Licensing of yeast centrosome duplication requires phosphoregulation of sfi1.

Duplication of centrosomes once per cell cycle is essential for bipolar spindle formation and genome maintenance and is controlled in part by cyclin-dependent kinases (Cdks). Our study identifies Sfi1, a conserved component of centrosomes, as the first Cdk substrate required to restrict centrosome d...

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Main Authors: Jennifer S Avena, Shannon Burns, Zulin Yu, Christopher C Ebmeier, William M Old, Sue L Jaspersen, Mark Winey
Format: Article
Language:English
Published: Public Library of Science (PLoS) 2014-10-01
Series:PLoS Genetics
Online Access:http://europepmc.org/articles/PMC4207612?pdf=render
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spelling doaj-465ba8b744de49d0ac008a624402374a2020-11-25T02:00:23ZengPublic Library of Science (PLoS)PLoS Genetics1553-73901553-74042014-10-011010e100466610.1371/journal.pgen.1004666Licensing of yeast centrosome duplication requires phosphoregulation of sfi1.Jennifer S AvenaShannon BurnsZulin YuChristopher C EbmeierWilliam M OldSue L JaspersenMark WineyDuplication of centrosomes once per cell cycle is essential for bipolar spindle formation and genome maintenance and is controlled in part by cyclin-dependent kinases (Cdks). Our study identifies Sfi1, a conserved component of centrosomes, as the first Cdk substrate required to restrict centrosome duplication to once per cell cycle. We found that reducing Cdk1 phosphorylation by changing Sfi1 phosphorylation sites to nonphosphorylatable residues leads to defects in separation of duplicated spindle pole bodies (SPBs, yeast centrosomes) and to inappropriate SPB reduplication during mitosis. These cells also display defects in bipolar spindle assembly, chromosome segregation, and growth. Our findings lead to a model whereby phosphoregulation of Sfi1 by Cdk1 has the dual function of promoting SPB separation for spindle formation and preventing premature SPB duplication. In addition, we provide evidence that the protein phosphatase Cdc14 has the converse role of activating licensing, likely via dephosphorylation of Sfi1.http://europepmc.org/articles/PMC4207612?pdf=render
collection DOAJ
language English
format Article
sources DOAJ
author Jennifer S Avena
Shannon Burns
Zulin Yu
Christopher C Ebmeier
William M Old
Sue L Jaspersen
Mark Winey
spellingShingle Jennifer S Avena
Shannon Burns
Zulin Yu
Christopher C Ebmeier
William M Old
Sue L Jaspersen
Mark Winey
Licensing of yeast centrosome duplication requires phosphoregulation of sfi1.
PLoS Genetics
author_facet Jennifer S Avena
Shannon Burns
Zulin Yu
Christopher C Ebmeier
William M Old
Sue L Jaspersen
Mark Winey
author_sort Jennifer S Avena
title Licensing of yeast centrosome duplication requires phosphoregulation of sfi1.
title_short Licensing of yeast centrosome duplication requires phosphoregulation of sfi1.
title_full Licensing of yeast centrosome duplication requires phosphoregulation of sfi1.
title_fullStr Licensing of yeast centrosome duplication requires phosphoregulation of sfi1.
title_full_unstemmed Licensing of yeast centrosome duplication requires phosphoregulation of sfi1.
title_sort licensing of yeast centrosome duplication requires phosphoregulation of sfi1.
publisher Public Library of Science (PLoS)
series PLoS Genetics
issn 1553-7390
1553-7404
publishDate 2014-10-01
description Duplication of centrosomes once per cell cycle is essential for bipolar spindle formation and genome maintenance and is controlled in part by cyclin-dependent kinases (Cdks). Our study identifies Sfi1, a conserved component of centrosomes, as the first Cdk substrate required to restrict centrosome duplication to once per cell cycle. We found that reducing Cdk1 phosphorylation by changing Sfi1 phosphorylation sites to nonphosphorylatable residues leads to defects in separation of duplicated spindle pole bodies (SPBs, yeast centrosomes) and to inappropriate SPB reduplication during mitosis. These cells also display defects in bipolar spindle assembly, chromosome segregation, and growth. Our findings lead to a model whereby phosphoregulation of Sfi1 by Cdk1 has the dual function of promoting SPB separation for spindle formation and preventing premature SPB duplication. In addition, we provide evidence that the protein phosphatase Cdc14 has the converse role of activating licensing, likely via dephosphorylation of Sfi1.
url http://europepmc.org/articles/PMC4207612?pdf=render
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