Succinate Dehydrogenase Is a Direct Target of Sirtuin 3 Deacetylase Activity
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Summary
This study identifies SDHA as a binding partner and substrate for Sirt3 deacetylase activity, suggesting that SIRT3 may be an important physiological regulator of SDH activity.
- Type
- article
- Published
- 2011-08-17
- Cited by
- 370
- References
- 40
- Access
- Open access
- OpenAlex
- https://openalex.org/W1979815517
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:11762801
Keywords
SDHA, SIRT3, Sirtuin, NAD+ kinase, Acetylation
References
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- Progress in understanding structure–function relationships in respiratory chain complex II
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- SIRT3, a Mitochondrial Sirtuin Deacetylase, Regulates Mitochondrial Function and Thermogenesis in Brown Adipocytes*
- Recent progress in the biology and physiology of sirtuins
- Peroxisome Proliferator-activated Receptor-γ Coactivator-1α Controls Transcription of the Sirt3 Gene, an Essential Component of the Thermogenic Brown Adipocyte Phenotype*
- Stop and go extraction tips for matrix-assisted laser desorption/ionization, nanoelectrospray, and LC/MS sample pretreatment in proteomics.
- Lysine Acetylation Targets Protein Complexes and Co-Regulates Major Cellular Functions
- A role for the mitochondrial deacetylase Sirt3 in regulating energy homeostasis
- Substrate and functional diversity of lysine acetylation revealed by a proteomics survey.
- Sirt3-Mediated Deacetylation of Evolutionarily Conserved Lysine 122 Regulates MnSOD Activity in Response to Stress
- Substrates and regulation mechanisms for the human mitochondrial sirtuins Sirt3 and Sirt5.
- Crystal structure of mitochondrial respiratory membrane protein complex II.
- Sirt3 blocks the cardiac hypertrophic response by augmenting Foxo3a-dependent antioxidant defense mechanisms in mice.
- SIRT4 inhibits glutamate dehydrogenase and opposes the effects of calorie restriction in pancreatic beta cells.
- Reversible lysine acetylation controls the activity of the mitochondrial enzyme acetyl-CoA synthetase 2
- Sirt3 promotes the urea cycle and fatty acid oxidation during dietary restriction
- Calorie restriction reduces oxidative stress by SIRT3-mediated SOD2 activation.
Cited by
- Impaired TCA cycle flux in mitochondria in skeletal muscle from type 2 diabetic subjects: Marker or maker of the diabetic phenotype?
- An anticancer agent, pyrvinium pamoate inhibits the NADH-fumarate reductase system--a unique mitochondrial energy metabolism in tumour microenvironments.
- Sirtuins in Renal Health and Disease.
- The role Of sirtuin3 in regulating mitochondrial superoxide metabolism in response to ionizing radiation in mouse embryonic fibroblasts.
- The role of MnSOD and Sirtuin 3 in thymocyte responses to radiation and lymphomagenesis
- Biochemical and structural characterization of Sirtuins from mammals and Thermotoga maritima
- Rôle de la dysfonction mitochondriale dans deux maladies neurodégénératives, la Maladie de Huntington et la Maladie de Parkinson
- Impaired mitochondrial energy metabolism in Alzheimer's disease: Impact on pathogenesis via disturbed epigenetic regulation of chromatin landscape.
- The Role of Mitochondrial Dysfunction in Age-Related Diseases
- Sirtuins: double players in Huntington's disease.
- PGC-1α/ERRα-Sirt3 Pathway Regulates DAergic Neuronal Death by Directly Deacetylating SOD2 and ATP Synthase β
- Caffeic acid attenuates rat liver reperfusion injury through sirtuin 3-dependent regulation of mitochondrial respiratory chain.
- Impact of caloric restriction on myocardial ischaemia/reperfusion injury and new therapeutic options to mimic its effects
- Nuclear respiratory factor 2 induces SIRT3 expression
- Sirtuins and the metabolic hurdles in cancer
- Mitochondrial complex II is a source of the reserve respiratory capacity that is regulated by metabolic sensors and promotes cell survival
- Bioinformatic and molecular study of the regulation of SIRT3 expression
- The updated biology of hypoxia‐inducible factor
- Identification of the Acetylation and Ubiquitin-Modified Proteome during the Progression of Skeletal Muscle Atrophy
- Calorie restriction influences key metabolic enzyme activities and markers of oxidative damage in distinct mouse liver mitochondrial sub-populations
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