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

被引：641

作者：

Visintin, R

Craig, K

Hwang, ES

Prinz, S

Tyers, M

Amon, A

机构：

[1] Whitehead Inst Biomed Res, Cambridge, MA 02142 USA

[2] Mt Sinai Hosp, Samuel Lunenfeld Res Inst, Programme Canc & Mol Biol, Toronto, ON M5G 1X5, Canada

来源：

MOLECULAR CELL | 1998年 / 2卷 / 06期

关键词：

D O I：

10.1016/S1097-2765(00)80286-5

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Exit from mitosis requires the inactivation of mitotic cyclin-dependent kinases (CDKs) by an unknown mechanism. We show that the Gdc14 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.

引用

页码：709 / 718

页数：10

共 63 条

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