CDI1, A HUMAN G1-PHASE AND S-PHASE PROTEIN PHOSPHATASE THAT ASSOCIATES WITH CDK2
CDI1, A HUMAN G1-PHASE AND S-PHASE PROTEIN PHOSPHATASE THAT ASSOCIATES WITH CDK2
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DOI：
10.1016/0092-8674(93)90498-f
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发表时间：
1993-11-19
期刊：
影响因子：
64.5
通讯作者：
BRENT, R
中科院分区：
文献类型：
--
作者：
GYURIS, J;GOLEMIS, E;BRENT, R
我们使用了相互作用蛋白的酵母遗传选择的相互作用陷阱来分离人细胞周期蛋白依赖性激酶相互作用器1（CDI1）。在酵母中，CDI1与细胞周期蛋白依赖性激酶相互作用，包括人CDC2，CDK2和CDK3，但与CKD4不相互作用。 在HeLa细胞中，CDI1在G1到S跃迁时表达，蛋白质与CDK2形成稳定的复合物。 CDI1具有与已知酪氨酸和双重特异性磷酸酶相似的较弱的序列相似性。 在体外，CDI1从模型底物中的酪氨酸残基中去除磷酸盐，但是在推定的活性位点半胱氨酸中带有病变的突变蛋白没有。野生型CDI1的过表达延迟了酵母和HeLa细胞中细胞周期的进展。延迟取决于CDI1磷酸酶活性。这些实验将CDI1识别为一种新型的蛋白质磷酸酶，形成与细胞周期蛋白依赖性激酶的复合物。
We used the interaction trap, a yeast genetic selection for interacting proteins, to isolate human cyclin-dependent kinase interactor 1 (Cdi1). In yeast, Cdi1 interacts with cyclin-dependent kinases, including human Cdc2, Cdk2, and Cdk3, but not with Ckd4. In HeLa cells, Cdi1 is expressed at the G1 to S transition, and the protein forms stable complexes with Cdk2. Cdi1 bears weak sequence similarity to known tyrosine and dual specificity phosphatases. In vitro, Cdi1 removes phosphate from tyrosine residues in model substrates, but a mutant protein that bears a lesion in the putative active site cysteine does not. Overexpression of wild-type Cdi1 delays progression through the cell cycle in yeast and HeLa cells; delay is dependent on Cdi1 phosphatase activity. These experiments identify Cdi1 as a novel type of protein phosphatase that forms complexes with cyclin-dependent kinases.