Affiliation:
1. The authors are in the Department of Pharmacology, Weill Medical College of Cornell University, 1300 York Avenue, Room LC-218, New York, NY 10021, USA..
Abstract
Nitric oxide (NO) is a free-radical product of mammalian cell metabolism that plays diverse and important roles in the regulation of cell function. Biological actions of NO arise as a direct consequence of chemical reactions between NO or NO-derived species and protein targets. Reactions of NO with transition metals in target proteins have garnered the most attention to date as the principal mechanism of NO signaling; nonetheless,
S
-nitrosylation of protein Cys residues is rapidly moving to center stage in importance. In general, however, there has been a delay in adequate appreciation of the role of
S
-nitrosylation in biological signaling by NO. This lag is attributed to a poor understanding of the basis for selective targeting of NO to particular thiols, and methodological limitations in accurately quantifying this modification--recent breakthroughs in concepts and methods diminish these barriers. Here, we consider the wheres and whys of protein
S
-nitrosylation and its basis for specificity. Protein
S
-nitrosylation potentially represents a ubiquitous and fundamental mechanism for posttranslational control of protein activity on a par with that of
O
-phosphorylation.
Publisher
American Association for the Advancement of Science (AAAS)
Cited by
83 articles.
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