期刊
FEBS LETTERS
卷 582, 期 8, 页码 1182-1188出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.febslet.2007.12.036
关键词
RhoGAP; phosphorylation; phosphoprotein phosphatase 2A; cytokinesis
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 central-spindlin complex and associates with the RhoGEF Ect2. The GAP activity of MgcRacGAP is regulated by Aurora B phosphorylation. We have isolated B56 epsilon, 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 CdkI 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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