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

FEBS Lett. 2007 Apr 17;581(8):1661-72. doi: 10.1016/j.febslet.2007.03.041. Epub 2007 Mar 28.


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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Actins / metabolism*
  • Amino Acid Sequence
  • CDC2 Protein Kinase / metabolism*
  • Contractile Proteins / analysis
  • Contractile Proteins / metabolism*
  • Cyclin B / analysis
  • Cyclin B / metabolism*
  • Cyclin B1
  • Filamins
  • Humans
  • Microfilament Proteins / analysis
  • Microfilament Proteins / metabolism*
  • Molecular Sequence Data
  • Phosphorylation
  • Protein Interaction Mapping
  • Serine / metabolism
  • Two-Hybrid System Techniques


  • Actins
  • CCNB1 protein, human
  • Contractile Proteins
  • Cyclin B
  • Cyclin B1
  • Filamins
  • Microfilament Proteins
  • Serine
  • CDC2 Protein Kinase