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

Rosella Visintin, Karen Craig, Ellen S. Hwang, Susanne Prinz, Mike Tyers, Angelika Amon

Research output: Contribution to journalArticle

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.

Original languageEnglish
Pages (from-to)709-718
Number of pages10
JournalMolecular Cell
Volume2
Issue number6
Publication statusPublished - Dec 1998

ASJC Scopus subject areas

  • Molecular Biology

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    Visintin, R., Craig, K., Hwang, E. S., Prinz, S., Tyers, M., & Amon, A. (1998). The phosphatase Cdc14 triggers mitotic exit by reversal of Cdk-dependent phosphorylation. Molecular Cell, 2(6), 709-718.