Redox Regulation of Actin by Thioredoxin-1 Is Mediated by the Interaction of the Proteins via Cysteine 62

被引：31

作者：

Wang, Xiaogang ^{[1
]}

Ling, Shukuan ^{[1
]}

Zhao, Dingsheng ^{[1
]}

Sun, Qiao ^{[1
]}

Li, Qi ^{[1
]}

Wu, Feng ^{[1
]}

Nie, Jielin ^{[1
]}

Qu, Lina ^{[1
]}

Wang, Bo ^{[1
]}

Shen, Xun ^{[2
,3
]}

Bai, Yanqiang ^{[1
]}

Li, Yingxian ^{[1
]}

Li, Yinghui ^{[1
]}

机构：

[1] China Astronaut Res & Training Ctr, Dept Cellular & Mol Biol, State Key Lab Space Med Fundamentals & Applicat, Beijing, Peoples R China

[2] Chinese Acad Sci, Inst Biophys, Beijing 100080, Peoples R China

[3] Chinese Acad Sci, Grad Sch, Beijing 100080, Peoples R China

来源：

ANTIOXIDANTS & REDOX SIGNALING | 2010年 / 13卷 / 05期

基金：

中国国家自然科学基金;

关键词：

OXIDATIVE STRESS; BETA-ACTIN; CELL-DEATH; CYTOSKELETON; APOPTOSIS; KINASE; YEAST;

D O I：

10.1089/ars.2009.2833

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：

Actin is a highly conserved protein in eukaryotic cells, and has been identified as one of the main redox targets by redox proteomics under oxidative stress. However, little is known about the mechanisms of regulation of the redox state of actin. In this study, we investigated how thioredoxin-1 (Trx1) affected the redox state of actin and its polymerization under oxidative stress in SH-SY5Y cells. Trx1 decreased the levels of reactive oxygen species (ROS) in the cells, and cysteine residues at positions 32, 35, and 69 of the Trx1 protein were active sites for redox regulation. Actin could be kept in a reduced state by Trx1 under H2O2 stimulation. A physical interaction was found to exist between actin and Trx1. Cysteine 62 in Trx1 was the key site that interacted with actin, and it was required to maintain cellular viability and anti-apoptotic function. Taken together, these results suggested that Trx1 could protect cells from apoptosis under oxidative stress not only by increasing the total antioxidant capability and decreasing the ROS levels, but also by stabilizing the actin cytoskeletal system, which cooperatively contributed to the enhancement of cell viability and worked against apoptosis. Antioxid. Redox Signal. 13, 565-573.

引用

页码：565 / 573

页数：9

共 21 条

[1] Regulated protein denitrosylation by cytosolic and mitochondrial thioredoxins [J].