ArticleThe Journal of biological chemistry2016
Redox Control of the Human Iron-Sulfur Repair Protein MitoNEET Activity via Its Iron-Sulfur Cluster.
Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.
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Who cites it
44 citing papers in PubMed, 82 citations in OpenAlex.
- Gram-scale synthesis of the thiazolidinedione-based mitoNEET ligand NL-1 using a Hantzsch ester reduction.Tetrahedron letters · 2026Article
- Rust and redemption: iron-sulfur clusters and oxygen in human disease and health.Metallomics : integrated biometal science · 2025Review
- Article
- Redox-Guided DNA Scanning by the Dynamic Repair Enzyme Endonuclease III.Biochemistry · 2025Article
- Iron-sulfur protein odyssey: exploring their cluster functional versatility and challenging identification.Metallomics : integrated biometal science · 2024Review
- Biochemical and cellular characterization of the CISD3 protein: Molecular bases of cluster release and destabilizing effects of nitric oxide.The Journal of biological chemistry · 2024Article
- Dysregulated iron homeostasis in dystrophin-deficient cardiomyocytes: correction by gene editing and pharmacological treatment.Cardiovascular research · 2024Article
- Paramagnetic NMR to study iron sulfur proteins:Journal of biomolecular NMR · 2023Article
- PINK1 and Parkin regulate IPNature communications · 2023Article
- Biochemical Control of the Mitochondrial Protein MitoNEET by Biological Thiols and Lipid-derived Electrophiles.Advances in redox research · 2023Article
- Mitochondrial Aconitase ACO2 Links Iron Homeostasis with Tumorigenicity in Non-Small Cell Lung Cancer.Molecular cancer research : MCR · 2023Article
- The Intriguing mitoNEET: Functional and Spectroscopic Properties of a Unique [2Fe-2S] Cluster Coordination Geometry.Molecules (Basel, Switzerland) · 2022Review
- Electron transfer activity of the nanodisc-bound mitochondrial outer membrane protein mitoNEET.Free radical biology & medicine · 2022Article
- An anti-diabetic drug targets NEET (CISD) proteins through destabilization of their [2Fe-2S] clusters.Communications biology · 2022Article
- A VDAC1-mediated NEET protein chain transfers [2Fe-2S] clusters between the mitochondria and the cytosol and impacts mitochondrial dynamics.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Determination of the Absolute Molar Mass of [Fe-S]-Containing Proteins Using Size Exclusion Chromatography-Multi-Angle Light Scattering (SEC-MALS).Biomolecules · 2022Article
- Nitric oxide reversibly binds the reduced [2Fe-2S] cluster in mitochondrial outer membrane protein mitoNEET and inhibits its electron transfer activity.Frontiers in molecular biosciences · 2022Article
- Clinically relevant mitochondrial-targeted therapy improves chronic outcomes after traumatic brain injury.Brain : a journal of neurology · 2021Article
- Modulation of MagR magnetic properties via iron-sulfur cluster binding.Scientific reports · 2021Article
- Sulfur Administration in Fe-S Cluster Homeostasis.Antioxidants (Basel, Switzerland) · 2021Review
Corrections and comments
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Authors and funding
10 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Human mitoNEET (mNT) is the first identified Fe-S protein of the mammalian outer mitochondrial membrane. Recently, mNT has been implicated in cytosolic Fe-S repair of a key regulator of cellular iron homeostasis. Here, we aimed to decipher the mechanism by which mNT triggers its Fe-S repair capacity. By using tightly controlled reactions combined with complementary spectroscopic approaches, we have determined the differential roles played by both the redox state of the mNT cluster and dioxygen in cluster transfer and protein stability. We unambiguously demonstrated that only the oxidized state of the mNT cluster triggers cluster transfer to a generic acceptor protein and that dioxygen is neither required for the cluster transfer reaction nor does it affect the transfer rate. In the absence of apo-acceptors, a large fraction of the oxidized holo-mNT form is converted back to reduced holo-mNT under low oxygen tension. Reduced holo-mNT, which holds a [2Fe-2S](+)with a global protein fold similar to that of the oxidized form is, by contrast, resistant in losing its cluster or in transferring it. Our findings thus demonstrate that mNT uses an iron-based redox switch mechanism to regulate the transfer of its cluster. The oxidized state is the "active state," which reacts promptly to initiate Fe-S transfer independently of dioxygen, whereas the reduced state is a "dormant form." Finally, we propose that the redox-sensing function of mNT is a key component of the cellular adaptive response to help stress-sensitive Fe-S proteins recover from oxidative injury.
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