Regulation by S-Nitrosylation of Protein Post-translational Modification

被引：302

作者：

Hess, Douglas T. ^{[1
,2
]}

Stamler, Jonathan S. ^{[1
,2
,3
]}

机构：

[1] Case Western Reserve Univ, Inst Transformat Mol Med, Cleveland, OH 44106 USA

[2] Case Western Reserve Univ, Dept Med, Cleveland, OH 44106 USA

[3] Univ Hosp Case Med Ctr, Cleveland, OH USA

来源：

JOURNAL OF BIOLOGICAL CHEMISTRY | 2012年 / 287卷 / 07期

基金：

美国国家卫生研究院;

关键词：

NITRIC-OXIDE SYNTHASE; AKT/PROTEIN KINASE-B; NEURONAL CELL-DEATH; NF-KAPPA-B; PARKINSONS-DISEASE; TYROSINE PHOSPHATASES; MEDIATED DEGRADATION; SIGNAL-TRANSDUCTION; INSULIN-RESISTANCE; OXIDATIVE STRESS;

D O I：

10.1074/jbc.R111.285742

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：

Protein post-translational modification by S-nitrosylation conveys a ubiquitous influence of nitric oxide on signal transduction in eukaryotic cells. The wide functional purview of S-nitrosylation reflects in part the regulation by S-nitrosylation of the principal protein post-translational modifications that play a role in cell signaling, including phosphorylation, acetylation, ubiquitylation and related modifications, palmitoylation, and alternative Cys-based redox modifications. In this minireview, we discuss the mechanisms through which S-nitrosylation exerts its broad pleiotropic influence on protein post-translational modification.

引用

收藏

页码：4411 / 4418

页数：8

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