Cdk1-dependent regulation of the mitotic inhibitor Wee1
Cdk1-dependent regulation of the mitotic inhibitor Wee1
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DOI：
10.1016/j.cell.2005.05.029
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发表时间：
2005-08-12
期刊：
影响因子：
64.5
通讯作者：
Kellogg, DR
中科院分区：
文献类型：
--
作者：
Harvey, SL;Charlet, A;Kellogg, DR
Wee1激酶磷酸化并抑制细胞周期蛋白依赖性激酶1(CDK1)，从而延迟进入有丝分裂，直到满足适当的条件。对Wee1调控机制的理解应该会为细胞如何做出进入有丝分裂的决定提供新的见解。我们在这里报道了Wee1的发芽酵母同源物Swe1直接受CDK1调控。CDK1对Swe1的磷酸化激活了Swe1，这是形成稳定的Swe1-CDK1复合体所必需的，该复合体将CDK1保持在抑制状态。CDK1的去磷酸化导致Swe1的进一步磷酸化和CDK1的释放。因此，CDK1对其自身的抑制物既有正向调节，也有负向调节。调节Swe1-CDK1复合体可能在控制向有丝分裂的转变过程中发挥关键作用。
The Wee1 kinase phosphorylates and inhibits cyclin-dependent kinase 1 (Cdk1), thereby delaying entry into mitosis until appropriate conditions have been met. An understanding of the mechanisms that regulate Wee1 should provide new insight into how cells make the decision to enter mitosis. We report here that Swe1, the budding-yeast homolog of Wee1, is directly regulated by Cdk1. Phosphorylation of Swe1 by Cdk1 activates Swe1 and is required for formation of a stable Swe1-Cdk1 complex that maintains Cdk1 in the inhibited state. Dephosphorylation of Cdk1 leads to further phosphorylation of Swe1 and release of Cdk1. Thus, Cdk1 both positively and negatively regulates its own inhibitor. Regulation of the Swe1-Cdk1 complex is likely to play a critical role in controlling the transition into mitosis.