KAP - A DUAL-SPECIFICITY PHOSPHATASE THAT INTERACTS WITH CYCLIN-DEPENDENT KINASES
KAP - A DUAL-SPECIFICITY PHOSPHATASE THAT INTERACTS WITH CYCLIN-DEPENDENT KINASES
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DOI：
10.1073/pnas.91.5.1731
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发表时间：
1994-03-01
影响因子：
11.1
通讯作者：
BEACH, D
中科院分区：
文献类型：
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作者：
HANNON, GJ;CASSO, D;BEACH, D
细胞周期蛋白依赖性激酶是关键的细胞周期调节因子，其激活是从一个细胞周期阶段进入下一个阶段所必需的。在哺乳动物细胞中，CDK 2与G（1）和S期的控制有关。我们已经使用双杂交蛋白相互作用筛选来鉴定编码可以与CDK 2相互作用的蛋白的cDNA。在这些被鉴定的是一种蛋白质（KAP），其中包含HCXX-XXGR蛾特征的蛋白质酪氨酸磷酸酶。KAP对含有磷酸酪氨酸或磷酸丝氨酸残基的底物表现出磷酸酶活性。由于KAP是不显着类似于已知的磷酸酶以外的催化核心蛾，它代表了另一类的双特异性磷酸酶。在酵母中，KAP与cdc 2和CDK 2相互作用。在哺乳动物细胞中，KAP也与cdc 2和CDK 2相关，但表现出对cdc 2的偏好。KAP结合多种细胞周期蛋白依赖性激酶的能力表明它可能在细胞周期调节中发挥作用。
The cyclin-dependent kinases are key cell cycle regulators whose activation is required for passage from one cell cycle phase to the next. In mammalian cells, CDK2 has been implicated in control of the G(1) and S phases. We have used a two hybrid protein interaction screen to identify cDNAs encoding proteins that can interact with CDK2. Among those identified was a protein (KAP), which contained the HCXX-XXGR moth characteristic of protein tyrosine phosphatases. KAP showed phosphatase activity toward substrates containing either phosphotyrosine or phosphoserine residues. Since KAP is not significantly similar to known phosphatases beyond the catalytic core moth, it represents an additional class of dual specificity phosphatase. KAP interacted with cdc2 and CDK2 in yeast. In mammalian cells, KAP also associated with cdc2 and CDK2 but showed a preference for cdc2. The ability of KAP to bind multiple cyclin-dependent kinases suggests that it may play a role in cell cycle regulation.