Phosphoregulation of MgcRacGAP in mitosis involves Aurora B and Cdk1 protein kinases and the PP2A phosphatase
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 B56ε, 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.
Structured summary:
physically interacts (MI:0218) with B56ε (uniprotkb:Q16537) by coimmunoprecipitation (MI:0019)
Keywords: RhoGAP, Phosphorylation, Phosphoprotein Phosphatase 2A, Cytokinesis
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PII: S0014-5793(08)00012-4
doi:10.1016/j.febslet.2007.12.036
© 2008 Federation of European Biochemical Societies
Refers to corrigendum:
- Corrigendum to “Phosphoregulation of MgcRacGAP in mitosis involves Aurora B and Cdk1 protein kinases and the PP2A phosphatase” [FEBS Lett. 582 (2008) 1182–1188] , 14 April 2008
