S-nitrosylation signaling in cell biology.

Benjamin M. Gaston, Jeannean Carver, Allan Doctor, Lisa A. Palmer

Research output: Contribution to journalReview articlepeer-review

172 Scopus citations


S-Nitrosylated proteins form when a cysteine thiol reacts with nitric oxide (NO) in the presence of an electron acceptor to form an S-NO bond. Under physiological conditions, this posttranslational modification affects the function a wide array of cell proteins, ranging from ion channels to nuclear regulatory proteins. Recent evidence suggests that 1) S-nitrosylated proteins can be synthesized by exposure of specific redox-active motifs to NO, through transnitrosation/transfer reactions, or through metalloprotein-catalyzed reactions; 2) S-nitrosothiols can be sequestered in membranes, lipophilic protein folds, or in vesicles to preserve their activity; and 3) S-nitrosothiols can be degraded by a number of enzymes systems. These recent insights regarding the bioactivities, molecular signaling pathways, and metabolism of endogenous S-nitrosothiols have suggested several new therapies for disease ranging from cystic fibrosis to pulmonary hypertension.

Original languageEnglish
Pages (from-to)253-263
Number of pages11
JournalMolecular interventions
Issue number5
StatePublished - Aug 2003


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