Phosphoregulation of MgcRacGAP in Mitosis Involves Aurora B and Cdk1 Protein Kinases and the PP2A Phosphatase

Overview

Journal FEBS Lett

Specialty Biochemistry

Date 2008 Jan 19

PMID 18201571

Citations 21

Authors

Aminata Toure

Rym Mzali

Caroline Liot

Laetitia Seguin

Laurence Morin

Catherine Crouin

Ilin Chen-Yang

Yeou-Guang Tsay

Olivier Dorseuil

Gerard Gacon

Jacques Bertoglio

Affiliations

Soon will be listed here.

Abstract

MgcRacGAP, a Rho GAP essential to cytokinesis, works both as a Rho GTPase regulator and as a scaffolding protein. MgcRacGAP interacts with MKLP1 to form the centralspindlin complex and associates with the RhoGEF Ect2. The GAP activity of MgcRacGAP is regulated by Aurora B phosphorylation. We have isolated B56epsilon, a PP2A regulatory subunit, as a new MgcRacGAP partner. We report here that (i) MgcRacGAP is phosphorylated by Aurora B and Cdk1, (ii) PP2A dephosphorylates Aurora B and Cdk1 phosphorylated sites and (iii) inhibition of PP2A abrogates MgcRacGAP/Ect2 interaction. Therefore, PP2A may regulate cytokinesis by dephosphorylating MgcRacGAP and its interacting partners.

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