학술논문
Regulations of mitoNEET by the key redox homeostasis molecule glutathione.
Document Type
Academic Journal
Author
Mons C; Université Paris-Saclay, Institut de Chimie des Substances Naturelles, CNRS UPR 2301, Gif-sur-Yvette cedex 91198, France.; Salameh M; Université Paris-Saclay, Institut de Chimie des Substances Naturelles, CNRS UPR 2301, Gif-sur-Yvette cedex 91198, France.; Botzanowski T; Laboratoire de Spectrométrie de Masse BioOrganique, Université de Strasbourg, CNRS, IPHC UMR 7178, Strasbourg 67000, France; Infrastructure Nationale de Protéomique ProFI - FR2048, Strasbourg 67000, France.; Clémancey M; Université Grenoble Alpes, CEA, CNRS, Laboratoire de Chimie et Biologie des Métaux (LCBM), Grenoble 38000, France.; Dorlet P; Université Paris-Saclay, CEA, CNRS, Institute for Integrative Biology of the Cell (I2BC), Gif-sur-Yvette cedex 91198, France; CNRS, Aix Marseille Université, BIP, IMM, Marseille cedex 09 13402, France.; Vallières C; Université Paris-Saclay, Institut de Chimie des Substances Naturelles, CNRS UPR 2301, Gif-sur-Yvette cedex 91198, France.; Erb S; Laboratoire de Spectrométrie de Masse BioOrganique, Université de Strasbourg, CNRS, IPHC UMR 7178, Strasbourg 67000, France; Infrastructure Nationale de Protéomique ProFI - FR2048, Strasbourg 67000, France.; Vernis L; Université Paris-Saclay, Institut de Chimie des Substances Naturelles, CNRS UPR 2301, Gif-sur-Yvette cedex 91198, France.; Guittet O; Université Paris-Saclay, Institut de Chimie des Substances Naturelles, CNRS UPR 2301, Gif-sur-Yvette cedex 91198, France.; Lepoivre M; Université Paris-Saclay, Institut de Chimie des Substances Naturelles, CNRS UPR 2301, Gif-sur-Yvette cedex 91198, France.; Huang ME; Université Paris-Saclay, Institut de Chimie des Substances Naturelles, CNRS UPR 2301, Gif-sur-Yvette cedex 91198, France.; Cianferani S; Laboratoire de Spectrométrie de Masse BioOrganique, Université de Strasbourg, CNRS, IPHC UMR 7178, Strasbourg 67000, France; Infrastructure Nationale de Protéomique ProFI - FR2048, Strasbourg 67000, France.; Latour JM; Université Grenoble Alpes, CEA, CNRS, Laboratoire de Chimie et Biologie des Métaux (LCBM), Grenoble 38000, France.; Blondin G; Université Grenoble Alpes, CEA, CNRS, Laboratoire de Chimie et Biologie des Métaux (LCBM), Grenoble 38000, France.; Golinelli-Cohen MP; Université Paris-Saclay, Institut de Chimie des Substances Naturelles, CNRS UPR 2301, Gif-sur-Yvette cedex 91198, France. Electronic address: marie-pierre.golinelli@cnrs.fr.
Source
Publisher: Elsevier Country of Publication: United States NLM ID: 7905788 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1873-3344 (Electronic) Linking ISSN: 01620134 NLM ISO Abbreviation: J Inorg Biochem Subsets: MEDLINE
Subject
Language
English
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 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.
Competing Interests: Declaration of competing interest The authors declare the following financial interests/personal relationships which may be considered as potential competing interests: Mons and Salameh report financial support was provided by French Ministry of National Education. Golinelli, Blondin and Cianferani reports financial support was provided by French National Research Agency. Vernis reports financial support was provided by INSERM. Cianferani reports financial support was provided by French Proteomic Infrastructure. Botzanowski reports financial support was provided by Institut de Recherches Internationales Servier. Blondin reports financial support was provided by Labex Arcane. If there are other authors, they declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.
(Copyright © 2024 The Authors. Published by Elsevier Inc. All rights reserved.)
Competing Interests: Declaration of competing interest The authors declare the following financial interests/personal relationships which may be considered as potential competing interests: Mons and Salameh report financial support was provided by French Ministry of National Education. Golinelli, Blondin and Cianferani reports financial support was provided by French National Research Agency. Vernis reports financial support was provided by INSERM. Cianferani reports financial support was provided by French Proteomic Infrastructure. Botzanowski reports financial support was provided by Institut de Recherches Internationales Servier. Blondin reports financial support was provided by Labex Arcane. If there are other authors, they declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.
(Copyright © 2024 The Authors. Published by Elsevier Inc. All rights reserved.)