PP1-Dependent Formin Bnr1 Dephosphorylation and Delocalization from a Cell Division Site.

Cell cycle ends with cytokinesis that is the physical separation of a cell into two daughter cells. For faithful cytokinesis, cells integrate multiple processes, such as actomyosin ring formation, contraction and plasma membrane closure, into coherent responses. Linear actin assembly by formins is e...

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Main Authors: Minami Orii, Keiko Kono, Hsin-I Wen, Makoto Nakanishi
Format: Article
Language:English
Published: Public Library of Science (PLoS) 2016-01-01
Series:PLoS ONE
Online Access:http://europepmc.org/articles/PMC4714816?pdf=render
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author Minami Orii
Keiko Kono
Hsin-I Wen
Makoto Nakanishi
author_facet Minami Orii
Keiko Kono
Hsin-I Wen
Makoto Nakanishi
author_sort Minami Orii
collection DOAJ
description Cell cycle ends with cytokinesis that is the physical separation of a cell into two daughter cells. For faithful cytokinesis, cells integrate multiple processes, such as actomyosin ring formation, contraction and plasma membrane closure, into coherent responses. Linear actin assembly by formins is essential for formation and maintenance of actomyosin ring. Although budding yeast's two formins, Bni1 and Bnr1, are known to switch their subcellular localization at the division site prior to cytokinesis, the underlying mechanisms were not completely understood. Here, we provide evidence showing that Bnr1 is dephosphorylated concomitant with its release from the division site. Impaired PP1/Glc7 activity delayed Bnr1 release and dephosphorylation, Bni1 recruitment and actomyosin ring formation at the division site. These results suggest the involvement of Glc7 in this regulation. Further, we identified Ref2 as the PP1 regulatory subunit responsible for this regulation. Taken together, Glc7 and Ref2 may have a role in actomyosin ring formation by modulating the localization of formins during cytokinesis.
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spelling doaj.art-ff39d9d39d524b8e99ea50b4f631843b2022-12-22T03:19:20ZengPublic Library of Science (PLoS)PLoS ONE1932-62032016-01-01111e014694110.1371/journal.pone.0146941PP1-Dependent Formin Bnr1 Dephosphorylation and Delocalization from a Cell Division Site.Minami OriiKeiko KonoHsin-I WenMakoto NakanishiCell cycle ends with cytokinesis that is the physical separation of a cell into two daughter cells. For faithful cytokinesis, cells integrate multiple processes, such as actomyosin ring formation, contraction and plasma membrane closure, into coherent responses. Linear actin assembly by formins is essential for formation and maintenance of actomyosin ring. Although budding yeast's two formins, Bni1 and Bnr1, are known to switch their subcellular localization at the division site prior to cytokinesis, the underlying mechanisms were not completely understood. Here, we provide evidence showing that Bnr1 is dephosphorylated concomitant with its release from the division site. Impaired PP1/Glc7 activity delayed Bnr1 release and dephosphorylation, Bni1 recruitment and actomyosin ring formation at the division site. These results suggest the involvement of Glc7 in this regulation. Further, we identified Ref2 as the PP1 regulatory subunit responsible for this regulation. Taken together, Glc7 and Ref2 may have a role in actomyosin ring formation by modulating the localization of formins during cytokinesis.http://europepmc.org/articles/PMC4714816?pdf=render
spellingShingle Minami Orii
Keiko Kono
Hsin-I Wen
Makoto Nakanishi
PP1-Dependent Formin Bnr1 Dephosphorylation and Delocalization from a Cell Division Site.
PLoS ONE
title PP1-Dependent Formin Bnr1 Dephosphorylation and Delocalization from a Cell Division Site.
title_full PP1-Dependent Formin Bnr1 Dephosphorylation and Delocalization from a Cell Division Site.
title_fullStr PP1-Dependent Formin Bnr1 Dephosphorylation and Delocalization from a Cell Division Site.
title_full_unstemmed PP1-Dependent Formin Bnr1 Dephosphorylation and Delocalization from a Cell Division Site.
title_short PP1-Dependent Formin Bnr1 Dephosphorylation and Delocalization from a Cell Division Site.
title_sort pp1 dependent formin bnr1 dephosphorylation and delocalization from a cell division site
url http://europepmc.org/articles/PMC4714816?pdf=render
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AT keikokono pp1dependentforminbnr1dephosphorylationanddelocalizationfromacelldivisionsite
AT hsiniwen pp1dependentforminbnr1dephosphorylationanddelocalizationfromacelldivisionsite
AT makotonakanishi pp1dependentforminbnr1dephosphorylationanddelocalizationfromacelldivisionsite