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An extended γ-tubulin ring functions as a stable platform in microtubule nucleation

γ-Tubulin complexes are essential for microtubule (MT) nucleation. The γ-tubulin small complex (γ-TuSC) consists of two molecules of γ-tubulin and one molecule each of Spc97 and Spc98. In vitro, γ-TuSCs oligomerize into spirals of 13 γ-tubulin molecules per turn. However, the properties and numbers...

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Autores principales: Erlemann, Sarah, Neuner, Annett, Gombos, Linda, Gibeaux, Romain, Antony, Claude, Schiebel, Elmar
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The Rockefeller University Press 2012
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3317808/
https://www.ncbi.nlm.nih.gov/pubmed/22472440
http://dx.doi.org/10.1083/jcb.201111123
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author Erlemann, Sarah
Neuner, Annett
Gombos, Linda
Gibeaux, Romain
Antony, Claude
Schiebel, Elmar
author_facet Erlemann, Sarah
Neuner, Annett
Gombos, Linda
Gibeaux, Romain
Antony, Claude
Schiebel, Elmar
author_sort Erlemann, Sarah
collection PubMed
description γ-Tubulin complexes are essential for microtubule (MT) nucleation. The γ-tubulin small complex (γ-TuSC) consists of two molecules of γ-tubulin and one molecule each of Spc97 and Spc98. In vitro, γ-TuSCs oligomerize into spirals of 13 γ-tubulin molecules per turn. However, the properties and numbers of γ-TuSCs at MT nucleation sites in vivo are unclear. In this paper, we show by fluorescence recovery after photobleaching analysis that γ-tubulin was stably integrated into MT nucleation sites and was further stabilized by tubulin binding. Importantly, tubulin showed a stronger interaction with the nucleation site than with the MT plus end, which probably provides the basis for MT nucleation. Quantitative analysis of γ-TuSCs on single MT minus ends argued for nucleation sites consisting of approximately seven γ-TuSCs with approximately three additional γ-tubulin molecules. Nucleation and anchoring of MTs required the same number of γ-tubulin molecules. We suggest that a spiral of seven γ-TuSCs with a slight surplus of γ-tubulin nucleates MTs in vivo.
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spelling pubmed-33178082012-10-02 An extended γ-tubulin ring functions as a stable platform in microtubule nucleation Erlemann, Sarah Neuner, Annett Gombos, Linda Gibeaux, Romain Antony, Claude Schiebel, Elmar J Cell Biol Research Articles γ-Tubulin complexes are essential for microtubule (MT) nucleation. The γ-tubulin small complex (γ-TuSC) consists of two molecules of γ-tubulin and one molecule each of Spc97 and Spc98. In vitro, γ-TuSCs oligomerize into spirals of 13 γ-tubulin molecules per turn. However, the properties and numbers of γ-TuSCs at MT nucleation sites in vivo are unclear. In this paper, we show by fluorescence recovery after photobleaching analysis that γ-tubulin was stably integrated into MT nucleation sites and was further stabilized by tubulin binding. Importantly, tubulin showed a stronger interaction with the nucleation site than with the MT plus end, which probably provides the basis for MT nucleation. Quantitative analysis of γ-TuSCs on single MT minus ends argued for nucleation sites consisting of approximately seven γ-TuSCs with approximately three additional γ-tubulin molecules. Nucleation and anchoring of MTs required the same number of γ-tubulin molecules. We suggest that a spiral of seven γ-TuSCs with a slight surplus of γ-tubulin nucleates MTs in vivo. The Rockefeller University Press 2012-04-02 /pmc/articles/PMC3317808/ /pubmed/22472440 http://dx.doi.org/10.1083/jcb.201111123 Text en © 2012 Erlemann et al. 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 Research Articles
Erlemann, Sarah
Neuner, Annett
Gombos, Linda
Gibeaux, Romain
Antony, Claude
Schiebel, Elmar
An extended γ-tubulin ring functions as a stable platform in microtubule nucleation
title An extended γ-tubulin ring functions as a stable platform in microtubule nucleation
title_full An extended γ-tubulin ring functions as a stable platform in microtubule nucleation
title_fullStr An extended γ-tubulin ring functions as a stable platform in microtubule nucleation
title_full_unstemmed An extended γ-tubulin ring functions as a stable platform in microtubule nucleation
title_short An extended γ-tubulin ring functions as a stable platform in microtubule nucleation
title_sort extended γ-tubulin ring functions as a stable platform in microtubule nucleation
topic Research Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3317808/
https://www.ncbi.nlm.nih.gov/pubmed/22472440
http://dx.doi.org/10.1083/jcb.201111123
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