The cryo-EM structure of a γ-TuSC elucidates architecture and regulation of minimal microtubule nucleation systems

The nucleation of microtubules from αβ-tubulin subunits is mediated by γtubulin complexes, which vary in composition across organisms. Here, authors present the cryo-EM structure of the heterotetrameric γ-tubulin small complex (γ-TuSC) from C. albicans at near-atomic resolution.

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Autores principales:	Erik Zupa, Anjun Zheng, Annett Neuner, Martin Würtz, Peng Liu, Anna Böhler, Elmar Schiebel, Stefan Pfeffer
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2020
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/c3b177b1e448457da20ea32c914c464f
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spelling	oai:doaj.org-article:c3b177b1e448457da20ea32c914c464f2021-12-02T14:40:41ZThe cryo-EM structure of a γ-TuSC elucidates architecture and regulation of minimal microtubule nucleation systems10.1038/s41467-020-19456-82041-1723https://doaj.org/article/c3b177b1e448457da20ea32c914c464f2020-11-01T00:00:00Zhttps://doi.org/10.1038/s41467-020-19456-8https://doaj.org/toc/2041-1723The nucleation of microtubules from αβ-tubulin subunits is mediated by γtubulin complexes, which vary in composition across organisms. Here, authors present the cryo-EM structure of the heterotetrameric γ-tubulin small complex (γ-TuSC) from C. albicans at near-atomic resolution.Erik ZupaAnjun ZhengAnnett NeunerMartin WürtzPeng LiuAnna BöhlerElmar SchiebelStefan PfefferNature PortfolioarticleScienceQENNature Communications, Vol 11, Iss 1, Pp 1-12 (2020)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Erik Zupa Anjun Zheng Annett Neuner Martin Würtz Peng Liu Anna Böhler Elmar Schiebel Stefan Pfeffer The cryo-EM structure of a γ-TuSC elucidates architecture and regulation of minimal microtubule nucleation systems
description	The nucleation of microtubules from αβ-tubulin subunits is mediated by γtubulin complexes, which vary in composition across organisms. Here, authors present the cryo-EM structure of the heterotetrameric γ-tubulin small complex (γ-TuSC) from C. albicans at near-atomic resolution.
format	article
author	Erik Zupa Anjun Zheng Annett Neuner Martin Würtz Peng Liu Anna Böhler Elmar Schiebel Stefan Pfeffer
author_facet	Erik Zupa Anjun Zheng Annett Neuner Martin Würtz Peng Liu Anna Böhler Elmar Schiebel Stefan Pfeffer
author_sort	Erik Zupa
title	The cryo-EM structure of a γ-TuSC elucidates architecture and regulation of minimal microtubule nucleation systems
title_short	The cryo-EM structure of a γ-TuSC elucidates architecture and regulation of minimal microtubule nucleation systems
title_full	The cryo-EM structure of a γ-TuSC elucidates architecture and regulation of minimal microtubule nucleation systems
title_fullStr	The cryo-EM structure of a γ-TuSC elucidates architecture and regulation of minimal microtubule nucleation systems
title_full_unstemmed	The cryo-EM structure of a γ-TuSC elucidates architecture and regulation of minimal microtubule nucleation systems
title_sort	cryo-em structure of a γ-tusc elucidates architecture and regulation of minimal microtubule nucleation systems
publisher	Nature Portfolio
publishDate	2020
url	https://doaj.org/article/c3b177b1e448457da20ea32c914c464f
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The cryo-EM structure of a γ-TuSC elucidates architecture and regulation of minimal microtubule nucleation systems

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