Sirtuins deacetylate and activate mammalian acetyl-CoA synthetases
By W. Hallows, Susan Lee, J. Denu. Proceedings of the National Academy of Sciences of the United States of America, 2006
833 citations recorded by the source corpus.
Subfields: Geriatrics and Gerontology, Physiology
View Paper: https://www.semanticscholar.org/paper/c8a6e4fedf2ca0a938817fba0b1a34318622b5d0
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In Geriatrics and Gerontology
In Physiology
Citations in the corpus
- Mammalian sirtuins--emerging roles in physiology, aging, and calorie restriction. (2006, background): “Two recent studies demonstrate that SIRT3 may regulate the activity of acetyl-CoA synthetase (AceCS) (Hallows et al. 2006; Schwer et al. 2006), representing a striking, conserved activity with the bacterial sirtuin, cobB (Tsang and Escalante-Semerena 1998; Starai et al.”
- Calorie restriction and SIRT3 trigger global reprogramming of the mitochondrial protein acetylome. (2013, neutral): “Hallows et al. (2011). Hirschey et al.”
- SIRT5 Deacetylates Carbamoyl Phosphate Synthetase 1 and Regulates the Urea Cycle (2009, positive): “SIRT3 deacetylates acetyl-CoA synthetase 2 (ACS2) at Lys-642 to regulate its activity (Hallows et al., 2006; Schwer et al., 2006).”
- Sirtuin Regulation of Mitochondria - Energy Production, Apoptosis, and Signaling (2010, background): “Surprisingly, many of the phenotypes observed in Sirt3-/- mice were also observed in mice lacking acetyl-CoA synthetase 2 (AceCS2), a previously identified substrate of SIRT3 [39,40].”
- Therapeutic application of histone deacetylase inhibitors for central nervous system disorders (2008, background): “Acetyl-CoA synthetase (ACS2) has been identified as a SIRT3 substrate; however other data suggest a broad role for SIRT3 in regulating global mitochondrial lysine acetylatio”
- Sirtuin 3, a New Target of PGC-1α, Plays an Important Role in the Suppression of ROS and Mitochondrial Biogenesis (2010, background): “Acetyl-CoA synthetase 2 (AceCS2), a mitochondrial enzyme that converts acetate into acetyl-CoA, was the first mitochondrial substrate of SIRT3 identified [23,24].”
- The world of protein acetylation. (2016, background): “Respectively, they are found in the cytosol and in themitochondria, and deacetylated by SIRT1 and SIRT3 [321].”
- Influence of Metabolism on Epigenetics and Disease (2013, positive): “On a more microscopic level, the involvement of the mitochondrial SIRT3 enzyme in the deacetylation of the acetyl-CoA synthase enzyme AceCS2 is revealing (Hallows et al., 2006; Schwer et al., 2006).”
- NAD(H) and NADP(H) Redox Couples and Cellular Energy Metabolism (2018, background): “In addition, SIRT1 has been found to activate acetyl-CoA synthetase 1 (AceCS1) by deacetylation, resulting in a pronounced increase in AceCS1-dependent fatty acid synthesis from acetate in Cos-7 cells (58).”
- Sirt3 Mediates Reduction of Oxidative Damage and Prevention of Age-related Hearing Loss under Caloric Restriction (2010, methodology): “Acetylated Idh2 in buffer (Tris [pH 7.5], with or without 1 mM NAD, and 1 mM DTT) was incubated with purified 50 nM Sirt3 or Sirt5 (Hallows et al., 2006) at 37 C for 1 hr, followed by Idh2 activity assay (n = 3).”