Control of cyclin ubiquitination by CDK-regulated binding of Hct1 to the anaphase promoting complex
Control of cyclin ubiquitination by CDK-regulated binding of Hct1 to the anaphase promoting complex
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DOI：
10.1126/science.282.5394.1721
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发表时间：
1998-11-27
期刊：
影响因子：
56.9
通讯作者：
Seufert, W
中科院分区：
文献类型：
--
作者：
Zachariae, W;Schwab, M;Seufert, W
有丝分裂期细胞周期蛋白的蛋白水解依赖于一种多亚基泛素-蛋白连接酶，即后期促进复合物（APC）。蛋白水解始于后期，持续于G（1）期，直至细胞进入S期时被细胞周期蛋白依赖性激酶（CDKs）终止。酵母中有丝分裂细胞周期蛋白的蛋白水解需要APC与底物特异性激活剂Hct 1（也称为Cdh 1）的结合。CDK对Hct 1的磷酸化阻断了Hct 1与APC的相互作用。APC和CDK之间的相互抑制解释了细胞如何在G（1）期间抑制有丝分裂CDK活性，然后建立从S期到后期的激酶活性升高的时期。
Proteolysis of mitotic cyclins depends on a multisubunit ubiquitin-protein Ligase, the anaphase promoting complex (APC), Proteolysis commences during anaphase, persisting throughout G(1) until it is terminated by-cyclin-dependent kinases (CDKs) as cells enter S phase. Proteolysis of mitotic cyclins in yeast was shown to require association of the APC with the substrate-specific activator Hct1 (also called Cdh1). Phosphorylation of Hct1 by CDKs blocked the Hct1-APC interaction. The mutual inhibition between APC and CDKs explains how cells suppress mitotic CDK activity during G(1) and then establish a period with elevated kinase activity from S phase until anaphase.