Fiche publication
Date publication
mars 2024
Journal
Journal of inorganic biochemistry
Auteurs
Membres identifiés du Cancéropôle Est :
Dr CIANFERANI Sarah
Tous les auteurs :
Mons C, Salameh M, Botzanowski T, Clémancey M, Dorlet P, Vallières C, Erb S, Vernis L, Guittet O, Lepoivre M, Huang ME, Cianferani S, Latour JM, Blondin G, Golinelli-Cohen MP
Lien Pubmed
Résumé
Human mitoNEET (mNT) and CISD2 are two NEET proteins characterized by an atypical [2Fe-2S] cluster coordination involving three cysteines and one histidine. They act as redox switches with an active state linked to the oxidation of their cluster. In the present study, we show that reduced glutathione but also free thiol-containing molecules such as β-mercaptoethanol can induce a loss of the mNT cluster under aerobic conditions, while CISD2 cluster appears more resistant. This disassembly occurs through a radical-based mechanism as previously observed with the bacterial SoxR. Interestingly, adding cysteine prevents glutathione-induced cluster loss. At low pH, glutathione can bind mNT in the vicinity of the cluster. These results suggest a potential new regulation mechanism of mNT activity by glutathione, an essential actor of the intracellular redox state.
Mots clés
CISD2, NEET proteins, glutathione, iron‑sulfur protein, mitoNEET, thiyl radicals
Référence
J Inorg Biochem. 2024 03 20;255:112535
