Protein S-glutathionylation, the reversible formation of mixed disulfides between glutathione and low-pK, cysteinyl residues, not only is a cellular response to mild oxidative/nitrosative stress, but also occurs under basal (physiological) conditions. S-glutathionylation has now emerged as a potential mechanism for dynamic, posttranslational regulation of a variety of regulatory, structural, and metabolic proteins. Moreover, substantial recent studies have implicated S-glutathionylation in the regulation of signaling and metabolic pathways in intact cellular systems. The growing list of S-glutathionylated proteins, in both animal and plant cells, attests to the occurrence of S-glutathionylation in cellular response pathways. The existence of antioxidant enzymes that specifically regulate S-glutathionylation would emphasize its importance in modulating protein function, suggesting that this protein modification too might have a role in cell signaling. The continued development of proteomic and analytical methods for disulfide analysis will help us better understand the full extent of the roles these modifications play in the regulation of cell function. In this review, we describe recent breakthroughs in our understanding of the potential role of protein S-glutathionylation in the redox regulation of signal transduction.
|Titolo:||S-glutathionylation in protein redox regulation|
|Parole Chiave:||Free radicals; Glutathione; GSH/GSSG ratio; Mixed disulfides; Oxidative stress; Protein thiols; Reactive thiolate anions; Redox regulation; Signal transduction|
|Settore Scientifico Disciplinare:||Settore BIO/06 - Anatomia Comparata e Citologia|
|Data di pubblicazione:||2007|
|Digital Object Identifier (DOI):||10.1016/j.freeradbiomed.2007.06.014|
|Appare nelle tipologie:||01 - Articolo su periodico|