Regulations of mitoNEET by the key redox homeostasis molecule glutathione.
J Inorg Biochem
; 255: 112535, 2024 Jun.
Article
em En
| MEDLINE
| ID: mdl-38527404
ABSTRACT
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 ß-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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Base de dados:
MEDLINE
Assunto principal:
Proteínas Mitocondriais
Limite:
Humans
Idioma:
En
Revista:
J Inorg Biochem
Ano de publicação:
2024
Tipo de documento:
Article
País de afiliação:
França