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首页> 外文期刊>The biochemical journal >NIMA-related kinase 2 (Nek2), a cell-cycle-regulated protein kinase localized to centrosomes, is complexed to protein phosphatase 1
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NIMA-related kinase 2 (Nek2), a cell-cycle-regulated protein kinase localized to centrosomes, is complexed to protein phosphatase 1

机译:NIMA相关激酶2(Nek2)是一种细胞周期调节的蛋白激酶,位于蛋白体中,与蛋白磷酸酶1复合。

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pThe cell cycle-regulated protein serine/threonine NIMA-related kinase 2 (Nek2), which shows a predominant localization at centrosomes, is identified as a protein which interacts with protein phosphatase 1 (PP1) using the yeast two-hybrid system. Complex formation between Nek2 and PP1 is supported by co-precipitation of the two proteins using transfected expression constructs of Nek2 and the endogenous Nek2/PP1 proteins. The sequence KVHF in the C-terminal region of Nek2, which conforms to the consensus PP1-binding motif, is shown to be essential for the interaction of Nek2 with PP1. Nek2 activity increases with autophosphorylation and addition of phosphatase inhibitors and decreases in the presence of PP1. PP1 is a substrate for Nek2 and phosphorylation of PP1γsub1/sub on two C-terminal sites reduces its phosphatase activity. The presence of a ternary complex containing centrosomal Nek2-associated protein (C-Nap1), Nek2 and PP1 has also been demonstrated, and C-Nap1 is shown to be a substrate for both Nek2 and PP1 iin vitro/i and in cell extracts. The implications of kinase-phosphatase complex formation involving Nek2 and PP1 are discussed in terms of the coordination of centrosome separation with cell cycle progression./p
机译:>细胞周期调节蛋白丝氨酸/苏氨酸NIMA相关激酶2(Nek2)表现出主要定位于中心体,已被鉴定为使用酵母双杂交系统与蛋白磷酸酶1(PP1)相互作用的蛋白。 。使用转染的Nek2和内源性Nek2 / PP1表达构建体对这两种蛋白质进行共沉淀,可以支持Nek2和PP1之间的复合物形成。 Nek2的C末端区域中的序列KVHF符合共有的PP1结合基序,显示为Nek2与PP1相互作用必不可少的。 Nek2活性随着自身磷酸化和磷酸酶抑制剂的添加而增加,而在PP1存在下降低。 PP1是Nek2的底物,PP1γ 1 在两个C末端位点的磷酸化会降低其磷酸酶活性。还证明了含有中心体Nek2相关蛋白(C-Nap1),Nek2和PP1的三元复合物的存在,并且C-Nap1被证明是Nek2和PP1的底物和细胞提取物中。从中心体分离与细胞周期进程的协调性上讨论了涉及Nek2和PP1的激酶-磷酸酶复合物形成的意义。

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