Phosphorylation by cyclin B-Cdk underlies release of mitotic exit activator Cdc14 from the nucleolus
Phosphorylation by cyclin B-Cdk underlies release of mitotic exit activator Cdc14 from the nucleolus
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DOI：
10.1126/science.1099402
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发表时间：
2004-07-23
期刊：
影响因子：
56.9
通讯作者：
Deshaies, RJ
中科院分区：
文献类型：
--
作者：
Azzam, R;Chen, SL;Deshaies, RJ
芽殖酵母蛋白磷酸酶Cdc14在间期期间被锚蛋白Net1以非活性状态隔离在核仁中。进入后期后，Cdc14早期后期释放（FEAR）网络启动分散活性Cdc14在整个细胞。我们报告说，FEAR网络促进Net1的磷酸化细胞周期蛋白依赖性激酶（Cdk）与细胞周期蛋白B1或细胞周期蛋白B2复合。这些磷酸化似乎是FEAR所必需的，并维持晚期有丝分裂事件的适当时机。因此，存在一个调节回路来确保有丝分裂状态的仲裁者Cdk启动最终退出有丝分裂的事件。
Budding yeast protein phosphatase Cdc14 is sequestered in the nucleolus in an inactive state during interphase by the anchor protein Net1. Upon entry into anaphase, the Cdc14 early anaphase release ( FEAR) network initiates dispersal of active Cdc14 throughout the cell. We report that the FEAR network promotes phosphorylation of Net1 by cyclin-dependent kinase (Cdk) complexed with cyclin B1 or cyclin B2. These phosphorylations appear to be required for FEAR and sustain the proper timing of late mitotic events. Thus, a regulatory circuit exists to ensure that the arbiter of the mitotic state, Cdk, sets in motion events that culminate in exit from mitosis.