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Higher-order oligomerization of Spc110p drives γ-tubulin ring complex assembly
The microtubule (MT) cytoskeleton plays important roles in many cellular processes. In vivo, MT nucleation is controlled by the γ-tubulin ring complex (γTuRC), a 2.1-MDa complex composed of γ-tubulin small complex (γTuSC) subunits. The mechanisms underlying the assembly of γTuRC are largely unknown....
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The American Society for Cell Biology
2016
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4945142/ https://www.ncbi.nlm.nih.gov/pubmed/27226487 http://dx.doi.org/10.1091/mbc.E16-02-0072 |
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author | Lyon, Andrew S. Morin, Geneviève Moritz, Michelle Yabut, King Clyde B. Vojnar, Tamira Zelter, Alex Muller, Eric Davis, Trisha N. Agard, David A. |
author_facet | Lyon, Andrew S. Morin, Geneviève Moritz, Michelle Yabut, King Clyde B. Vojnar, Tamira Zelter, Alex Muller, Eric Davis, Trisha N. Agard, David A. |
author_sort | Lyon, Andrew S. |
collection | PubMed |
description | The microtubule (MT) cytoskeleton plays important roles in many cellular processes. In vivo, MT nucleation is controlled by the γ-tubulin ring complex (γTuRC), a 2.1-MDa complex composed of γ-tubulin small complex (γTuSC) subunits. The mechanisms underlying the assembly of γTuRC are largely unknown. In yeast, the conserved protein Spc110p both stimulates the assembly of the γTuRC and anchors the γTuRC to the spindle pole body. Using a quantitative in vitro FRET assay, we show that γTuRC assembly is critically dependent on the oligomerization state of Spc110p, with higher-order oligomers dramatically enhancing the stability of assembled γTuRCs. Our in vitro findings were confirmed with a novel in vivo γTuSC recruitment assay. We conclude that precise spatial control over MT nucleation is achieved by coupling localization and higher-order oligomerization of the receptor for γTuRC. |
format | Online Article Text |
id | pubmed-4945142 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | The American Society for Cell Biology |
record_format | MEDLINE/PubMed |
spelling | pubmed-49451422016-09-30 Higher-order oligomerization of Spc110p drives γ-tubulin ring complex assembly Lyon, Andrew S. Morin, Geneviève Moritz, Michelle Yabut, King Clyde B. Vojnar, Tamira Zelter, Alex Muller, Eric Davis, Trisha N. Agard, David A. Mol Biol Cell Articles The microtubule (MT) cytoskeleton plays important roles in many cellular processes. In vivo, MT nucleation is controlled by the γ-tubulin ring complex (γTuRC), a 2.1-MDa complex composed of γ-tubulin small complex (γTuSC) subunits. The mechanisms underlying the assembly of γTuRC are largely unknown. In yeast, the conserved protein Spc110p both stimulates the assembly of the γTuRC and anchors the γTuRC to the spindle pole body. Using a quantitative in vitro FRET assay, we show that γTuRC assembly is critically dependent on the oligomerization state of Spc110p, with higher-order oligomers dramatically enhancing the stability of assembled γTuRCs. Our in vitro findings were confirmed with a novel in vivo γTuSC recruitment assay. We conclude that precise spatial control over MT nucleation is achieved by coupling localization and higher-order oligomerization of the receptor for γTuRC. The American Society for Cell Biology 2016-07-15 /pmc/articles/PMC4945142/ /pubmed/27226487 http://dx.doi.org/10.1091/mbc.E16-02-0072 Text en © 2016 Lyon et al. This article is distributed by The American Society for Cell Biology under license from the author(s). Two months after publication it is available to the public under an Attribution–Noncommercial–Share Alike 3.0 Unported Creative Commons License (http://creativecommons.org/licenses/by-nc-sa/3.0). “ASCB®,” “The American Society for Cell Biology®,” and “Molecular Biology of the Cell®” are registered trademarks of The American Society for Cell Biology. |
spellingShingle | Articles Lyon, Andrew S. Morin, Geneviève Moritz, Michelle Yabut, King Clyde B. Vojnar, Tamira Zelter, Alex Muller, Eric Davis, Trisha N. Agard, David A. Higher-order oligomerization of Spc110p drives γ-tubulin ring complex assembly |
title | Higher-order oligomerization of Spc110p drives γ-tubulin ring complex assembly |
title_full | Higher-order oligomerization of Spc110p drives γ-tubulin ring complex assembly |
title_fullStr | Higher-order oligomerization of Spc110p drives γ-tubulin ring complex assembly |
title_full_unstemmed | Higher-order oligomerization of Spc110p drives γ-tubulin ring complex assembly |
title_short | Higher-order oligomerization of Spc110p drives γ-tubulin ring complex assembly |
title_sort | higher-order oligomerization of spc110p drives γ-tubulin ring complex assembly |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4945142/ https://www.ncbi.nlm.nih.gov/pubmed/27226487 http://dx.doi.org/10.1091/mbc.E16-02-0072 |
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