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Cyclin B1/Cdk1 binds and phosphorylates Filamin A and regulates its ability to cross‐link actin
Author(s) -
Cukier I. Howard,
Li Yun,
Lee Jonathan M.
Publication year - 2007
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2007.03.041
Subject(s) - filamin , flna , cyclin b1 , microbiology and biotechnology , cyclin dependent kinase 1 , cyclin a , mitosis , cyclin b , biology , cyclin dependent kinase , cell cycle , chemistry , cyclin , biochemistry , cytoskeleton , cell
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.