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
收藏
页码：892 / 896
页数：5
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