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S-nitrosylation of cysteine thiols in proteins by the highly labile NO radical has been identified as a important effector of NO-related bioactivity both in NOS-containing cells and intercellular signaling, regulating NO-derived signal transduction pathways.
S-nitrosylation of proteins serves as a ubiquitous post-translational modification that dynamically regulates a broad functional spectrum of proteins.
S-nitrosylation of cysteine thiols has been shown to contribute to the cGMP-independent effects of NO. NO-sensitive ion channels, including the cardiac and skeletal muscle ryanodine receptor (RyR1), N-methyl-D-aspartate receptor (NMDAR) complex, and cyclic-nucleotide gated ion channel, are modulated by S-nitrosylation of critical cysteine residues.
S-nitrosylation of capsase-3 inhibits apoptosis signaling. S-nitrosylation activates matrix metalloproteinase-9 (MMP-9) and induces neuronal apoptosis.The small G-protein p21Ras and Jun kinases are regulated by S-nitrosylation. The activity of transcription factors such as NFkB, c-jun, and c-fos is modulated by S-nitrosylation.
