Phosphoregulation of MgcRacGAP in mitosis involves Aurora B and Cdk1 protein kinases and the PP2A phosphatase
- 作者：Aminata Touré ; Rym Mzali ; Caroline Liot ; Laetitia Seguin ; Laurence Morin ; Catherine Crouin ; Ilin Chen-Yang ; Yeou-Guang Tsay ; Olivier Dorseuil ; Gé ; rard Gacon ; Jacques Bertoglio
- 关键词：RhoGAP ; Phosphorylation ; Phosphoprotein Phosphatase 2A ; Cytokinesis
- 刊名：FEBS Letters
- 出版年：2008
- 期刊代码：70_00145793
- 类别：bio
- 出版时间：9 April 2008
- 卷：582
- 期：8
- 页码：1182-1188
- 文件大小：280 K
摘要
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.