubule inner proteins (MIPs) bound to the inner surface of the doublet that appear to stabilize its structure.
format article
author Muneyoshi Ichikawa
Dinan Liu
Panagiotis L. Kastritis
Kaustuv Basu
Tzu Chin Hsu
Shunkai Yang
Khanh Huy Bui
author_facet Muneyoshi Ichikawa
Dinan Liu
Panagiotis L. Kastritis
Kaustuv Basu
Tzu Chin Hsu
Shunkai Yang
Khanh Huy Bui
author_sort Muneyoshi Ichikawa
title Subnanometre-resolution structure of the doublet microtubule reveals new classes of microtubule-associated proteins
title_short Subnanometre-resolution structure of the doublet microtubule reveals new classes of microtubule-associated proteins
title_full Subnanometre-resolution structure of the doublet microtubule reveals new classes of microtubule-associated proteins
title_fullStr Subnanometre-resolution structure of the doublet microtubule reveals new classes of microtubule-associated proteins
title_full_unstemmed Subnanometre-resolution structure of the doublet microtubule reveals new classes of microtubule-associated proteins
title_sort subnanometre-resolution structure of the doublet microtubule reveals new classes of microtubule-associated proteins
publisher Nature Portfolio
publishDate 2017
url https://doaj.org/article/c6bf466253ae4a448f152879a69ac15a
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