S-Nitrosylation Is Emerging as a Specific and Fundamental Posttranslational Protein Modification: Head-to-Head Comparison with O-Phosphorylation

Paul Lane, Gang Hao, and Steven S. Gross

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. E-mail: ssgross{at}med.cornell.edu.

Nitric oxide (NO) is a mammalian cell product that has been implicated in the control of essentially all cellular functions. Key to NO's bioactivity is its chemical reactivity. Recent studies suggest that a biologically important reaction of NO is with SH-groups on cysteine residues of proteins--this modification has been termed S-nitrosylation. Until recently, our appreciation of the importance of S-nitrosylation as a mechanism for posttranslational regulation of protein activity has been hindered by an inadequate understanding of how S-nitrosylation may be targeted to specific protein thiols and the lack of a simple method for identification of proteins that are S-nitrosylated in vivo. This review highlights emerging concepts and a new technique that may help to overcome these obstacles. A head-to-head comparison suggests that S-nitrosylation, like O-phosphorylation, may similarly play a fundamental role in the post-translational control of protein activity and cellular function.

Citation:
P. Lane, G. Hao, S. S. Gross, S-Nitrosylation Is Emerging as a Specific and Fundamental Posttranslational Protein Modification: Head-to-Head Comparison with O-Phosphorylation. Science's STKE (2001), http://stke.sciencemag.org/cgi/content/full/OC_sigtrans;2001/86/re1.

© 2001 American Association for the Advancement of Science

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