Phosphorylation of the yeast γ-tubulin Tub4 regulates microtubule function.
The yeast γ-tubulin Tub4 is assembled with Spc97 and Spc98 into the small Tub4 complex. The Tub4 complex binds via the receptor proteins Spc72 and Spc110 to the spindle pole body (SPB), the functional equivalent of the mammalian centrosome, where the Tub4 complex organizes cytoplasmic and nuclear mi...
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2011
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oai:doaj.org-article:45788b7e5f394afd92bd54afdcf3f7ca2021-11-18T06:54:24ZPhosphorylation of the yeast γ-tubulin Tub4 regulates microtubule function.1932-620310.1371/journal.pone.0019700https://doaj.org/article/45788b7e5f394afd92bd54afdcf3f7ca2011-05-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/21573187/?tool=EBIhttps://doaj.org/toc/1932-6203The yeast γ-tubulin Tub4 is assembled with Spc97 and Spc98 into the small Tub4 complex. The Tub4 complex binds via the receptor proteins Spc72 and Spc110 to the spindle pole body (SPB), the functional equivalent of the mammalian centrosome, where the Tub4 complex organizes cytoplasmic and nuclear microtubules. Little is known about the regulation of the Tub4 complex. Here, we isolated the Tub4 complex with the bound receptors from yeast cells. Analysis of the purified Tub4 complex by mass spectrometry identified more than 50 phosphorylation sites in Spc72, Spc97, Spc98, Spc110 and Tub4. To examine the functional relevance of the phosphorylation sites, phospho-mimicking and non-phosphorylatable mutations in Tub4, Spc97 and Spc98 were analyzed. Three phosphorylation sites in Tub4 were found to be critical for Tub4 stability and microtubule organization. One of the sites is highly conserved in γ-tubulins from yeast to human.Tien-chen LinLinda GombosAnnett NeunerDominik SebastianJesper V OlsenAjla HrleChristian BendaElmar SchiebelPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 6, Iss 5, p e19700 (2011) |
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Medicine R Science Q Tien-chen Lin Linda Gombos Annett Neuner Dominik Sebastian Jesper V Olsen Ajla Hrle Christian Benda Elmar Schiebel Phosphorylation of the yeast γ-tubulin Tub4 regulates microtubule function. |
description |
The yeast γ-tubulin Tub4 is assembled with Spc97 and Spc98 into the small Tub4 complex. The Tub4 complex binds via the receptor proteins Spc72 and Spc110 to the spindle pole body (SPB), the functional equivalent of the mammalian centrosome, where the Tub4 complex organizes cytoplasmic and nuclear microtubules. Little is known about the regulation of the Tub4 complex. Here, we isolated the Tub4 complex with the bound receptors from yeast cells. Analysis of the purified Tub4 complex by mass spectrometry identified more than 50 phosphorylation sites in Spc72, Spc97, Spc98, Spc110 and Tub4. To examine the functional relevance of the phosphorylation sites, phospho-mimicking and non-phosphorylatable mutations in Tub4, Spc97 and Spc98 were analyzed. Three phosphorylation sites in Tub4 were found to be critical for Tub4 stability and microtubule organization. One of the sites is highly conserved in γ-tubulins from yeast to human. |
format |
article |
author |
Tien-chen Lin Linda Gombos Annett Neuner Dominik Sebastian Jesper V Olsen Ajla Hrle Christian Benda Elmar Schiebel |
author_facet |
Tien-chen Lin Linda Gombos Annett Neuner Dominik Sebastian Jesper V Olsen Ajla Hrle Christian Benda Elmar Schiebel |
author_sort |
Tien-chen Lin |
title |
Phosphorylation of the yeast γ-tubulin Tub4 regulates microtubule function. |
title_short |
Phosphorylation of the yeast γ-tubulin Tub4 regulates microtubule function. |
title_full |
Phosphorylation of the yeast γ-tubulin Tub4 regulates microtubule function. |
title_fullStr |
Phosphorylation of the yeast γ-tubulin Tub4 regulates microtubule function. |
title_full_unstemmed |
Phosphorylation of the yeast γ-tubulin Tub4 regulates microtubule function. |
title_sort |
phosphorylation of the yeast γ-tubulin tub4 regulates microtubule function. |
publisher |
Public Library of Science (PLoS) |
publishDate |
2011 |
url |
https://doaj.org/article/45788b7e5f394afd92bd54afdcf3f7ca |
work_keys_str_mv |
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