Dual Roles of Reducing Systems in Protein Persulfidation and Depersulfidation
2025
Liu, Zhichao | Rouhier, Nicolas | Couturier, Jérémy | Interactions Arbres-Microorganismes (IAM) ; Université de Lorraine (UL)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE) | Institut universitaire de France (IUF) ; Ministère de l'Education nationale, de l’Enseignement supérieur et de la Recherche (M.E.N.E.S.R.) | Lorraine Université d’Excellence, as part of the France 2030 Program (ANR-15-IDEX-04-LUE)ANR-11-LABX-0002-01, Lab of Excellence ARBRE | ANR-11-LABX-0002,ARBRE,Recherches Avancées sur l'Arbre et les Ecosytèmes Forestiers(2011)
International audience
Показать больше [+] Меньше [-]Английский. <div><p>The oxidative modification of specific cysteine residues to persulfides is thought to be the main way by which hydrogen sulfide (H 2 S) exerts its biological and signaling functions. Therefore, protein persulfidation represents an important thiol-switching mechanism as other reversible redox post-translational modifications. Considering their reductase activity but also their connections with proteins that generate H 2 S and its related molecules, the glutaredoxin (GRX) and thioredoxin (TRX)-reducing systems have potential dual roles in both protein persulfidation and depersulfidation. In this review, we will first focus on recent advances describing the physiological pathways leading to protein persulfidation before discussing the dual roles of the physiological TRX and glutathione/GRX-reducing systems in protein persulfidation/depersulfidation.</p></div>
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