The phosphatase Cdc14 triggers mitotic exit by reversal of CDK-dependent phosphorylation
The phosphatase Cdc14 triggers mitotic exit by reversal of CDK-dependent phosphorylation
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DOI：
10.1016/s1097-2765(00)80286-5
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发表时间：
1998-12-01
期刊：
影响因子：
16
通讯作者：
Amon, A
中科院分区：
文献类型：
--
作者：
Visintin, R;Craig, K;Amon, A
退出有丝分裂需要有丝分裂细胞周期蛋白依赖性激酶（CDKs）通过未知的机制失活。我们发现，Gdc 14磷酸酶触发有丝分裂退出：通过三个平行的机制，其中每一个抑制Cdk活性。Cdc 14去磷酸化Sic 1（Cdk抑制剂）和Swi 5（SIC 1的转录因子），并诱导有丝分裂细胞周期蛋白的降解，可能是通过去磷酸化有丝分裂细胞周期蛋白降解的激活剂Cdh 1/Hct 1。这些途径之间的反馈可能导致有丝分裂CDK活性的急剧崩溃，并帮助协调有丝分裂的退出。
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.