The phosphatase Cdc14 triggers mitotic exit by reversal of Cdk-dependent phosphorylation.
Mol Cell
; 2(6): 709-18, 1998 Dec.
Article
em En
| MEDLINE
| ID: mdl-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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Base de dados:
MEDLINE
Assunto principal:
Saccharomyces cerevisiae
/
Proteínas Tirosina Fosfatases
/
Quinases Ciclina-Dependentes
/
Proteínas de Ciclo Celular
/
Ciclina B
/
Proteínas de Saccharomyces cerevisiae
/
Complexos Ubiquitina-Proteína Ligase
/
Proteínas de Ligação a DNA
/
Mitose
Idioma:
En
Ano de publicação:
1998
Tipo de documento:
Article