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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....

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Autores principales: Lyon, Andrew S., Morin, Geneviève, Moritz, Michelle, Yabut, King Clyde B., Vojnar, Tamira, Zelter, Alex, Muller, Eric, Davis, Trisha N., Agard, David A.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The American Society for Cell Biology 2016
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.
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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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