Defining the S-Glutathionylation Proteome by Biochemical and Mass Spectrometric Approaches.

ABSTRACT: Protein S-glutathionylation (SSG) is a reversible post-translational modification (PTM) featuring the conjugation of glutathione to a protein cysteine thiol. SSG can alter protein structure, activity, subcellular localization, and interaction with small molecules and other proteins. Thus, it plays a critical role in redox signaling and regulation in various physiological activities and pathological events. In this review, we summarize current biochemical and analytical approaches for characterizing SSG at both the proteome level and at individual protein levels. To illustrate the mechanism underlying SSG-mediated redox regulation, we highlight recent examples of functional and structural consequences of SSG modifications. Finally, we discuss the analytical challenges in characterizing SSG

SUBMITTER: Li X 

PROVIDER: S-EPMC9687251 | biostudies-literature | 2022 Nov

REPOSITORIES: biostudies-literature