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FEBS Lett. 2008 Apr 9;582(8):1182-8. doi: 10.1016/j.febslet.2007.12.036. Epub 2008 Jan 15.

Phosphoregulation of MgcRacGAP in mitosis involves Aurora B and Cdk1 protein kinases and the PP2A phosphatase.

Author information

1
Institut Cochin, Département de Génétique et Développement, INSERM U567/CNRS UMR8104/Université Paris Descartes, 24 rue du Faubourg Saint Jacques, 75014 Paris, France.

Erratum in

  • FEBS Lett. 2008 May 14;582(11):1635.

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.

PMID:
18201571
DOI:
10.1016/j.febslet.2007.12.036
[Indexed for MEDLINE]
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