Protein S-nitrosylation:: a physiological signal for neuronal nitric oxide

被引：1168

作者：

Jaffrey, SR

Erdjument-Bromage, H

Ferris, CD

Tempst, P

Snyder, SH ^{[1
]}

机构：

[1] Johns Hopkins Univ, Sch Med, Dept Neurosci, Baltimore, MD 21205 USA

[2] Johns Hopkins Univ, Sch Med, Dept Pharmacol & Mol Sci, Baltimore, MD 21205 USA

[3] Johns Hopkins Univ, Sch Med, Dept Psychiat, Baltimore, MD 21205 USA

[4] Mem Sloan Kettering Canc Ctr, Program Mol Biol, New York, NY 10021 USA

来源：

NATURE CELL BIOLOGY | 2001年 / 3卷 / 02期

关键词：

D O I：

10.1038/35055104

中图分类号：

Q2 [细胞生物学];

学科分类号：

071009 ; 090102 ;

摘要：

Nitric oxide (NO) has been linked to numerous physiological and pathophysiological events that ave not readily explained by the well established effects of NO on soluble guanylyl cyclase. Exogenous NO S-nitrosylates cysteine residues in proteins, but whether this is an important function of endogenous NO is unclear. Here, using a new proteomic approach, we identify a population of proteins that are endogenously S-nitrosylated, and demonstrate the loss of this modification in mice harbouring a genomic deletion of neuronal NO synthase (nNOS). Targets of NO include metabolic, structural and signalling proteins that may be effecters for neuronally generated PIG. These findings establish protein S-nitrosylation as a physiological signalling mechanism for nNOS.

引用

页码：193 / 197

页数：5

共 49 条

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