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Downregulation of PP2A(Cdc55) phosphatase by separase initiates mitotic exit in budding yeast.

TitleDownregulation of PP2A(Cdc55) phosphatase by separase initiates mitotic exit in budding yeast.
Publication TypeJournal Article
Year of Publication2006
AuthorsQueralt E, Lehane C, Novak B, Uhlmann F
Date Published2006 May 19
KeywordsCell Cycle Proteins, Cell Nucleolus, Cyclin B, Down-Regulation, Endopeptidases, Enzyme Activation, Mitosis, Models, Biological, Nuclear Proteins, Phosphoprotein Phosphatases, Phosphorylation, Protein Tyrosine Phosphatases, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins

After anaphase, the high mitotic cyclin-dependent kinase (Cdk) activity is downregulated to promote exit from mitosis. To this end, in the budding yeast S. cerevisiae, the Cdk counteracting phosphatase Cdc14 is activated. In metaphase, Cdc14 is kept inactive in the nucleolus by its inhibitor Net1. During anaphase, Cdk- and Polo-dependent phosphorylation of Net1 is thought to release active Cdc14. How Net1 is phosphorylated specifically in anaphase, when mitotic kinase activity starts to decline, has remained unexplained. Here, we show that PP2A(Cdc55) phosphatase keeps Net1 underphosphorylated in metaphase. The sister chromatid-separating protease separase, activated at anaphase onset, interacts with and downregulates PP2A(Cdc55), thereby facilitating Cdk-dependent Net1 phosphorylation. PP2A(Cdc55) downregulation also promotes phosphorylation of Bfa1, contributing to activation of the "mitotic exit network" that sustains Cdc14 as Cdk activity declines. These findings allow us to present a new quantitative model for mitotic exit in budding yeast.

Alternate JournalCell

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