ArticleRedox report : communications in free radical research2023
Ndufaf2, a protein in mitochondrial complex I, interacts
Article in Redox report : communications in free radical research, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed, 5 citations in OpenAlex.
- NDUFAF2 promotes abdominal aortic aneurysm formation through mitochondrial dysfunction-induced apoptosis.iScience · 2026Article
- Article
- Fuzheng Huayu recipe inhibits alveolar macrophage M2 polarization and oxidative phosphorylation via METTL3-mediated NDUFA2 m6A modification.Journal of bioenergetics and biomembranes · 2025Article
- Development and Optimization of a Redox Enzyme-Based Fluorescence Biosensor for the Identification of MsrB1 Inhibitors.Antioxidants (Basel, Switzerland) · 2024Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
backgroundMethionine sulfoxide reductases are found in all aerobic organisms. They function in antioxidant defense, cellular regulation by reversible oxidation of methionine in proteins, and in protein structure. However, very few
methodsWe implemented a proximity labeling method, TurboID, to covalently link mitochondrial methionine sulfoxide reductase A (MSRA) to its binding partners in HEK293 cells. Proteomic analyses were performed to identify putative binding partners.
resultsWe show that human Ndufaf2, also called mimitin, is a binding partner of MSRA as well as all 3 MSRBs. We found that both methionine residues in Ndufaf2 were susceptible to oxidation by hydrogen peroxide and that the methionine sulfoxide reductases can reduce these methionine sulfoxide residues back to methionine.
conclusionMethionine sulfoxide reductases can reduce methionine sulfoxide back to methionine in Ndufaf2. In addition to a repair function, it also creates a mechanism that could regulate cellular processes by modulation of methionine oxidation in Ndufaf2.
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