Ring closure activates yeast γTuRC for species-specific microtubule nucleation

The γ-tubulin ring complex (γTuRC) is the primary microtubule nucleator in cells. γTuRC is assembled from repeating γ-tubulin small complex (γTuSC) subunits and is thought to function as a template by presenting a γ-tubulin ring that mimics microtubule geometry. However, a previous yeast γTuRC struc...

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Main Authors:	Kollman, Justin M., Greenberg, Charles H., Li, Sam, Moritz, Michelle, Zelter, Alex, Fong, Kimberly K., Fernandez, Jose-Jesus, Sali, Andrej, Kilmartin, John, Davis, Trisha N., Agard, David A.
Format:	Online
Language:	English
Published:	2015
Online Access:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4318760/

id	pubmed-4318760
recordtype	oai_dc
spelling	pubmed-43187602015-08-01 Ring closure activates yeast γTuRC for species-specific microtubule nucleation Kollman, Justin M. Greenberg, Charles H. Li, Sam Moritz, Michelle Zelter, Alex Fong, Kimberly K. Fernandez, Jose-Jesus Sali, Andrej Kilmartin, John Davis, Trisha N. Agard, David A. Article The γ-tubulin ring complex (γTuRC) is the primary microtubule nucleator in cells. γTuRC is assembled from repeating γ-tubulin small complex (γTuSC) subunits and is thought to function as a template by presenting a γ-tubulin ring that mimics microtubule geometry. However, a previous yeast γTuRC structure showed γTuSC in an open conformation that prevents matching to microtubule symmetry. By contrast, we show here that γ-tubulin complexes are in a closed conformation when attached to microtubules. To confirm its functional importance we trapped the closed state and determined its structure, showing that the γ-tubulin ring precisely matches microtubule symmetry and providing detailed insight into γTuRC architecture. Importantly, the closed state is a stronger nucleator, suggesting this conformational switch may allosterically control γTuRC activity. Finally, we demonstrate that γTuRCs have a profound preference for tubulin from the same species. 2015-01-19 2015-02 /pmc/articles/PMC4318760/ /pubmed/25599398 http://dx.doi.org/10.1038/nsmb.2953 Text en http://www.nature.com/authors/editorial_policies/license.html#terms Users may view, print, copy, and download text and data-mine the content in such documents, for the purposes of academic research, subject always to the full Conditions of use:http://www.nature.com/authors/editorial_policies/license.html#terms
repository_type	Open Access Journal
institution_category	Foreign Institution
institution	US National Center for Biotechnology Information
building	NCBI PubMed
collection	Online Access
language	English
format	Online
author	Kollman, Justin M. Greenberg, Charles H. Li, Sam Moritz, Michelle Zelter, Alex Fong, Kimberly K. Fernandez, Jose-Jesus Sali, Andrej Kilmartin, John Davis, Trisha N. Agard, David A.
spellingShingle	Kollman, Justin M. Greenberg, Charles H. Li, Sam Moritz, Michelle Zelter, Alex Fong, Kimberly K. Fernandez, Jose-Jesus Sali, Andrej Kilmartin, John Davis, Trisha N. Agard, David A. Ring closure activates yeast γTuRC for species-specific microtubule nucleation
author_facet	Kollman, Justin M. Greenberg, Charles H. Li, Sam Moritz, Michelle Zelter, Alex Fong, Kimberly K. Fernandez, Jose-Jesus Sali, Andrej Kilmartin, John Davis, Trisha N. Agard, David A.
author_sort	Kollman, Justin M.
title	Ring closure activates yeast γTuRC for species-specific microtubule nucleation
title_short	Ring closure activates yeast γTuRC for species-specific microtubule nucleation
title_full	Ring closure activates yeast γTuRC for species-specific microtubule nucleation
title_fullStr	Ring closure activates yeast γTuRC for species-specific microtubule nucleation
title_full_unstemmed	Ring closure activates yeast γTuRC for species-specific microtubule nucleation
title_sort	ring closure activates yeast γturc for species-specific microtubule nucleation
description	The γ-tubulin ring complex (γTuRC) is the primary microtubule nucleator in cells. γTuRC is assembled from repeating γ-tubulin small complex (γTuSC) subunits and is thought to function as a template by presenting a γ-tubulin ring that mimics microtubule geometry. However, a previous yeast γTuRC structure showed γTuSC in an open conformation that prevents matching to microtubule symmetry. By contrast, we show here that γ-tubulin complexes are in a closed conformation when attached to microtubules. To confirm its functional importance we trapped the closed state and determined its structure, showing that the γ-tubulin ring precisely matches microtubule symmetry and providing detailed insight into γTuRC architecture. Importantly, the closed state is a stronger nucleator, suggesting this conformational switch may allosterically control γTuRC activity. Finally, we demonstrate that γTuRCs have a profound preference for tubulin from the same species.
publishDate	2015
url	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4318760/
_version_	1613184763372240896

Ring closure activates yeast γTuRC for species-specific microtubule nucleation

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