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Regulations of mitoNEET by the key redox homeostasis molecule glutathione. 2024
Cécile Mons, and
Myriam Salameh, and
Thomas Botzanowski, and
Martin Clémancey, and
Pierre Dorlet, and
Cindy Vallières, and
Stéphane Erb, and
Laurence Vernis, and
Olivier Guittet, and
Michel Lepoivre, and
Meng-Er Huang, and
Sarah Cianferani, and
Jean-Marc Latour, and
Geneviève Blondin, and
Marie-Pierre Golinelli-Cohen
Université Paris-Saclay, Institut de Chimie des Substances Naturelles, CNRS UPR 2301, Gif-sur-Yvette cedex 91198, France.
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.
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