Cdk-counteracting phosphatases unlock mitotic exit.
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.
Cancer Epigenetics and Biology Program (PEBC), Catalan Institute of Oncology, Av. Gran Via S/N, 08907 L'Hospitalet de Llobregat, Barcelona, Spain. equeralt@iconcologia.net
Ethel
E
Queralt
Frank
F
Uhlmann
D000818:Animals; D018844:Cyclin-Dependent Kinases / Q000235:genetics / Q000378:metabolism*; D006801:Humans; D008938:Mitosis / Q000502:physiology*; D008954:Models, Biological; D010749:Phosphoprotein Phosphatases / Q000235:genetics / Q000378:metabolism*; D004718:Saccharomycetales / Q000201:enzymology / Q000378:metabolism; D029702:Schizosaccharomyces pombe Proteins / Q000235:genetics / Q000378:metabolism
D029702:Schizosaccharomyces pombe Proteins; D018844:Cyclin-Dependent Kinases; C503885:CDC14 protein, S pombe; D010749:Phosphoprotein Phosphatases