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  • Title: The phosphatase Cdc14 triggers mitotic exit by reversal of Cdk-dependent phosphorylation.
    Author: Visintin R, Craig K, Hwang ES, Prinz S, Tyers M, Amon A.
    Journal: Mol Cell; 1998 Dec; 2(6):709-18. PubMed ID: 9885559.
    Abstract:
    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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