Cyclin B1/Cdk1 binds and phosphorylates Filamin A and regulates its ability to cross-link actin

被引:36
作者
Cukier, I. Howard
Li, Yun
Lee, Jonathan M.
机构
[1] Univ Ottawa, Dept Biochem Microbiol & Immunol, Ottawa, ON K1H 8M5, Canada
[2] McMaster Univ, Juravinski Canc Ctr, Hamilton, ON, Canada
[3] McMaster Univ, Dept Pathol & Mol Med, Hamilton, ON, Canada
来源
FEBS LETTERS | 2007年 / 581卷 / 08期
关键词
cyclin B1; Filamin A; mitosis; phosphorylation; cytoskeleton; actin; gelation; cyclin dependent kinase; Cdk1; cell cycle;
D O I
10.1016/j.febslet.2007.03.041
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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.
引用
收藏
页码:1661 / 1672
页数:12
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