The Redox Biochemistry of Protein Sulfenylation and Sulfinylation

• Published in: The Journal of biological chemistry Vol. 288; no. 37; pp. 26480 - 26488
• Main Authors: Lo Conte, Mauro, Carroll, Kate S.
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 13.09.2013; American Society for Biochemistry and Molecular Biology
• Subjects: Animals; Cysteine - analogs & derivatives; Cysteine - chemistry; Cysteine Oxidation; Gene Expression Regulation; Humans; Hydrogen Peroxide; Hydrogen Peroxide - chemistry; Ions; Minireviews; Oxidation-Reduction; Oxygen - chemistry; Post-translational Modification; Protein Processing, Post-Translational; Protein Tyrosine Phosphatases - chemistry; Proteins - chemistry; Reactive Oxygen Species; Redox Regulation; Redox Signaling; Signal Transduction; Sulfenic Acids - chemistry; Sulfhydryl Compounds - chemistry; Thiol; Cysteine Oxidation; Redox Regulation; Thiol; Post-translational Modification; Hydrogen Peroxide; Redox Signaling
• ISSN: 0021-9258; 1083-351X; 1083-351X
• DOI: 10.1074/jbc.R113.467738

Controlled generation of reactive oxygen species orchestrates numerous physiological signaling events (Finkel, T. (2011) Signal transduction by reactive oxygen species. J. Cell Biol. 194, 7–15). A major cellular target of reactive oxygen species is the thiol side chain (RSH) of Cys, which may assume a wide range of oxidation states (i.e. −2 to +4). Within this context, Cys sulfenic (Cys-SOH) and sulfinic (Cys-SO2H) acids have emerged as important mechanisms for regulation of protein function. Although this area has been under investigation for over a decade, the scope and biological role of sulfenic/sulfinic acid modifications have been recently expanded with the introduction of new tools for monitoring cysteine oxidation in vitro and directly in cells. This minireview discusses selected recent examples of protein sulfenylation and sulfinylation from the literature, highlighting the role of these post-translational modifications in cell signaling.