期刊
NATURE CELL BIOLOGY
卷 3, 期 2, 页码 193-197出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/35055104
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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.
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