Cargando…
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...
Autores principales: | , , , , , |
---|---|
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 |
_version_ | 1782228625826775040 |
---|---|
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. |
format | Online Article Text |
id | pubmed-3317808 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2012 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
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 |
work_keys_str_mv | AT erlemannsarah anextendedgtubulinringfunctionsasastableplatforminmicrotubulenucleation AT neunerannett anextendedgtubulinringfunctionsasastableplatforminmicrotubulenucleation AT gomboslinda anextendedgtubulinringfunctionsasastableplatforminmicrotubulenucleation AT gibeauxromain anextendedgtubulinringfunctionsasastableplatforminmicrotubulenucleation AT antonyclaude anextendedgtubulinringfunctionsasastableplatforminmicrotubulenucleation AT schiebelelmar anextendedgtubulinringfunctionsasastableplatforminmicrotubulenucleation AT erlemannsarah extendedgtubulinringfunctionsasastableplatforminmicrotubulenucleation AT neunerannett extendedgtubulinringfunctionsasastableplatforminmicrotubulenucleation AT gomboslinda extendedgtubulinringfunctionsasastableplatforminmicrotubulenucleation AT gibeauxromain extendedgtubulinringfunctionsasastableplatforminmicrotubulenucleation AT antonyclaude extendedgtubulinringfunctionsasastableplatforminmicrotubulenucleation AT schiebelelmar extendedgtubulinringfunctionsasastableplatforminmicrotubulenucleation |