SIRT3 functions in the nucleus in the control of stress-related gene expression

Molecular and Cellular Biology

Volumn 32, Issue 24, 2012, Pages 5022-5034

  Iwahara, Toshinori ^a   Bonasio, Roberto ^a   Narendra, Varun ^a   Reinberg, Danny ^a  

^a NEW YORK UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

HISTONE DEACETYLASE; SIRTUIN 3;

ARTICLE; CELL STRESS; GENE EXPRESSION; GENE TARGETING; HUMAN; HUMAN CELL; IMMUNOPRECIPITATION; MITOCHONDRION; OXIDATIVE STRESS; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN FUNCTION; ULTRAVIOLET RADIATION;

BASE SEQUENCE; CELL LINE; CELL NUCLEUS; GENE EXPRESSION REGULATION; HEK293 CELLS; HELA CELLS; HUMANS; MITOCHONDRIA; MUTAGENESIS, SITE-DIRECTED; OXIDATIVE STRESS; RECOMBINANT PROTEINS; RNA, SMALL INTERFERING; S-PHASE KINASE-ASSOCIATED PROTEINS; SEQUENCE DELETION; SIRTUIN 3; STRESS, PHYSIOLOGICAL; UBIQUITIN-PROTEIN LIGASES; ULTRAVIOLET RAYS;

EID: 84871852995     PISSN: 02707306     EISSN: 10985549     Source Type: Journal    
DOI: 10.1128/MCB.00822-12     Document Type: Article

References (53)

1. Allison SJ, Milner J. 2007. SIRT3 is pro-apoptotic and participates in distinct basal apoptotic pathways. Cell Cycle 6:2669 -2677.
2. Asp P, et al. 2011. Genome-wide remodeling of the epigenetic landscape during myogenic differentiation. Proc. Natl. Acad. Sci. U. S. A. 108:E149-E158.
3. Bao J, et al. 2010. Characterization of the murine SIRT3 mitochondrial localization sequence and comparison of mitochondrial enrichment and deacetylase activity of long and short SIRT3 isoforms. J. Cell Biochem.110:238 -247.
4. Bellizzi D, et al. 2005. A novel VNTR enhancer within the SIRT3 gene, a human homologue of SIR2, is associated with survival at oldest ages. Genomics 85:258 -263.
5. Brunet A, et al. 2004. Stress-dependent regulation of FOXO transcription factors by the SIRT1 deacetylase. Science 303:2011-2015.
6. Chen Y, et al. 2011. Tumour suppressor SIRT3 deacetylates and activates manganese superoxide dismutase to scavenge ROS. EMBO Rep. 12:534-541.
7. Cohen HY, et al. 2004. Acetylation of the C terminus of Ku70 by CBP and PCAF controls Bax-mediated apoptosis. Mol. Cell 13:627- 638.
8. Cohen HY, et al. 2004. Calorie restriction promotes mammalian cell survival by inducing the SIRT1 deacetylase. Science 305:390 -392.
9. Cooper HM, Spelbrink JN. 2008. The human SIRT3 protein deacetylase is exclusively mitochondrial. Biochem. J. 411:279 -285.
10. Doi K, et al. 2011. ZFAT is a critical molecule for cell survival in mouse embryonic fibroblasts. Cell. Mol. Biol. Lett. 16:89 -100.
11. Finley LW, et al. 2011. SIRT3 opposes reprogramming of cancer cell metabolism through HIF1alpha destabilization. Cancer Cell 19:416-428.
12. Frescas D, Pagano M. 2008. Deregulated proteolysis by the F-box proteins SKP2 and beta-TrCP: tipping the scales of cancer. Nat. Rev. Cancer 8:438-449.
13. Frye RA. 1999. Characterization of five human cDNAs with homology to the yeast SIR2 gene: Sir2-like proteins (sirtuins) metabolizeNADand may have protein ADP-ribosyltransferase activity. Biochem. Biophys. Res.Commun. 260:273-279.
14. Fujimoto T, et al. 2009. ZFAT is an antiapoptotic molecule and critical for cell survival in MOLT-4 cells. FEBS Lett. 583:568 -572.
15. Gao Z, et al. 2012. PCGF homologs, CBX proteins, and RYBP define functionally distinct PRC1 family complexes. Mol. Cell 45:344 -356.
16. Guarente L, Picard F. 2005. Calorie restriction-the SIR2 connection. Cell 120:473- 482.
17. Gurd BJ, Holloway GP, Yoshida Y, Bonen A. 2012. In mammalian muscle, SIRT3 is present in mitochondria and not in the nucleus; and SIRT3 is upregulated by chronic muscle contraction in an adenosine monophosphate-activated protein kinase-independent manner. Metabolism. 61:733-741.
18. Hallows WC, Lee S, Denu JM. 2006. Sirtuins deacetylate and activate mammalian acetyl-CoA synthetases. Proc. Natl. Acad. Sci. U. S. A. 103: 10230-10235.
19. Hallows WC, et al. 2011. Sirt3 promotes the urea cycle and fatty acid oxidation during dietary restriction. Mol. Cell 41:139 -149.
20. Hirschey MD, et al. 2010. SIRT3 regulates mitochondrial fatty-acid oxidation by reversible enzyme deacetylation. Nature 464:121-125.
21. Hoeller D, Hecker CM, Dikic I. 2006. Ubiquitin and ubiquitin-like proteins in cancer pathogenesis. Nat. Rev. Cancer 6:776 -788.
22. Iwahara T, Akagi T, Fujitsuka Y, Hanafusa H. 2004. CrkII regulates focal adhesion kinase activation by making a complex with Crk-associated substrate, p130Cas. Proc. Natl. Acad. Sci. U. S. A. 101:17693-17698.
23. Kim HS, et al. 2010. SIRT3 is a mitochondria-localized tumor suppressor required for maintenance of mitochondrial integrity and metabolism during stress. Cancer Cell 17:41-52.
24. Kitamura YI, et al. 2005. FoxO1 protects against pancreatic beta cell failure through NeuroD and MafA induction. Cell Metab. 2:153-163.
25. Langmead B, Trapnell C, Pop M, Salzberg SL. 2009. Ultrafast and memory-efficient alignment of short DNA sequences to the human genome.Genome Biol. 10:R25.
26. Li H, et al. 2009. The Sequence Alignment/Map format and SAMtools. Bioinformatics 25:2078 -2079.
27. Lombard DB, et al. 2007. Mammalian Sir2 homolog SIRT3 regulates global mitochondrial lysine acetylation. Mol. Cell. Biol. 27:8807- 8814.
28. Marchenko ND, Wolff S, Erster S, Becker K, Moll UM. 2007. Monoubiquitylation promotes mitochondrial p53 translocation. EMBO J. 26:923-934.
29. Margueron R, et al. 2008. Ezh1 and Ezh2 maintain repressive chromatin through different mechanisms. Mol. Cell 32:503-518.
30. McLean CY, et al. 2010. GREAT improves functional interpretation of cis-regulatory regions. Nat. Biotechnol. 28:495-501.
31. Morita S, Kojima T, Kitamura T. 2000. Plat-E: an efficient and stable system for transient packaging of retroviruses. Gene Ther. 7:1063-1066.
32. Motta MC, et al. 2004. Mammalian SIRT1 represses forkhead transcription factors. Cell 116:551-563.
33. Nakamura Y, Ogura M, Tanaka D, Inagaki N. 2008. Localization of mouse mitochondrial SIRT proteins: shift of SIRT3 to nucleus by coexpression with SIRT5. Biochem. Biophys. Res. Commun. 366:174 -179.
34. +-dependent tubulin deacetylase. Mol. Cell 11:437- 444.
35. Oberdoerffer P, et al. 2008. SIRT1 redistribution on chromatin promotes genomic stability but alters gene expression during aging. Cell 135:907-918.
36. Oikawa K, et al. 2004. Expression of a novel human gene, human wings apart-like (hWAPL), is associated with cervical carcinogenesis and tumor progression. Cancer Res. 64:3545-3549.
37. Onyango P, Celic I, McCaffery JM, Boeke JD, Feinberg AP. 2002. SIRT3, a human SIR2 homologue, is an NAD-dependent deacetylase localized to mitochondria. Proc. Natl. Acad. Sci. U. S. A. 99:13653-13658.
38. Pillai VB, et al. 2010. Exogenous NAD blocks cardiac hypertrophic response via activation of the SIRT3-LKB1-AMP-activated kinase pathway. J. Biol. Chem. 285:3133-3144.
39. Qiu X, Brown K, Hirschey MD, Verdin E, Chen D. 2010. Calorie restriction reduces oxidative stress by SIRT3-mediated SOD2 activation. Cell Metab. 12:662- 667.
40. Ramakrishna M, et al. 2010. Identification of candidate growth promoting genes in ovarian cancer through integrated copy number and expression analysis. PLoS One 5:e9983. doi:10.1371/journal.pone.0009983.
41. +- dependent histone deacetylase that translocates to the mitochondria upon cellular stress. Genes Dev. 21:920 -928.
42. Schwer B, Bunkenborg J, Verdin RO, Andersen JS, Verdin E. 2006. Reversible lysine acetylation controls the activity of the mitochondrial enzyme acetyl-CoA synthetase 2. Proc. Natl. Acad. Sci. U. S. A. 103: 10224-10229.
43. Schwer B, North BJ, Frye RA, Ott M, Verdin E. 2002. The human silent information regulator (Sir)2 homologue hSIRT3 is a mitochondrial nicotinamide adenine dinucleotide-dependent deacetylase. J. Cell Biol. 158:647-657.
44. Shi T, Wang F, Stieren E, Tong Q. 2005. SIRT3, a mitochondrial sirtuin deacetylase, regulates mitochondrial function and thermogenesis in brown adipocytes. J. Biol. Chem. 280:13560 -13567.
45. Sundaresan NR, et al. 2009. Sirt3 blocks the cardiac hypertrophic response by augmenting Foxo3a-dependent antioxidant defense mechanisms in mice. J. Clin. Invest. 119:2758 -2771.
46. Sundaresan NR, Samant SA, Pillai VB, Rajamohan SB, Gupta MP. 2008. SIRT3 is a stress-responsive deacetylase in cardiomyocytes that protects cells from stress-mediated cell death by deacetylation of Ku70. Mol. Cell. Biol. 28:6384-6401.
47. Vaquero A, Reinberg D. 2009. Calorie restriction and the exercise of chromatin. Genes Dev. 23:1849 -1869.
48. Vaquero A, et al. 2004. Human SirT1 interacts with histone H1 and promotes formation of facultative heterochromatin. Mol. Cell 16:93-105.
49. Vaquero A, et al. 2006. SirT2 is a histone deacetylase with preference for histone H4 Lys 16 during mitosis. Genes Dev. 20:1256 -1261.
50. +-dependent deacetylation of H4 lysine 16 by class III HDACs. Oncogene 26:5505-5520.
51. Yang Y, et al. 2007. Inhibitors of ubiquitin-activating enzyme (E1), a new class of potential cancer therapeutics. Cancer Res. 67:9472-9481.
52. Yih LH, Peck K, Lee TC. 2002. Changes in gene expression profiles of human fibroblasts in response to sodium arsenite treatment. Carcinogenesis 23:867- 876.
53. Zhang YY, Zhou LM. 2012. Sirt3 inhibits hepatocellular carcinoma cell growth through reducing Mdm2-mediated p53 degradation. Biochem. Biophys. Res. Commun. 423:26 -31.