Litcius/Paper detail

Redox Regulation by Protein S-Glutathionylation: From Molecular Mechanisms to Implications in Health and Disease

Aysenur Musaogullari, Yuh-Cherng Chai

2020International Journal of Molecular Sciences105 citationsDOIOpen Access PDF

Abstract

S-glutathionylation, the post-translational modification forming mixed disulfides between protein reactive thiols and glutathione, regulates redox-based signaling events in the cell and serves as a protective mechanism against oxidative damage. S-glutathionylation alters protein function, interactions, and localization across physiological processes, and its aberrant function is implicated in various human diseases. In this review, we discuss the current understanding of the molecular mechanisms of S-glutathionylation and describe the changing levels of expression of S-glutathionylation in the context of aging, cancer, cardiovascular, and liver diseases.

Topics & Concepts

Context (archaeology)Cell biologyOxidative stressFunction (biology)GlutathioneMechanism (biology)BiologyOxidative phosphorylationReactive oxygen speciesChemistryBiochemistryEnzymePaleontologyEpistemologyPhilosophyRedox biology and oxidative stressSulfur Compounds in BiologyGlutathione Transferases and Polymorphisms