Cyclin B1/Cdk1 binds and phosphorylates Filamin A and regulates its ability to cross-link actin
Cyclin B1/Cdk1 binds and phosphorylates Filamin A and regulates its ability to cross-link actin
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DOI：
10.1016/j.febslet.2007.03.041
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发表时间：
2007-04-17
期刊：
影响因子：
3.5
通讯作者：
Lee, Jonathan M.
中科院分区：
文献类型：
--
作者：
Cukier, I. Howard;Li, Yun;Lee, Jonathan M.
在有丝分裂之前，当细胞改变它们的形状为胞质分裂做准备时，大量的肌动蛋白重塑发生。在哺乳动物细胞中，有丝分裂由细胞周期蛋白B1和细胞周期蛋白依赖性激酶1（Cdk 1）丝氨酸/苏氨酸激酶的异源二聚体启动。在这份报告中。我们发现人细胞周期蛋白B1结合肌动蛋白交联蛋白Filamin-A（FLNa）。这些蛋白质在有丝分裂的人类细胞中共免疫沉淀和共定位。我们发现，细胞周期蛋白B1/Cdk 1可以磷酸化FLNa在体外，并降低其能力，凝胶化肌动蛋白。我们还确定了丝氨酸1436作为一个FLNa残基磷酸化的细胞周期蛋白B1/Cdk 1在体外。我们的研究结果表明，细胞周期蛋白B1/Cdk 1在FLNa依赖的肌动蛋白重塑的作用。(c)2007年由Elsevier B. V.代表欧洲生物化学学会联合会出版。
Substantial actin remodelling occurs prior to mitosis as cells alter their shape in preparation for cytokinesis. In mammalian cells, mitosis is initiated by a heterodimer of cyclin B1 and the cyclin dependent kinase 1 (Cdk1) serine/threonine kinase. In this report. we show that human cyclin B1 binds the actin cross-linking protein Filamin-A (FLNa). The proteins co-immunoprecipitate and co-localize in mitotic human cells. We find that cyclin B1/Cdk1 can phosphorylate FLNa in vitro and reduce its ability to gelate actin. We have also identified serine 1436 as one FLNa residue phosphorylated by cyclin B1/Cdk1 in vitro. Our results suggest a role for cyclin B1/Cdk1 in FLNa-dependent actin remodelling. (c) 2007 Published by Elsevier B.V. on behalf of the Federation of European Biochemical Societies.