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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2014-10-01
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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 |
work_keys_str_mv |
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1724960918301835264 |