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

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.
Mesh Terms:
Cell Cycle Proteins, Cyclin B, Cyclin-Dependent Kinase Inhibitor Proteins, Cyclin-Dependent Kinases, Cyclins, DNA Replication, DNA-Binding Proteins, Fungal Proteins, GTP-Binding Proteins, Gene Expression Regulation, Enzymologic, Gene Expression Regulation, Fungal, Ligases, Mitosis, Mutation, Phosphoprotein Phosphatases, Phosphorylation, Protein Kinases, Protein Tyrosine Phosphatases, Protein-Serine-Threonine Kinases, RNA-Binding Proteins, Recombinant Fusion Proteins, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Substrate Specificity, Transcription Factors, Transcription, Genetic, Ubiquitin-Protein Ligase Complexes, Ubiquitin-Protein Ligases
Mol. Cell
Date: Dec. 01, 1998
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