ArticleBiochemistry2010
Regulation of succinate dehydrogenase activity by SIRT3 in mammalian mitochondria.
Article in Biochemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 248 papers.
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Who cites it
248 citing papers in PubMed, 476 citations in OpenAlex.
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- Impact of mitochondrial reductive stress due to respiratory chain limitation on cancer via posttranslational modifications.Redox biology · 2026Review
- Targeting Sirtuins in Thyroid Cancer: Mechanisms, Drug Development, and Emerging Roles in Tumor Immunity and Ferroptosis.Cancers · 2026Review
- Subtype-specific sirtuin expression signatures link mitochondrial-epigenetic networks to breast cancer survival.GeroScience · 2026Article
- Review
- β-Nicotinamide mononucleotide preserves muscle strength in septic male mice.Scientific reports · 2026Article
- Mitochondria as key targets underlying hypomagnetic field-induced biological effects.iScience · 2026Review
- Targeting SIRT3 dysfunction with a sprayable honokiol hydrogel for diabetic burn wound repair.Frontiers in pharmacology · 2026Article
- Potential 14-3-3 binding sites in sirtuins reveal extended phosphosite-recognition modes.Acta crystallographica. Section F, Structural biology communications · 2026Article
- Establishing a direct interaction between the 19,20-EDP analog SA-22 and SIRT3: impact on cardiac mitochondrial homeostasis.Frontiers in pharmacology · 2026Article
- Sirtuins may mediate temperature-induced metabolic remodeling in threespine stickleback.Journal of comparative physiology. B, Biochemical, systemic, and environmental physiology · 2025Article
- Dynamic proteome profiling of differentiating human embryonic stem cells towards cardiomyocytes.Scientific reports · 2025Article
- Mitochondrial hyper-acetylation induced by an engineered acetyltransferase promotes cellular senescence.iScience · 2025Article
- Left ventricular myocardial molecular profile of human diabetic ischaemic cardiomyopathy.EMBO molecular medicine · 2025Article
- The protective effect of kaempferol on high glucose-stimulated renal tubular epithelial cells.BMC nephrology · 2025Article
- Mitochondrial sirtuins, key regulators of aging.Life medicine · 2025Review
- Are Hippocampal Hypoperfusion and ATP Depletion Prime Movers in the Genesis of Alzheimer's Disease? A Review of Recent Pertinent Observations from Molecular Biology.International journal of molecular sciences · 2025Review
- Metabolic reprogramming of the neovascular niche promotes regenerative angiogenesis in proliferative retinopathy.Nature communications · 2025Article
- Cardioprotective effect of 19,20-epoxydocosapentaenoic acid (19,20-EDP) in ischaemic injury involves direct activation of mitochondrial sirtuin 3.Cardiovascular research · 2025Article
- Unraveling the metabolic‒epigenetic nexus: a new frontier in cardiovascular disease treatment.Cell death & disease · 2025Review
188 more citing papers are in PubMed but not listed here.
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
A member of the sirtuin family of NAD(+)-dependent deacetylases, SIRT3, is identified as one of the major mitochondrial deacetylases located in mammalian mitochondria responsible for deacetylation of several metabolic enzymes and components of oxidative phosphorylation. Regulation of protein deacetylation by SIRT3 is important for mitochondrial metabolism, cell survival, and longevity. In this study, we identified one of the Complex II subunits, succinate dehydrogenase flavoprotein (SdhA) subunit, as a novel SIRT3 substrate in SIRT3 knockout mice. Several acetylated Lys residues were mapped by tandem mass spectrometry, and we determined the role of acetylation in Complex II activity in SIRT3 knockout mice. In agreement with SIRT3-dependent activation of Complex I, we observed that deacetylation of the SdhA subunit increased the Complex II activity in wild-type mice. In addition, we treated K562 cell lines with nicotinamide and kaempferol to inhibit deacetylase activity of SIRT3 and stimulate SIRT3 expression, respectively. Stimulation of SIRT3 expression decreased the level of acetylation of the SdhA subunit and increased Complex II activity in kaempherol-treated cells compared to control and nicotinamide-treated cells. Evaluation of acetylated residues in the SdhA crystal structure from porcine and chicken suggests that acetylation of the hydrophilic surface of SdhA may control the entry of the substrate into the active site of the protein and regulate the enzyme activity. Our findings constitute the first evidence of the regulation of Complex II activity by the reversible acetylation of the SdhA subunit as a novel substrate of the NAD(+)-dependent deacetylase, SIRT3.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.