title: The Expanding Landscape of the Thiol Redox Proteome.
abstract: Cysteine occupies a unique place in protein chemistry. The nucleophilic thiol group allows cysteine to undergo a broad range of redox modifications beyond classical thiol-disulfide redox equilibria, including S-sulfenylation (-SOH), S-sulfinylation (-SO(2)H), S-sulfonylation (-SO(3)H), S-nitrosylation (-SNO), S-sulfhydration (-SSH), S-glutathionylation (-SSG), and others. Emerging evidence suggests that these post-translational modifications (PTM) are important in cellular redox regulation and protection against oxidative damage. Identification of protein targets of thiol redox modifications is crucial to understanding their roles in biology and disease. However, analysis of these highly labile and dynamic modifications poses challenges. Recent advances in the design of probes for thiol redox forms, together with innovative mass spectrometry based chemoproteomics methods make it possible to perform global, site-specific, and quantitative analyses of thiol redox modifications in complex proteomes. Here, we review chemical proteomic strategies used to expand the landscape of thiol redox modifications.
authors.affiliation: From the ‡National Center for Protein Sciences · Beijing, Beijing, 102206, China; §State Key Laboratory of Proteomics, Beijing Proteome Research Center, Beijing, 102206, China; yangjing54@hotmail.com Daniel.liebler@vanderbilt.edu.
authors.forename: Jing
authors.initials: J
authors.lastname: Yang
authors.affiliation: ¶Department of Chemistry, The Scripps Research Institute, Jupiter, Florida 33458;
authors.forename: Kate S
authors.initials: KS
authors.lastname: Carroll
authors.affiliation: ‖Department of Biochemistry, Vanderbilt University School of Medicine, Nashville, Tennessee 37232 yangjing54@hotmail.com Daniel.liebler@vanderbilt.edu.
authors.forename: Daniel C
authors.initials: DC
authors.lastname: Liebler
mesh_terms: D000818:Animals; D003545:Cysteine / Q000378:metabolism; D006801:Humans; D013058:Mass Spectrometry / Q000379:methods; D010084:Oxidation-Reduction; D011499:Protein Processing, Post-Translational; D020543:Proteome / Q000378:metabolism*; D040901:Proteomics / Q000379:methods*; D015203:Reproducibility of Results; D013438:Sulfhydryl Compounds / Q000378:metabolism*
chemical_list: D020543:Proteome; D013438:Sulfhydryl Compounds; D003545:Cysteine