S-glutathionylation regulates GTP-binding of Rac2

被引：9

作者：

Kil, In Sup ^{[1
]}

Shin, Seoung Woo ^{[1
]}

Park, Jeen-Woo ^{[1
]}

机构：

[1] Kyungpook Natl Univ, Coll Nat Sci, Sch Life Sci & Biotechnol, Taegu 702701, South Korea

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 2012年 / 425卷 / 04期

基金：

新加坡国家研究基金会;

关键词：

Rac2; Cysteine; Glutathionylation; Structural alterations; GTP binding; NADPH OXIDASE; OXIDATIVE MODIFICATION; RESPIRATORY BURST; REDOX REGULATION; KAPPA-B; GLUTATHIOLATION; ACTIVATION; THIOLATION; DISULFIDE; KINASE;

D O I：

10.1016/j.bbrc.2012.07.169

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：

Phagocyte NADPH oxidase catalyzes the reduction of molecular oxygen to superoxide and is essential for defense against microbes. Rac2 is a low molecular weight GTP-binding protein that has been implicated in the regulation of phagocyte NADPH oxidase. Here we report that Cys(157) of Rac2 is a target of S-glutathionylation and that this modification is reversed by dithiothreitol as well as enzymatically by thioltransferase in the presence of GSH. S-glutathionylated Rac2 enhanced the binding of GTP, presumably due to structural alterations. These results elucidate the redox regulation of cysteine in Rac2 and a possible mechanism for regulating NADPH oxidase activation. (C) 2012 Elsevier Inc. All rights reserved.

引用

页码：892 / 896

页数：5

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