Abstract
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.
Highlights
Cytokinesis is the final stage of cell cycle, which distributes cellular content into two daughter cells
Accumulating evidence suggest that loss of cell polarity before entering cytokinesis is critical for actomyosin ring formation, which is regulated at least in part by inhibition of Racand PAK1-dependent adhesion in mammals [3,4], or by inhibition of Cdc42 in yeast [5]
We further propose that PP1/Glc7 and its regulatory subunit Ref2 may play a role in the release and dephosphorylation of Bnr1, Bni1 recruitment and actomyosin ring formation
Summary
Cytokinesis is the final stage of cell cycle, which distributes cellular content into two daughter cells. Actomyosin-dependent formation of contractile ring is critical for successful cytokinesis in diverse eukaryotes. Cdc5/Polo kinase triggers activation of Rho1/RhoA at the division site in anaphase, leading to recruitment and activation of linear actin nucleator formin 1,2]. Accumulating evidence suggest that loss of cell polarity before entering cytokinesis is critical for actomyosin ring formation, which is regulated at least in part by inhibition of Racand PAK1-dependent adhesion in mammals [3,4], or by inhibition of Cdc in yeast [5]. Diaphanous-related formins (DRFs) are auto-inhibited by the binding between N-terminal Diaphanous inhibitory domain (DID) and C-terminal Diaphanous autoregulatory domain (DAD). This auto-inhibition could be relieved primarily by the binding of PLOS ONE | DOI:10.1371/journal.pone.0146941. This auto-inhibition could be relieved primarily by the binding of PLOS ONE | DOI:10.1371/journal.pone.0146941 January 15, 2016
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