Emerging Role of Sirtuin 2 in the Regulation of Mammalian Metabolism

Trends in Pharmacological Sciences

Volumn 36, Issue 11, 2015, Pages 756-768

  Gomes, Pedro ^a   Fleming Outeiro, Tiago ^b,c   Cavadas, Cláudia ^a,d  

^a UNIVERSITY OF COIMBRA   (Portugal)

^b NOVA MEDICAL SCHOOL   (Portugal)

^c UNIVERSITY MEDICAL CENTER GÖTTINGEN   (Germany)

^d UNIVERSITY OF COIMBRA   (Portugal)

Author keywords

[No Author keywords available]

Indexed keywords

GLUCOSE; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; INSULIN; MITOGEN ACTIVATED PROTEIN KINASE; PROTEIN KINASE B; REACTIVE OXYGEN METABOLITE; TRANSCRIPTION FACTOR FKHR; SIRTUIN 2;

ADIPOGENESIS; CARCINOGENESIS; CELL CYCLE REGULATION; DRUG TARGETING; FATTY ACID OXIDATION; GLUCONEOGENESIS; GLUCOSE METABOLISM; HUMAN; HUNTINGTON CHOREA; INFLAMMATION; INSULIN SENSITIVITY; LIPID METABOLISM; LIPOGENESIS; MAMMAL; METABOLIC DISORDER; METABOLIC REGULATION; NERVE DEGENERATION; NON INSULIN DEPENDENT DIABETES MELLITUS; NONHUMAN; OXIDATIVE STRESS; PARKINSON DISEASE; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN TARGETING; REVIEW; TISSUE DISTRIBUTION; ANIMAL; CELL CYCLE; HOMEOSTASIS; METABOLISM;

ANIMALS; CELL CYCLE; GLUCOSE; HOMEOSTASIS; HUMANS; LIPID METABOLISM; SIRTUIN 2;

EID: 84946227815     PISSN: 01656147     EISSN: 18733735     Source Type: Journal    
DOI: 10.1016/j.tips.2015.08.001     Document Type: Review

References (102)

1. J. Rine, and et al. A suppressor of mating-type locus mutations in Saccharomyces cerevisiae: evidence for and identification of cryptic mating-type loci Genetics 93 1979 877 901
2. M. Kaeberlein, and et al. The SIR2/3/4 complex and SIR2 alone promote longevity in Saccharomyces cerevisiae by two different mechanisms Genes Dev. 13 1999 2570 2580
3. H.A. Tissenbaum, and L. Guarente Increased dosage of a sir-2 gene extends lifespan in Caenorhabditis elegans Nature 410 2001 227 230
4. B. Rogina, and S.L. Helfand Sir2 mediates longevity in the fly through a pathway related to calorie restriction Proc. Natl. Acad. Sci. U.S.A. 101 2004 15998 16003
5. S. Imai, and et al. Transcriptional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase Nature 403 2000 795 800
6. J.C. Tanny, and et al. An enzymatic activity in the yeast Sir2 protein that is essential for gene silencing Cell 99 1999 735 745
7. S.J. Lin, and et al. Requirement of NAD and SIR2 for life-span extension by calorie restriction in Saccharomyces cerevisiae Science 289 2000 2126 2128
8. C. Burnett, and et al. Absence of effects of Sir2 overexpression on lifespan in C. elegans and Drosophila Nature 477 2011 482 485
9. R.H. Houtkooper, and et al. Sirtuins as regulators of metabolism and healthspan Nat. Rev. Mol. Cell Biol. 13 2012 225 238
10. R.A. Frye Phylogenetic classification of prokaryotic and eukaryotic Sir2-like proteins Biochem. Biophys. Res. Commun. 273 2000 793 798
11. +-dependent histone deacetylase SIRT1 J. Biol. Chem. 282 2007 6823 6832
12. R. Mostoslavsky, and et al. Genomic instability and aging-like phenotype in the absence of mammalian SIRT6 Cell 124 2006 315 329
13. E. Ford, and et al. Mammalian Sir2 homolog SIRT7 is an activator of RNA polymerase I transcription Genes Dev. 20 2006 1075 1080
14. J.Y. Huang, and et al. Mitochondrial sirtuins Biochim. Biophys. Acta 1804 2010 1645 1651
15. A. Vaquero, and et al. SirT2 is a histone deacetylase with preference for histone H4 Lys 16 during mitosis Genes Dev. 20 2006 1256 1261
16. D. Rauh, and et al. An acetylome peptide microarray reveals specificities and deacetylation substrates for all human sirtuin isoforms Nat. Commun. 4 2013 2327
17. Y.B. Teng, and et al. Efficient demyristoylase activity of SIRT2 revealed by kinetic and structural studies Sci. Rep. 5 2015 8529
18. M.C. Haigis, and et al. SIRT4 inhibits glutamate dehydrogenase and opposes the effects of calorie restriction in pancreatic beta cells Cell 126 2006 941 954
19. G. Liszt, and et al. Mouse Sir2 homolog SIRT6 is a nuclear ADP-ribosyltransferase J. Biol. Chem. 280 2005 21313 21320
20. J. Du, and et al. Sirt5 is a NAD-dependent protein lysine demalonylase and desuccinylase Science 334 2011 806 809
21. Y. Han, and et al. Acetylation of Sirt2 by p300 attenuates its deacetylase activity Biochem. Biophys. Res. Commun. 375 2008 576 580
22. C. Escande, and et al. Deleted in breast cancer-1 regulates SIRT1 activity and contributes to high-fat diet-induced liver steatosis in mice J. Clin. Invest. 120 2010 545 558
23. + Mol. Cell 44 2011 851 863
24. R. Pandithage, and et al. The regulation of SIRT2 function by cyclin-dependent kinases affects cell motility J. Cell Biol. 180 2008 915 929
25. J.A. Baur, and et al. Are sirtuins viable targets for improving healthspan and lifespan? Nat. Rev. Drug Discov. 11 2012 443 461
26. F. Wang, and et al. SIRT2 deacetylates FOXO3a in response to oxidative stress and caloric restriction Aging Cell 6 2007 505 514
27. H.S. Kim, and et al. SIRT2 maintains genome integrity and suppresses tumorigenesis through regulating APC/C activity Cancer Cell 20 2011 487 499
28. M.M. Maxwell, and et al. The Sirtuin 2 microtubule deacetylase is an abundant neuronal protein that accumulates in the aging CNS Hum. Mol. Genet. 20 2011 3986 3996
29. E. Jing, and et al. SIRT2 regulates adipocyte differentiation through FoxO1 acetylation/deacetylation Cell Metab. 6 2007 105 114
30. F. Wang, and Q. Tong SIRT2 suppresses adipocyte differentiation by deacetylating FOXO1 and enhancing FOXO1's repressive interaction with PPARγ Mol. Biol. Cell 20 2009 801 808
31. A.B. Crujeiras, and et al. Sirtuin gene expression in human mononuclear cells is modulated by caloric restriction Eur. J. Clin. Invest. 38 2008 672 678
32. + system Genes Dev. 26 2012 259 270
33. +-dependent tubulin deacetylase Mol. Cell 11 2003 437 444
34. R.M. de Oliveira, and et al. SIRT2 as a therapeutic target for age-related disorders Front. Pharmacol. 3 2012 82
35. T. Inoue, and et al. SIRT2, a tubulin deacetylase, acts to block the entry to chromosome condensation in response to mitotic stress Oncogene 26 2007 945 957
36. A. Vaquero, and et al. Human SirT1 interacts with histone H1 and promotes formation of facultative heterochromatin Mol. Cell 16 2004 93 105
37. B.J. North, and E. Verdin Interphase nucleo-cytoplasmic shuttling and localization of SIRT2 during mitosis PLoS ONE 2 2007 e784
38. B.J. North, and et al. SIRT2 induces the checkpoint kinase BubR1 to increase lifespan EMBO J. 33 2014 1438 1453
39. S.C. Dryden, and et al. Role for human SIRT2 NAD-dependent deacetylase activity in control of mitotic exit in the cell cycle Mol. Cell. Biol. 23 2003 3173 3185
40. S. Lain, and et al. Discovery, in vivo activity, and mechanism of action of a small-molecule p53 activator Cancer Cell 13 2008 454 463
41. J. Chen, and et al. SIRT2 overexpression in hepatocellular carcinoma mediates epithelial to mesenchymal transition by protein kinase B/glycogen synthase kinase-3β/β-catenin signaling Hepatology 57 2013 2287 2298
42. T.F. Outeiro, and et al. Sirtuin 2 inhibitors rescue α-synuclein-mediated toxicity in models of Parkinson's disease Science 317 2007 516 519
43. R. Luthi-Carter, and et al. SIRT2 inhibition achieves neuroprotection by decreasing sterol biosynthesis Proc. Natl. Acad. Sci. U.S.A. 107 2010 7927 7932
44. G. Donmez, and T.F. Outeiro SIRT1 and SIRT2: emerging targets in neurodegeneration EMBO Mol. Med. 5 2013 344 352
45. X. Chen, and et al. The sirtuin-2 inhibitor AK7 is neuroprotective in models of Parkinson's disease but not amyotrophic lateral sclerosis and cerebral ischemia PLoS ONE 10 2015 e0116919
46. V. Chopra, and et al. The sirtuin 2 inhibitor AK-7 is neuroprotective in Huntington's disease mouse models Cell Rep. 2 2012 1492 1497
47. A. Bobrowska, and et al. SIRT2 ablation has no effect on tubulin acetylation in brain, cholesterol biosynthesis or the progression of Huntington's disease phenotypes in vivo PLoS ONE 7 2012 e34805
48. E.E. Kershaw, and J.S. Flier Adipose tissue as an endocrine organ J. Clin. Endocrinol. Metab. 89 2004 2548 2556
49. R.H. Unger, and et al. Lipid homeostasis, lipotoxicity and the metabolic syndrome Biochim. Biophys. Acta 1801 2010 209 214
50. J. Nakae, and et al. The forkhead transcription factor Foxo1 regulates adipocyte differentiation Dev. Cell 4 2003 119 129
51. F. Picard, and et al. Sirt1 promotes fat mobilization in white adipocytes by repressing PPAR-γ Nature 429 2004 771 776
52. R. Mayoral, and et al. Adipocyte SIRT1 knockout promotes PPARγ activity, adipogenesis and insulin sensitivity in chronic-HFD and obesity Mol. Metab. 4 2015 378 391
53. M.S. Strable, and J.M. Ntambi Genetic control of de novo lipogenesis: role in diet-induced obesity Crit. Rev. Biochem. Mol. Biol. 45 2010 199 214
54. P.A. Srere The citrate cleavage enzyme. I. Distribution and purification J. Biol. Chem. 234 1959 2544 2547
55. K.E. Wellen, and et al. ATP-citrate lyase links cellular metabolism to histone acetylation Science 324 2009 1076 1080
56. R. Lin, and et al. Acetylation stabilizes ATP-citrate lyase to promote lipid biosynthesis and tumor growth Mol. Cell 51 2013 506 518
57. Q. Wang, and et al. Abrogation of hepatic ATP-citrate lyase protects against fatty liver and ameliorates hyperglycemia in leptin receptor-deficient mice Hepatology 49 2009 1166 1175
58. D.M. Taylor, and et al. A brain-permeable small molecule reduces neuronal cholesterol by inhibiting activity of sirtuin 2 deacetylase ACS Chem. Biol. 6 2011 540 546
59. R.B. Vega, and et al. The coactivator PGC-1 cooperates with peroxisome proliferator-activated receptor α in transcriptional control of nuclear genes encoding mitochondrial fatty acid oxidation enzymes Mol. Cell. Biol. 20 2000 1868 1876
60. Z. Wu, and et al. Mechanisms controlling mitochondrial biogenesis and respiration through the thermogenic coactivator PGC-1 Cell 98 1999 115 124
61. C. Bouche, and et al. The cellular fate of glucose and its relevance in type 2 diabetes Endocr. Rev. 25 2004 807 830
62. S.H. Koo, and et al. The CREB coactivator TORC2 is a key regulator of fasting glucose metabolism Nature 437 2005 1109 1111
63. P. Puigserver, and et al. Insulin-regulated hepatic gluconeogenesis through FOXO1-PGC-1α interaction Nature 423 2003 550 555
64. S. Zhao, and et al. Regulation of cellular metabolism by protein lysine acetylation Science 327 2010 1000 1004
65. W. Jiang, and et al. Acetylation regulates gluconeogenesis by promoting PEPCK1 degradation via recruiting the UBR5 ubiquitin ligase Mol. Cell 43 2011 33 44
66. A.R. Saltiel, and C.R. Kahn Insulin signalling and the regulation of glucose and lipid metabolism Nature 414 2001 799 806
67. B.J. Goldstein Insulin resistance as the core defect in type 2 diabetes mellitus Am. J. Cardiol. 90 2002 3G 10G
68. C.M. Taniguchi, and et al. Critical nodes in signalling pathways: insights into insulin action Nat. Rev. Mol. Cell Biol. 7 2006 85 96
69. B.D. Manning, and L.C. Cantley AKT/PKB signaling: navigating downstream Cell 129 2007 1261 1274
70. M.C. Motta, and et al. Mammalian SIRT1 represses forkhead transcription factors Cell 116 2004 551 563
71. G. Ramakrishnan, and et al. Sirt2 deacetylase is a novel AKT binding partner critical for AKT activation by insulin J. Biol. Chem. 289 2014 6054 6066
72. A. Arora, and C.S. Dey SIRT2 negatively regulates insulin resistance in C2C12 skeletal muscle cells Biochim. Biophys. Acta 1842 2014 1372 1378
73. J.S. Bogan, and et al. Functional cloning of TUG as a regulator of GLUT4 glucose transporter trafficking Nature 425 2003 727 733
74. J.P. Belman, and et al. Acetylation of TUG protein promotes the accumulation of GLUT4 glucose transporters in an insulin-responsive intracellular compartment J. Biol. Chem. 290 2015 4447 4463
75. Y. Xu, and et al. Dual-mode of insulin action controls GLUT4 vesicle exocytosis J. Cell Biol. 193 2011 643 653
76. O. Osborn, and J.M. Olefsky The cellular and signaling networks linking the immune system and metabolism in disease Nat. Med. 18 2012 363 374
77. K.E. Wellen, and G.S. Hotamisligil Inflammation, stress, and diabetes J. Clin. Invest. 115 2005 1111 1119
78. C.N. Lumeng, and A.R. Saltiel Inflammatory links between obesity and metabolic disease J. Clin. Invest. 121 2011 2111 2117
79. X. Zhang, and et al. Hypothalamic IKKβ/NF-κB and ER stress link overnutrition to energy imbalance and obesity Cell 135 2008 61 73
80. K.M. Rothgiesser, and et al. SIRT2 regulates NF-κB dependent gene expression through deacetylation of p65 Lys310 J. Cell Sci. 123 2010 4251 4258
81. T.F. Pais, and et al. The NAD-dependent deacetylase sirtuin 2 is a suppressor of microglial activation and brain inflammation EMBO J. 32 2013 2603 2616
82. G. Lo Sasso, and et al. SIRT2 deficiency modulates macrophage polarization and susceptibility to experimental colitis PLoS ONE 9 2014 e103573
83. J. Lin, and et al. Sirt2 suppresses inflammatory responses in collagen-induced arthritis Biochem. Biophys. Res. Commun. 441 2013 897 903
84. M.J. Kim, and et al. PEP-1-SIRT2 inhibits inflammatory response and oxidative stress-induced cell death via expression of antioxidant enzymes in murine macrophages Free Radic. Biol. Med. 63 2013 432 445
85. M. Frisard, and E. Ravussin Energy metabolism and oxidative stress: impact on the metabolic syndrome and the aging process Endocrine 29 2006 27 32
86. B.R. Webster, and et al. The role of sirtuins in modulating redox stressors Free Radic. Biol. Med. 52 2012 281 290
87. Y. Zhao, and et al. Cytosolic FoxO1 is essential for the induction of autophagy and tumour suppressor activity Nat. Cell Biol. 12 2010 665 675
88. N. Hariharan, and et al. Deacetylation of FoxO by Sirt1 plays an essential role in mediating starvation-induced autophagy in cardiac myocytes Circ. Res. 107 2010 1470 1482
89. T. Inoue, and et al. SIRT2 knockdown increases basal autophagy and prevents postslippage death by abnormally prolonging the mitotic arrest that is induced by microtubule inhibitors FEBS J. 281 2014 2623 2637
90. J. Gal, and et al. SIRT2 interferes with autophagy-mediated degradation of protein aggregates in neuronal cells under proteasome inhibition Neurochem. Int. 61 2012 992 1000
91. J.D. Rabinowitz, and E. White Autophagy and metabolism Science 330 2010 1344 1348
92. B. Levine, and G. Kroemer Autophagy in the pathogenesis of disease Cell 132 2008 27 42
93. Y.P. Wang, and et al. Regulation of G6PD acetylation by SIRT2 and KAT9 modulates NADPH homeostasis and cell survival during oxidative stress EMBO J. 33 2014 1304 1320
94. Y. Xu, and et al. Oxidative stress activates SIRT2 to deacetylate and stimulate phosphoglycerate mutase Cancer Res. 74 2014 3630 3642
95. M.J. Morgan, and Z.G. Liu Crosstalk of reactive oxygen species and NF-κB signaling Cell Res. 21 2011 103 115
96. L. Guarente Sirtuins as potential targets for metabolic syndrome Nature 444 2006 868 874
97. + precursor nicotinamide riboside enhances oxidative metabolism and protects against high-fat diet-induced obesity Cell Metab. 15 2012 838 847
98. + intermediate, treats the pathophysiology of diet- and age-induced diabetes in mice Cell Metab. 14 2011 528 536
99. + dependence in sirtuin-catalyzed deacylation Biochemistry 54 2015 3037 3050
100. M. Pacholec, and et al. SRT1720, SRT2183, SRT1460, and resveratrol are not direct activators of SIRT1 J. Biol. Chem. 285 2010 8340 8351
101. R.R. Alcendor, and et al. Sirt1 regulates aging and resistance to oxidative stress in the heart Circ. Res. 100 2007 1512 1521
102. P.T. Pfluger, and et al. Sirt1 protects against high-fat diet-induced metabolic damage Proc. Natl. Acad. Sci. U.S.A. 105 2008 9793 9798