SIRT3 weighs heavily in the metabolic balance: A new role for SIRT3 in metabolic syndrome

Journals of Gerontology - Series A Biological Sciences and Medical Sciences

Volumn 68, Issue 2, 2013, Pages 105-107

  Green, Michelle F ^a   Hirschey, Matthew D ^a,b  

^a DUKE UNIVERSITY   (United States)

^b DUKE UNIVERSITY MEDICAL CENTER   (United States)

Author keywords

Metabolic syndrome; SIRT3; Sirtuins

Indexed keywords

MITOCHONDRIAL PROTEIN; REACTIVE OXYGEN METABOLITE; SIRTUIN 3;

ANIMAL; GENETICS; HUMAN; INSULIN RESISTANCE; METABOLIC SYNDROME X; METABOLISM; MITOCHONDRION; NOTE; PHYSIOLOGY; SIGNAL TRANSDUCTION; SKELETAL MUSCLE;

ANIMALS; HUMANS; INSULIN RESISTANCE; METABOLIC SYNDROME X; MITOCHONDRIA; MITOCHONDRIAL PROTEINS; MUSCLE, SKELETAL; REACTIVE OXYGEN SPECIES; SIGNAL TRANSDUCTION; SIRTUIN 3;

EID: 84870352685     PISSN: 10795006     EISSN: 1758535X     Source Type: Journal    
DOI: 10.1093/gerona/gls132     Document Type: Article

References (23)

1. Bordone L, Guarente L. Calorie restriction, SIRT1 and metabolism: understanding longevity. Nat Rev Mol Cell Biol. 2005;6:298-305. (Pubitemid 40516896)
2. Reaven GM. Banting lecture 1988. Role of insulin resistance in human disease. Diabetes. 1988;37:1595-1607. (Pubitemid 19004941)
3. Edward JM. Caloric restriction-induced life extension of rats and mice: A critique of proposed mechanisms. Biochim Biophys Acta. 2009;1790:1040-1048.
4. Schwer B, Verdin E. Conserved metabolic regulatory functions of sirtuins. Cell Metabolism. 2008;7:104-112. (Pubitemid 351168554)
5. Lombard DB, Alt FW, Cheng HL, et al. Mammalian Sir2 homolog SIRT3 regulates global mitochondrial lysine acetylation. Mol Cell Biol. 2007; 27:8807-8814.
6. Hirschey MD, Shimazu T, Goetzman E, et al. SIRT3 regulates mitochon-drial fatty-acid oxidation by reversible enzyme deacetylation. Nature. 2010;464:121-125.
7. Qiu X, Brown K, Hirschey MD, Verdin E, Chen D. Calorie restriction reduces oxidative stress by SIRT3-mediated SOD2 activation. Cell Metabolism. 2010;12:662-667.
8. Hallows WC, Yu W, Smith BC, et al. Sirt3 promotes the urea cycle and fatty acid oxidation during dietary restriction. Mol Cell. 2011; 41:139-149.
9. Shimazu T, Hirschey MD, Hua L, et al. SIRT3 deacetylates mito-chondrial 3-hydroxy-3-methylglutaryl CoA synthase 2 and regulates ketone body production. Cell Metabolism. 2010;12:654-661.
10. Hirschey MD, Shimazu T, Jing E, et al. SIRT3 deficiency and mitochondrial protein hyperacetylation accelerate the development of the metabolic syndrome. Mol Cell. 2011; 44(2):177-190.
11. Jing E, Emanuelli B, Hirschey MD, et al. Sirtuin-3 (Sirt3) regulates skeletal muscle metabolism and insulin signaling via altered mitochondrial oxidation and reactive oxygen species production. Proc Natl Acad Sci U S A. 2011;108:14608-14613.
12. Cantó C, Auwerx J. Caloric restriction, SIRT1 and longevity. Trends Endocrinol Metabolism. 2009;20:325-331.
13. Du J, Zhou Y, Su X, et al. Sirt5 is a NAD-dependent protein lysine demalonylase and desuccinylase. Science. 2011;334:806-809.
14. Peng C, Lu Z, Xie Z, et al. The fi rst identifi cation of lysine malonyl-ation substrates and its regulatory enzyme. Mol Cell Proteomics. 2011;10. doi:10.1074/mcp.M111.012658
15. Kim SC, Sprung R, Yue C, et al. Substrate and functional diversity of lysine acetylation revealed by a proteomics survey. Mol Cell. 2006; 23:607-618. (Pubitemid 44205490)
16. Zhao S, Xu W, Jiang W, et al. Regulation of cellular metabolism by protein lysine acetylation. Science. 2010;327:1000-1004.
17. Wang Q, Zhang Y, Yang C, et al. Acetylation of metabolic enzymes coordinates carbon source utilization and metabolic flux. Science. 2010;327:1004-1007.
18. Choudhary C, Kumar C, Gnad F, et al. Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009;325:834-840.
19. Anderson KA, Hirschey MD. Mitochondrial protein acetylation regulates metabolism. Essays Biochem. In press.
20. Schwer B, Eckersdorff M, Li Y, et al. Calorie restriction alters mitochondrial protein acetylation. Aging Cell. 2009;8:604-606.
21. Matthew JP, Sr. Ethanol intoxication increases hepatic N-lysyl protein acetylation. Biochem Biophys Res Commun. 2008;376:615-619.
22. Kendrick AA, Choudhury M, Rahman SM, et al. Fatty liver is associated with reduced SIRT3 activity and mitochondrial protein hyperacetylation. Biochem J. 2011;433:505-514.
23. Giralt A, Hondares E, Villena JA, et al. Peroxisome proliferator- activated receptor-γ coactivator-1α controls transcription of the Sirt3 gene, an essential component of the thermogenic brown adipocyte phenotype. J Biol Chem. 2011;286:16958-16966.