Table 1.
A list of enzymes, receptors and regulatory proteins for which the literature reports evidence or hint that they are reversibly glutathionylated and/or are substrates for glutaredoxins (Grx) (re-elaborated and integrated from Deponte [129], Copyright 2013, Elsevier B.V., and Kil and Park [141], Copyright 2005, American Society for Biochemistry and Molecular Biology).
| Enzyme | Consequences of S-glutathionylation |
|---|---|
| glycolytic enzymes | alters enzymatic activity |
| glyceraldehyde-3-phosphate dehydrogenase | inactivated by S-glutathionylation |
| isocitrate dehydrogenases (ICDHs1; EC 1.1.1.41 and EC 1.1.1.42) | regulated by S-glutathionylation |
| creatine kinase | inactivation |
| carbonic anhydrase III | reversible regulation of phosphatase activity |
| components of the respiratory chain | formation of ROS |
| reversible glutathionylation of complex I increases mitochondrial superoxide formation | |
| Actin | polymerization and effect on cytoskeleton |
| membrane receptors, transporters and ion channels | alters ion and metabolite transport |
| causes cell death | |
| several protein kinases and phosphatases | alters signal transduction |
| protein kinase C (12), guanylate cyclase | alters enzymatic activity |
| nuclear factor I | alters signal transduction |
| Ras | alters signal transduction |
| c-Jun | redox-regulated by mechanisms that include protein S-thiolation |
| ubiquitin-activating enzymes | when cells are exposed to oxidants are glutathionylated, with a concomitant decrease in the ubiquitinination pathway |
| NFκB | redox-induced inhibition of DNA binding; cell death |