Rho small G-protein-dependent binding of mDia to an Src homology 3 domain-containing IRSp53/BAIAP2

被引：67

作者：

Fujiwara, T ^{[1
]}

Mammoto, A ^{[1
]}

Kim, Y ^{[1
]}

Takai, Y ^{[1
]}

机构：

[1] Osaka Univ, Grad Sch Med, Fac Med, Dept Mol Biol & Biochem, Suita, Osaka 5650871, Japan

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 2000年 / 271卷 / 03期

关键词：

D O I：

10.1006/bbrc.2000.2671

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：

mDial is a downstream effector of Rho small G: protein that is implicated in stress fiber formation and cytokinesis. We isolated an mDial-binding protein and identified it to be IRSp53/BAIAP2. IRSp53 and BAIAP2 have independently been isolated as a 58/53-kDa protein tyrosine phosphorylated in response to insulin and a BAI1-binding protein, respectively. BAI1 is a brain-specific seven-span transmembrane protein capable of inhibiting angiogenesis. The proline-rich formin homology 1 domain of mDial bound the Src homology 3 domain of IRSp53/BAIAP2 in a GTP-Rho-dependent manner. The results suggest that IRSp53/BAIAP2 is a downstream effector of mDial. (C) 2000 Academic Press.

引用

页码：626 / 629

页数：4

共 35 条

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