Reversible lysine acetylation controls the activity of the mitochondrial enzyme acetyl-CoA synthetase 2

By B. Schwer, J. Bunkenborg, R. Verdin, Jens S. Andersen, E. Verdin. Proceedings of the National Academy of Sciences of the United States of America, 2006

733 citations recorded by the source corpus.

Subfields: Cell Biology, Geriatrics and Gerontology

View Paper: https://www.semanticscholar.org/paper/275bf740cc9a93a9a6644f0ce24fc04c5fbeec74

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Cell Biology

1. Eyal Gottlieb
2. E. Seto
3. M. Haigis
4. Xiang-Jiao Yang

In Geriatrics and Gerontology

1. Johan Auwerx
2. C. Cantó
3. E. Verdin
4. R. Houtkooper
5. M. Haigis
6. E. Seto
7. L. Guarente
8. Xiang-Jiao Yang

Citations in the corpus

• Influence of Metabolism on Epigenetics and Disease (2013, unknown): “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).”
• Lysine acetylation: codified crosstalk with other posttranslational modifications (2008, background): “Lysine acetylation has also been found in many cytoplasmic enzymes, including acetyl-CoA synthase (Starai et al., 2002; Hallows et al., 2006; Schwer et al., 2006), glutamate dehydrogenase (Lombard et al., 2007), nitric oxide synthase (Mattagajasingh et al., 2007), and other metabolic enzymes (Kim…”
• The secret life of NAD+: an old metabolite controlling new metabolic signaling pathways. (2010, background): “An alternative, or complementary, explanation is that SIRT3 regulates the acetylation status of additional mitochondrial proteins, among which are glutamate dehydrogenase (GDH) (119) and acetyl-CoA synthetase 2 (120), which could also affect mitochondrial and global energy metabolism.”
• 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. 2002).”
• NAD+/NADH and NADP+/NADPH in Cellular Functions and Cell Death: Regulation and Biological Consequences (2008, unknown): “In mammalian cells it appears that SIRT1 can deacetylate and activate acetyl-CoA synthetase 1 in cytosol (114), while SIRT3 can deacetylate and activate acetyl-CoA synthetase 2 in mitochondria (114, 257); and f) the NADH/NAD ratio is one of the modulators of MPT pore opening (352), which can signifi”
• Sirt3-Mediated Deacetylation of Evolutionarily Conserved Lysine 122 Regulates MnSOD Activity in Response to Stress (2010, background): “It has previously been shown that substitution of a lysine with a glutamine mimics an acetylated amino acid state, while substitution with an arginine mimics deacetylation (Li et al., 2007; Schwer et al., 2006).”
• SIRT5 Deacetylates Carbamoyl Phosphate Synthetase 1 and Regulates the Urea Cycle (2009, unknown): “SIRT3 deacetylates acetyl-CoA synthetase 2 (ACS2) at Lys-642 to regulate its activity (Hallows et al., 2006; Schwer et al., 2006).”
• Sirtuins: critical regulators at the crossroads between cancer and aging (2007, background): “Deacetylation of acetyl-CoA synthetase 2 activates the enzyme and promotes the production of acetyl-CoA (Hallows et al., 2006; Schwer et al., 2006).”
• Acetyl-CoA Synthetase 2 Promotes Acetate Utilization and Maintains Cancer Cell Growth under Metabolic Stress (2015, methodology): “Hypoxia and Low-Serum Culture Conditions Synergistically Enhance ACSS2 Expression The Cancer Cell Line Encyclopedia was used to identify breast cancer cell lines with strong evidence for ACSS2 copynumber gain and upregulation (Barretina et al., 2012; Forbes et al., 2011; Shao et al., 2013).”