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

被引：33

作者：

Toure, Aminata ^{[1
]}

Mzali, Rym ^{[2
]}

Liot, Caroline ^{[2
]}

Seguin, Laetitia ^{[2
]}

Morin, Laurence ^{[1
]}

Crouin, Catherine ^{[2
]}

Chen-Yang, Ilin ^{[3
,4
]}

Tsay, Yeou-Guang ^{[3
,4
]}

Dorseuil, Olivier ^{[1
]}

Gacon, Gerard ^{[1
]}

Bertoglio, Jacques ^{[2
]}

机构：

[1] Univ Paris 05, Inst Cochin, Dept Genet & Dev, INSERM,CNRS,UMR 8104,U567, F-75014 Paris, France

[2] Fac Pharm Chatenay Malabry, INSERM, U749, F-92296 Chatenay Malabry, France

[3] Natl Yang Ming Univ, Inst Biochem & Mol Biol, Taipei 112, Taiwan

[4] Natl Yang Ming Univ, Prote Res Ctr, Taipei 112, Taiwan

来源：

FEBS LETTERS | 2008年 / 582卷 / 08期

关键词：

RhoGAP; phosphorylation; phosphoprotein phosphatase 2A; cytokinesis;

D O I：

10.1016/j.febslet.2007.12.036

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

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 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.

引用

页码：1182 / 1188

页数：7

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