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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Nature Portfolio
2017
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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) |
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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 |
work_keys_str_mv |
AT muneyoshiichikawa subnanometreresolutionstructureofthedoubletmicrotubulerevealsnewclassesofmicrotubuleassociatedproteins AT dinanliu subnanometreresolutionstructureofthedoubletmicrotubulerevealsnewclassesofmicrotubuleassociatedproteins AT panagiotislkastritis subnanometreresolutionstructureofthedoubletmicrotubulerevealsnewclassesofmicrotubuleassociatedproteins AT kaustuvbasu subnanometreresolutionstructureofthedoubletmicrotubulerevealsnewclassesofmicrotubuleassociatedproteins AT tzuchinhsu subnanometreresolutionstructureofthedoubletmicrotubulerevealsnewclassesofmicrotubuleassociatedproteins AT shunkaiyang subnanometreresolutionstructureofthedoubletmicrotubulerevealsnewclassesofmicrotubuleassociatedproteins AT khanhhuybui subnanometreresolutionstructureofthedoubletmicrotubulerevealsnewclassesofmicrotubuleassociatedproteins |
_version_ |
1718389716059947008 |