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The contribution of αβ-tubulin curvature to microtubule dynamics
Microtubules are dynamic polymers of αβ-tubulin that form diverse cellular structures, such as the mitotic spindle for cell division, the backbone of neurons, and axonemes. To control the architecture of microtubule networks, microtubule-associated proteins (MAPs) and motor proteins regulate microtu...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The Rockefeller University Press
2014
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4226729/ https://www.ncbi.nlm.nih.gov/pubmed/25385183 http://dx.doi.org/10.1083/jcb.201407095 |
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author | Brouhard, Gary J. Rice, Luke M. |
author_facet | Brouhard, Gary J. Rice, Luke M. |
author_sort | Brouhard, Gary J. |
collection | PubMed |
description | Microtubules are dynamic polymers of αβ-tubulin that form diverse cellular structures, such as the mitotic spindle for cell division, the backbone of neurons, and axonemes. To control the architecture of microtubule networks, microtubule-associated proteins (MAPs) and motor proteins regulate microtubule growth, shrinkage, and the transitions between these states. Recent evidence shows that many MAPs exert their effects by selectively binding to distinct conformations of polymerized or unpolymerized αβ-tubulin. The ability of αβ-tubulin to adopt distinct conformations contributes to the intrinsic polymerization dynamics of microtubules. αβ-Tubulin conformation is a fundamental property that MAPs monitor and control to build proper microtubule networks. |
format | Online Article Text |
id | pubmed-4226729 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2014 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-42267292015-05-10 The contribution of αβ-tubulin curvature to microtubule dynamics Brouhard, Gary J. Rice, Luke M. J Cell Biol Reviews Microtubules are dynamic polymers of αβ-tubulin that form diverse cellular structures, such as the mitotic spindle for cell division, the backbone of neurons, and axonemes. To control the architecture of microtubule networks, microtubule-associated proteins (MAPs) and motor proteins regulate microtubule growth, shrinkage, and the transitions between these states. Recent evidence shows that many MAPs exert their effects by selectively binding to distinct conformations of polymerized or unpolymerized αβ-tubulin. The ability of αβ-tubulin to adopt distinct conformations contributes to the intrinsic polymerization dynamics of microtubules. αβ-Tubulin conformation is a fundamental property that MAPs monitor and control to build proper microtubule networks. The Rockefeller University Press 2014-11-10 /pmc/articles/PMC4226729/ /pubmed/25385183 http://dx.doi.org/10.1083/jcb.201407095 Text en © 2014 Brouhard and Rice This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 3.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/3.0/). |
spellingShingle | Reviews Brouhard, Gary J. Rice, Luke M. The contribution of αβ-tubulin curvature to microtubule dynamics |
title | The contribution of αβ-tubulin curvature to microtubule dynamics |
title_full | The contribution of αβ-tubulin curvature to microtubule dynamics |
title_fullStr | The contribution of αβ-tubulin curvature to microtubule dynamics |
title_full_unstemmed | The contribution of αβ-tubulin curvature to microtubule dynamics |
title_short | The contribution of αβ-tubulin curvature to microtubule dynamics |
title_sort | contribution of αβ-tubulin curvature to microtubule dynamics |
topic | Reviews |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4226729/ https://www.ncbi.nlm.nih.gov/pubmed/25385183 http://dx.doi.org/10.1083/jcb.201407095 |
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