Sulfiredoxin Redox-Sensitive Interaction with S100A4 and Non-Muscle Myosin IIA Regulates Cancer Cell Motility

被引：33

作者：

Bowers, Robert R. ^{[1
]}

Manevich, Yefim ^{[1
]}

Townsend, Danyelle M. ^{[2
]}

Tew, Kenneth D. ^{[1
]}

机构：

[1] Med Univ S Carolina, Dept Cell & Mol Pharmacol & Expt Therapeut, Charleston, SC 29425 USA

[2] Med Univ S Carolina, Dept Pharmaceut & Biomed Sci, Charleston, SC 29425 USA

来源：

BIOCHEMISTRY | 2012年 / 51卷 / 39期

基金：

美国国家卫生研究院;

关键词：

CYSTEINE-SULFINIC ACID; S-GLUTATHIONYLATION; STRUCTURAL-CHANGES; SCAFFOLD PROTEINS; LUNG-CANCER; IN-VITRO; PEROXIREDOXIN; METASTASIS; MECHANISM; FAMILY;

D O I：

10.1021/bi301006w

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：

Sulfiredoxin (Srx) is a redox active protein that participates in the reduction of oxidized cysteine residues. Here we identify a novel function of Srx through its specific binding to S-glutathionylated S100A4 affecting its interaction with nonmuscle myosin (NMIIA), thereby modulating the effect of S100A4 on NMIIA function and impacting cell adhesion and migration. Srx forms a complex with S100A4 (and has stronger affinity for S-glutathionylated S100A4), regulates its activity, and mediates redox regulation of the interaction of S100A4 with NMIIA The consequence of this regulation is microfilament remodeling and altered cellular motility and adhesion. Srx-overexpressing cells had reduced levels of adhesion, decreased levels of Tyr(397)-phosphorylated focal adhesion kinase, and increased cell motility in wound healing assays. These results describe a novel redox-sensitive role for Srx in mediating complex protein interactions with plausible consequences for cancer cell motility.

引用

页码：7740 / 7754

页数：15

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