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Updated: Jul 15, 2026

Identification of Cyclin-dependent Kinase 1 Specific Phosphorylation Sites by an In Vitro Kinase Assay
Published on: May 3, 2018
Cyclin B1/Cdk1 binds and phosphorylates Filamin A and regulates its ability to cross-link actin
I Howard Cukier1, Yun Li, Jonathan M Lee
1Juravinski Cancer Centre and Department of Pathology and Molecular Medicine, McMaster University, Hamilton, Ontario, Canada.
Abstract:
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.
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