| Literature DB >> 18201571 |
Aminata Touré1, Rym Mzali, Caroline Liot, Laetitia Seguin, Laurence Morin, Catherine Crouin, Ilin Chen-Yang, Yeou-Guang Tsay, Olivier Dorseuil, Gérard Gacon, Jacques Bertoglio.
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.Entities:
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Year: 2008 PMID： 18201571 DOI： 10.1016/j.febslet.2007.12.036
Source DB: PubMed Journal: FEBS Lett ISSN： 0014-5793 Impact factor: 4.124