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Mol Cell. 1998 Dec;2(6):709-18.

The phosphatase Cdc14 triggers mitotic exit by reversal of Cdk-dependent phosphorylation.

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Whitehead Institute for Biomedical Research, Cambridge Center, Massachusetts 02142, USA.


Exit from mitosis requires the inactivation of mitotic cyclin-dependent kinases (CDKs) by an unknown mechanism. We show that the Cdc14 phosphatase triggers mitotic exit by three parallel mechanisms, each of which inhibits Cdk activity. Cdc14 dephosphorylates Sic1, a Cdk inhibitor, and Swi5, a transcription factor for SIC1, and induces degradation of mitotic cyclins, likely by dephosphorylating the activator of mitotic cyclin degradation, Cdh1/Hct1. Feedback between these pathways may lead to precipitous collapse of mitotic CDK activity and help coordinate exit from mitosis.

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