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• W2023348733 abstract "Entry into mitosis of the eukaryotic cell cycle is driven by rising cyclin-dependent kinase (Cdk) activity. During exit from mitosis, Cdk activity must again decline. Cdk downregulation by itself, however, is not able to guide mitotic exit, if not a phosphatase reverses mitotic Cdk phosphorylation events. In budding yeast, this role is played by the Cdc14 phosphatase. We are gaining an increasingly detailed picture of its regulation during anaphase, and of the way it orchestrates ordered progression through mitosis. Much less is known about protein dephosphorylation during mitotic exit in organisms other than budding yeast, but evidence is now mounting for crucial contributions of regulated phosphatases also in metazoan cells." @default.
• W2023348733 created "2016-06-24" @default.
• W2023348733 creator A5073121511 @default.
• W2023348733 creator A5088958035 @default.
• W2023348733 date "2008-12-01" @default.
• W2023348733 modified "2023-10-14" @default.
• W2023348733 title "Cdk-counteracting phosphatases unlock mitotic exit" @default.
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• W2023348733 doi "https://doi.org/10.1016/j.ceb.2008.09.003" @default.
• W2023348733 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2605245" @default.
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