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Regulation of protein function and signaling by reversible cysteine S-nitrosylation.

ABSTRACT: NO is a versatile free radical that mediates numerous biological functions within every major organ system. A molecular pathway by which NO accomplishes functional diversity is the selective modification of protein cysteine residues to form S-nitrosocysteine. This post-translational modification, S-nitrosylation, impacts protein function, stability, and location. Despite considerable advances with individual proteins, the in vivo biological chemistry, the structural elements that govern the selective S-nitrosylation of cysteine residues, and the potential overlap with other redox modifications are unknown. In this minireview, we explore the functional features of S-nitrosylation at the proteome level and the structural diversity of endogenously modified residues, and we discuss the potential overlap and complementation that may exist with other cysteine modifications.

SUBMITTER: Gould N

PROVIDER: S-EPMC3772194 | biostudies-literature | 2013 Sep

REPOSITORIES: biostudies-literature

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Regulation of protein function and signaling by reversible cysteine S-nitrosylation.

Gould Neal N Doulias Paschalis-Thomas PT Tenopoulou Margarita M Raju Karthik K Ischiropoulos Harry H

The Journal of biological chemistry 20130716 37

NO is a versatile free radical that mediates numerous biological functions within every major organ system. A molecular pathway by which NO accomplishes functional diversity is the selective modification of protein cysteine residues to form S-nitrosocysteine. This post-translational modification, S-nitrosylation, impacts protein function, stability, and location. Despite considerable advances with individual proteins, the in vivo biological chemistry, the structural elements that govern the sele ...[more]

PMID: 23861393

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