A role for the mitochondrial deacetylase Sirt3 in regulating energy homeostasis

By B. Ahn, Hyunseok Kim, Shiwei Song, In Hye Lee, Jie Liu, Athanassios Vassilopoulos, C. Deng, Toren Finkel. Proceedings of the National Academy of Sciences of the United States of America, 2008

1,278 citations recorded by the source corpus.

Subfields: Geriatrics and Gerontology, Molecular Biology, Physiology

View Paper: https://www.semanticscholar.org/paper/45e7885f6175772ea605b65ac55d3a4949c240b3

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Citations in the corpus

SIRT5 Deacetylates Carbamoyl Phosphate Synthetase 1 and Regulates the Urea Cycle (2009, positive): “A recent report indicates that SIRT3 deacetylates a component of electron transport chain complex 1 and regulates energy homeostasis (Ahn et al., 2008).”
Sirt3 blocks the cardiac hypertrophic response by augmenting Foxo3a-dependent antioxidant defense mechanisms in mice. (2009, background): “Expression of SIRT3 has also been implicated in the synthesis and maintenance of cellular ATP levels in many tissues, including heart, liver, and kidney (10).”
Cellular Stress Responses, The Hormesis Paradigm, and Vitagenes: Novel Targets for Therapeutic Intervention in Neurodegenerative Disorders (2010, neutral): “In comparison with SIRT1, very little is known concerning the functions of SIRTs 2–7, but their differential subcellular localization is providing interesting clues; for example, SIRT3 is associated with mitochondria, where it may deacetylate protein substrates involved in energy metabolism (3).”
Melatonin--a pleiotropic, orchestrating regulator molecule. (2011, background): “In fibroblasts, SIRT3 was shown to physically interact with a complex I subunit, the 39-kDa protein NDUFA9, to enhance complex I activity and ATP levels (Ahn et al., 2008), at least a parallelism to findings with melatonin.”
Sirtuin 3, a New Target of PGC-1α, Plays an Important Role in the Suppression of ROS and Mitochondrial Biogenesis (2010, background): “Mouse SIRT3 is localized in the mitochondria and associated with energy metabolism [26,35].”
Therapeutic potential of NAD-boosting molecules: the in vivo evidence (2018, neutral): “SIRT2 controls gluconeogenesis by deacetylating phosphoenolpyruvate carboxykinase (Jiang et al., 2011); SIRT3 regulates OXPHOS (Ahn et al., 2008), fatty acid oxidation (Hirschey et al., 2010), ketogenesis (Shimazu et al., 2010), and defense against oxidative stress (Finley et al., 2011; Someya et al”
Sirt3-Mediated Deacetylation of Evolutionarily Conserved Lysine 122 Regulates MnSOD Activity in Response to Stress (2010, methodology): “…MnSOD and alters enzymatic activity, two lentiviruses were constructed that expressed either the wild-type (lenti-Sirt3-WT) or a deacetylation null mutant (lenti-Sirt3-DN) Sirt3 gene (a gift from Toren Finkel, NHLBI) in which amino acid 248 was changed from histidine to tyrosine (Ahn et al., 2008).”
SIRT3 Deficiency and Mitochondrial Protein Hyperacetylation Accelerate the Development of the Metabolic Syndrome (2011, positive): “SIRT3 is a mitochondrial sirtuin (Onyango et al., 2002; Schwer et al., 2002) and regulates fatty acid oxidation during fasting and ATP production (Ahn et al., 2008; Hirschey et al., 2010).”
The world of protein acetylation. (2016, positive): “In vivo knockoutmice have increasedmitochondrial acetylation [333,334].”
Mitochondrial Energetics and Therapeutics (2010, positive): “Sirt3 deacetylates various OXPHOS proteins and also modulates the mitochondrial metabolic rate (139).”
SIRT3 is a Mitochondrial Localized Tumor Suppressor Required for Maintenance of Mitochondrial Integrity and Metabolism During Stress (2010, methodology): “As such, SIRT3 / Myc/Ras cells were infected with lentivirus expressing either a wild-type SIRT3 (lenti-SIRT3wt) or a deacetylation null mutant SIRT3 (Ahn et al., 2008) gene (lenti-SIRT3-dn).”
REACTIVE OXYGEN SPECIES, CELLULAR REDOX SYSTEMS AND APOPTOSIS (2010, positive): “For instance, Sirt3-mediated deacetylation of mitochondrial complex I engaged ATP production under normal homeostatic conditions, while decreased ATP generation during oxidant exposure resulted from Sirt3 dissociation and complex I acetylation [90].”
SIRTUIN 1 AND SIRTUIN 3: PHYSIOLOGICAL MODULATORS OF METABOLISM (2012, background): “These results suggest that SIRT3 plays an important role in regulating ATP synthesis in mitochondria and thus is a potential regulator of mitochondrial energy metabolism (5).”
Sirt3 Mediates Reduction of Oxidative Damage and Prevention of Age-related Hearing Loss under Caloric Restriction (2010, background): “regulates levels of ATP and the activity of complex I of the electron transport chain (Ahn et al., 2008) and, as such, may play a role in the metabolic reprogramming mediated by CR.”
Sirtuins as regulators of metabolism and healthspan (2012, neutral): “Moreover, SIRT3 deacetylates components of complex”
PARP-1 inhibition increases mitochondrial metabolism through SIRT1 activation (2011, neutral): “If increased SIRT1 activity was mainly driven by changes in NAD+, the unchanged SIRT2 and SIRT3 activities in PARP-1 / tissues suggest that the increase in NAD+ is either not enough to enhance SIRT2 and SIRT3 activities or that it only happens in specific cellular compartments, supporting an indepen”
The secret life of NAD+: an old metabolite controlling new metabolic signaling pathways. (2010, background): “SIRT3 action has been related to adaptive thermogenesis (80), mitochondrial function (80), energy homeostasis (118), and cellular survival during genotoxic stress (95).”