Phosphorylation of Right Open Reading Frame 2 (Rio2) Protein Kinase by Polo-like Kinase 1 Regulates Mitotic Progression
Phosphorylation of Right Open Reading Frame 2 (Rio2) Protein Kinase by Polo-like Kinase 1 Regulates Mitotic Progression
复制标题
Polo 样激酶 1 磷酸化右开放阅读框 2 (Rio2) 蛋白激酶调节有丝分裂进程
DOI：
10.1074/jbc.m111.250175
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发表时间：
2011-10-21
影响因子：
4.8
通讯作者：
Ye, Xin
中科院分区：
文献类型：
--
作者：
Liu, Ting;Deng, Min;Ye, Xin
Polo样激酶1（Plk 1）在有丝分裂的多个阶段通过磷酸化许多底物发挥重要作用。在这里，我们报告的非典型蛋白激酶Rio 2是一种新的底物Plk 1，可以磷酸化Plk 1在Ser-335，Ser-380，和Ser-548。R102的过表达导致延长的有丝分裂退出，而R102的敲低加速有丝分裂进程，表明R102是适当的有丝分裂进程所需的。磷酸化模拟突变体Rio 2 S3 D的过表达而非不可磷酸化的突变体Rio 2 S3 A的过表达显示出与野生型Rio 2类似的特征。这些结果表明R102的磷酸化状态与其在有丝分裂中的功能相关。此外，延时成像数据显示，R102而不是R102 S3 A的过表达导致中期-后期转换减慢。总的来说，这些研究结果强烈表明，Plk 1介导的磷酸化Rio 2调节有丝分裂过程中的中期-后期转换。
Polo-like kinase 1 (Plk1) plays essential roles during multiple stages of mitosis by phosphorylating a number of substrates. Here, we report that the atypical protein kinase Rio2 is a novel substrate of Plk1 and can be phosphorylated by Plk1 at Ser-335, Ser-380, and Ser-548. Overexpression of Rio2 causes a prolonged mitotic exit whereas knockdown of Rio2 accelerates mitotic progression, suggesting that Rio2 is required for the proper mitotic progression. Overexpression of phospho-mimicking mutant Rio2 S3D but not the nonphosphorylatable mutant Rio2 S3A displays a profile similar to that of wild-type Rio2. These results indicate that the phosphorylation status of Rio2 correlates with its function in mitosis. Furthermore, time-lapse imaging data show that overexpression of Rio2 but not Rio2 S3A results in a slowed metaphase-anaphase transition. Collectively, these findings strongly indicate that the Plk1-mediated phosphorylation of Rio2 regulates metaphase-anaphase transition during mitotic progression.