Glutathione in Protein Redox Modulation through S-Glutathionylation and S-Nitrosylation

S-glutathionylation and S-nitrosylation are reversible post-translational modifications on the cysteine thiol groups of proteins, which occur in cells under physiological conditions and oxidative/nitrosative stress both spontaneously and enzymatically. They are important for the regulation of the functional activity of proteins and intracellular processes. Connecting link and switch functions between S-glutathionylation and S-nitrosylation may be performed by GSNO, the generation of which depends on the GSH content, the GSH/GSSG ratio, and the cellular redox state. An important role in the regulation of these processes is played by Trx family enzymes (Trx, Grx, PDI), the activity of which is determined by the cellular redox status and depends on the GSH/GSSG ratio. In this review, we analyze data concerning the role of GSH/GSSG in the modulation of S-glutathionylation and S-nitrosylation and their relationship for the maintenance of cell viability.

Automated summary

S-glutathionylation and S-nitrosylation are reversible post-translational modifications on the cysteine thiol groups of proteins, important for regulating protein functional activity and cellular processes. The connection and switch functions between these modifications are performed by GSNO, dependent on factors like GSH content, GSH/GSSG ratio, and cellular redox state. Trx family enzymes play a crucial role in regulating these processes, with their activity determined by cellular redox status and GSH/GSSG ratio.