SIRT1-dependent regulation of chromatin and transcription: Linking NAD+ metabolism and signaling to the control of cellular functions

Biochimica et Biophysica Acta - Proteins and Proteomics

Volumn 1804, Issue 8, 2010, Pages 1666-1675

  Zhang, Tong ^a   Kraus, W Lee ^a,b  

^a Department of Obstetrics Gynecology   (United States)

^b WEILL CORNELL MEDICAL COLLEGE   (United States)

Author keywords

Chromatin; Deacetylation; Metabolism; NAD+; SIRT1; Transcription

Indexed keywords

HISTONE; NICOTINAMIDE ADENINE DINUCLEOTIDE; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE; NICOTINAMIDE NUCLEOTIDE ADENYLYLTRANSFERASE; NICOTINAMIDE PHOSPHORIBOSYLTRANSFERASE; PEROXISOME PROLIFERATOR ACTIVATED RECEPTOR GAMMA COACTIVATOR 1ALPHA; PROTEIN BMAL1; SIRTUIN 1; SIRTUIN 2; TRANSCRIPTION FACTOR CLOCK;

CELL AGING; CELL FUNCTION; CELL METABOLISM; CELLULAR STRESS RESPONSE; CHROMATIN STRUCTURE; CIRCADIAN RHYTHM; DEACETYLATION; DNA METHYLATION; ENERGY METABOLISM; ENZYME REGULATION; ENZYME SYNTHESIS; FATTY ACID OXIDATION; GENE EXPRESSION REGULATION; GENE INTERACTION; GLUCONEOGENESIS; METABOLIC REGULATION; MITOCHONDRIAL RESPIRATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN DNA INTERACTION; PROTEIN MODIFICATION; REVIEW; SIGNAL TRANSDUCTION; TRANSCRIPTION REGULATION;

ANIMALS; CHROMATIN; DNA METHYLATION; HISTONES; HUMANS; MODELS, BIOLOGICAL; NAD; NICOTINAMIDE PHOSPHORIBOSYLTRANSFERASE; NICOTINAMIDE-NUCLEOTIDE ADENYLYLTRANSFERASE; POLY(ADP-RIBOSE) POLYMERASES; SIGNAL TRANSDUCTION; SIRTUIN 1; SUBSTRATE SPECIFICITY; TRANSCRIPTION FACTORS; TRANSCRIPTION, GENETIC; TRANSCRIPTIONAL ACTIVATION;

MAMMALIA;

EID: 77953290752     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2009.10.022     Document Type: Review

References (150)

1. Naar A.M., Lemon B.D., and Tjian R. Transcriptional coactivator complexes. Annu. Rev. Biochem. 70 (2001) 475-501
2. Narlikar G.J., Fan H.Y., and Kingston R.E. Cooperation between complexes that regulate chromatin structure and transcription. Cell 108 (2002) 475-487
3. Reinberg D., Orphanides G., Ebright R., Akoulitchev S., Carcamo J., Cho H., Cortes P., Drapkin R., Flores O., Ha I., Inostroza J.A., Kim S., Kim T.K., Kumar P., Lagrange T., LeRoy G., Lu H., Ma D.M., Maldonado E., Merino A., Mermelstein F., Olave I., Sheldon M., Shiekhattar R., Zawel L., et al. The RNA polymerase II general transcription factors: past, present, and future. Cold Spring Harb. Symp. Quant. Biol. 63 (1998) 83-103
4. Blander G., and Guarente L. The Sir2 family of protein deacetylases. Annu. Rev. Biochem. 73 (2004) 417-435
5. Sauve A.A., Wolberger C., Schramm V.L., and Boeke J.D. The biochemistry of sirtuins. Annu. Rev. Biochem. 75 (2006) 435-465
6. Feige J.N., and Auwerx J. Transcriptional targets of sirtuins in the coordination of mammalian physiology. Curr. Opin. Cell Biol. 20 (2008) 303-309
7. Gasser S.M., and Cockell M.M. The molecular biology of the SIR proteins. Gene 279 (2001) 1-16
8. Anastasiou D., and Krek W. SIRT1: linking adaptive cellular responses to aging-associated changes in organismal physiology. Physiology (Bethesda) 21 (2006) 404-410
9. Wojcik M., Mac-Marcjanek K., and Wozniak L.A. Physiological and pathophysiological functions of SIRT1. Mini Rev. Med. Chem. 9 (2009) 386-394
10. Kwon H.S., and Ott M. The ups and downs of SIRT1. Trends Biochem. Sci. 33 (2008) 517-525
11. Vaquero A., Scher M., Lee D., Erdjument-Bromage H., Tempst P., and Reinberg D. Human SirT1 interacts with histone H1 and promotes formation of facultative heterochromatin. Mol. Cell 16 (2004) 93-105
12. Imai S., Armstrong C.M., Kaeberlein M., and Guarente L. Transcriptional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase. Nature 403 (2000) 795-800
13. Liou G.G., Tanny J.C., Kruger R.G., Walz T., and Moazed D. Assembly of the SIR complex and its regulation by O-acetyl-ADP-ribose, a product of NAD-dependent histone deacetylation. Cell 121 (2005) 515-527
14. Kraus W.L. New functions for an ancient domain. Nat. Struct. Mol. Biol. 16 (2009) 904-907
15. Kustatscher G., Hothorn M., Pugieux C., Scheffzek K., and Ladurner A.G. Splicing regulates NAD metabolite binding to histone macroH2A. Nat. Struct. Mol. Biol. 12 (2005) 624-625
16. McLennan A.G. The Nudix hydrolase superfamily. Cell. Mol. Life Sci. 63 (2006) 123-143
17. Lee S., Tong L., and Denu J.M. Quantification of endogenous sirtuin metabolite O-acetyl-ADP-ribose. Anal. Biochem. 383 (2008) 174-179
18. Rafty L.A., Schmidt M.T., Perraud A.L., Scharenberg A.M., and Denu J.M. Analysis of O-acetyl-ADP-ribose as a target for Nudix ADP-ribose hydrolases. J. Biol. Chem. 277 (2002) 47114-47122
19. Tong L., Lee S., and Denu J.M. Hydrolase regulates NAD+ metabolites and modulates cellular redox. J. Biol. Chem. 284 (2009) 11256-11266
20. Smeal T., Claus J., Kennedy B., Cole F., and Guarente L. Loss of transcriptional silencing causes sterility in old mother cells of S. cerevisiae. Cell 84 (1996) 633-642
21. Kennedy B.K., Gotta M., Sinclair D.A., Mills K., McNabb D.S., Murthy M., Pak S.M., Laroche T., Gasser S.M., and Guarente L. Redistribution of silencing proteins from telomeres to the nucleolus is associated with extension of life span in S. cerevisiae. Cell 89 (1997) 381-391
22. Sinclair D.A., and Guarente L. Extrachromosomal rDNA circles-a cause of aging in yeast. Cell 91 (1997) 1033-1042
23. Mills K.D., Sinclair D.A., and Guarente L. MEC1-dependent redistribution of the Sir3 silencing protein from telomeres to DNA double-strand breaks. Cell 97 (1999) 609-620
24. McAinsh A.D., Scott-Drew S., Murray J.A., and Jackson S.P. DNA damage triggers disruption of telomeric silencing and Mec1p-dependent relocation of Sir3p. Curr. Biol. 9 (1999) 963-966
25. Martin S.G., Laroche T., Suka N., Grunstein M., and Gasser S.M. Relocalization of telomeric Ku and SIR proteins in response to DNA strand breaks in yeast. Cell 97 (1999) 621-633
26. Oberdoerffer P., Michan S., McVay M., Mostoslavsky R., Vann J., Park S.K., Hartlerode A., Stegmuller J., Hafner A., Loerch P., Wright S.M., Mills K.D., Bonni A., Yankner B.A., Scully R., Prolla T.A., Alt F.W., and Sinclair D.A. SIRT1 redistribution on chromatin promotes genomic stability but alters gene expression during aging. Cell 135 (2008) 907-918
27. Dang W., Steffen K.K., Perry R., Dorsey J.A., Johnson F.B., Shilatifard A., Kaeberlein M., Kennedy B.K., and Berger S.L. Histone H4 lysine 16 acetylation regulates cellular lifespan. Nature 459 (2009) 802-807
28. Bouras T., Fu M., Sauve A.A., Wang F., Quong A.A., Perkins N.D., Hay R.T., Gu W., and Pestell R.G. SIRT1 deacetylation and repression of p300 involves lysine residues 1020/1024 within the cell cycle regulatory domain 1. J. Biol. Chem. 280 (2005) 10264-10276
29. Wang Z., Schones D.E., and Zhao K. Characterization of human epigenomes. Curr. Opin. Genet. Dev. 19 (2009) 127-134
30. Vaquero A., Scher M., Erdjument-Bromage H., Tempst P., Serrano L., and Reinberg D. SIRT1 regulates the histone methyl-transferase SUV39H1 during heterochromatin formation. Nature 450 (2007) 440-444
31. Murayama A., Ohmori K., Fujimura A., Minami H., Yasuzawa-Tanaka K., Kuroda T., Oie S., Daitoku H., Okuwaki M., Nagata K., Fukamizu A., Kimura K., Shimizu T., and Yanagisawa J. Epigenetic control of rDNA loci in response to intracellular energy status. Cell 133 (2008) 627-639
32. Kim J.E., Chen J., and Lou Z. DBC1 is a negative regulator of SIRT1. Nature 451 (2008) 583-586
33. Zhao W., Kruse J.P., Tang Y., Jung S.Y., Qin J., and Gu W. Negative regulation of the deacetylase SIRT1 by DBC1. Nature 451 (2008) 587-590
34. Li Z., Chen L., Kabra N., Wang C., Fang J., and Chen J. Inhibition of SUV39H1 methyltransferase activity by DBC1. J. Biol. Chem. 284 (2009) 10361-10366
35. Kuzmichev A., Margueron R., Vaquero A., Preissner T.S., Scher M., Kirmizis A., Ouyang X., Brockdorff N., Abate-Shen C., Farnham P., and Reinberg D. Composition and histone substrates of polycomb repressive group complexes change during cellular differentiation. Proc. Natl. Acad. Sci. U. S. A. 102 (2005) 1859-1864
36. Siuti N., and Kelleher N.L. Decoding protein modifications using top-down mass spectrometry. Nat. Methods 4 (2007) 817-821
37. Siuti N., and Kelleher N.L. Efficient readout of posttranslational codes on the 50-residue tail of histone H3 by high-resolution MS/MS. Anal. Biochem. 396 (2010) 180-187
38. Han X., Aslanian A., and Yates III J.R. Mass spectrometry for proteomics. Curr. Opin. Chem. Biol. 12 (2008) 483-490
39. Taverna S.D., Ueberheide B.M., Liu Y., Tackett A.J., Diaz R.L., Shabanowitz J., Chait B.T., Hunt D.F., and Allis C.D. Long-distance combinatorial linkage between methylation and acetylation on histone H3 N termini. Proc. Natl. Acad. Sci. U. S. A. 104 (2007) 2086-2091
40. Pruitt K., Zinn R.L., Ohm J.E., McGarvey K.M., Kang S.H., Watkins D.N., Herman J.G., and Baylin S.B. Inhibition of SIRT1 reactivates silenced cancer genes without loss of promoter DNA hypermethylation. PLoS Genet. 2 (2006) e40
41. O'Hagan H.M., Mohammad H.P., and Baylin S.B. Double strand breaks can initiate gene silencing and SIRT1-dependent onset of DNA methylation in an exogenous promoter CpG island. PLoS Genet. 4 (2008) e1000155
42. Vaziri H., Dessain S.K., Ng Eaton E., Imai S.I., Frye R.A., Pandita T.K., Guarente L., and Weinberg R.A. hSIR2(SIRT1) functions as an NAD-dependent p53 deacetylase. Cell 107 (2001) 149-159
43. Luo J., Nikolaev A.Y., Imai S., Chen D., Su F., Shiloh A., Guarente L., and Gu W. Negative control of p53 by Sir2alpha promotes cell survival under stress. Cell 107 (2001) 137-148
44. Brunet A., Sweeney L.B., Sturgill J.F., Chua K.F., Greer P.L., Lin Y., Tran H., Ross S.E., Mostoslavsky R., Cohen H.Y., Hu L.S., Cheng H.L., Jedrychowski M.P., Gygi S.P., Sinclair D.A., Alt F.W., and Greenberg M.E. Stress-dependent regulation of FOXO transcription factors by the SIRT1 deacetylase. Science 303 (2004) 2011-2015
45. Motta M.C., Divecha N., Lemieux M., Kamel C., Chen D., Gu W., Bultsma Y., McBurney M., and Guarente L. Mammalian SIRT1 represses forkhead transcription factors. Cell 116 (2004) 551-563
46. Nakahata Y., Kaluzova M., Grimaldi B., Sahar S., Hirayama J., Chen D., Guarente L.P., and Sassone-Corsi P. The NAD+-dependent deacetylase SIRT1 modulates CLOCK-mediated chromatin remodeling and circadian control. Cell 134 (2008) 329-340
47. Kim M.Y., Woo E.M., Chong Y.T., Homenko D.R., and Kraus W.L. Acetylation of estrogen receptor alpha by p300 at lysines 266 and 268 enhances the deoxyribonucleic acid binding and transactivation activities of the receptor. Mol. Endocrinol. 20 (2006) 1479-1493
48. Dai Y., Ngo D., Forman L.W., Qin D.C., Jacob J., and Faller D.V. Sirtuin 1 is required for antagonist-induced transcriptional repression of androgen-responsive genes by the androgen receptor. Mol. Endocrinol. 21 (2007) 1807-1821
49. Fu M., Liu M., Sauve A.A., Jiao X., Zhang X., Wu X., Powell M.J., Yang T., Gu W., Avantaggiati M.L., Pattabiraman N., Pestell T.G., Wang F., Quong A.A., Wang C., and Pestell R.G. Hormonal control of androgen receptor function through SIRT1. Mol. Cell. Biol. 26 (2006) 8122-8135
50. Li X., Zhang S., Blander G., Tse J.G., Krieger M., and Guarente L. SIRT1 deacetylates and positively regulates the nuclear receptor LXR. Mol. Cell 28 (2007) 91-106
51. Dioum E.M., Chen R., Alexander M.S., Zhang Q., Hogg R.T., Gerard R.D., and Garcia J.A. Regulation of hypoxia-inducible factor 2alpha signaling by the stress-responsive deacetylase sirtuin 1. Science 324 (2009) 1289-1293
52. Rodgers J.T., and Puigserver P. Fasting-dependent glucose and lipid metabolic response through hepatic sirtuin 1. Proc. Natl. Acad. Sci. U. S. A. 104 (2007) 12861-12866
53. Baur J.A., Pearson K.J., Price N.L., Jamieson H.A., Lerin C., Kalra A., Prabhu V.V., Allard J.S., Lopez-Lluch G., Lewis K., Pistell P.J., Poosala S., Becker K.G., Boss O., Gwinn D., Wang M., Ramaswamy S., Fishbein K.W., Spencer R.G., Lakatta E.G., Le Couteur D., Shaw R.J., Navas P., Puigserver P., Ingram D.K., de Cabo R., and Sinclair D.A. Resveratrol improves health and survival of mice on a high-calorie diet. Nature 444 (2006) 337-342
54. Lagouge M., Argmann C., Gerhart-Hines Z., Meziane H., Lerin C., Daussin F., Messadeq N., Milne J., Lambert P., Elliott P., Geny B., Laakso M., Puigserver P., and Auwerx J. Resveratrol improves mitochondrial function and protects against metabolic disease by activating SIRT1 and PGC-1alpha. Cell 127 (2006) 1109-1122
55. Gerhart-Hines Z., Rodgers J.T., Bare O., Lerin C., Kim S.H., Mostoslavsky R., Alt F.W., Wu Z., and Puigserver P. Metabolic control of muscle mitochondrial function and fatty acid oxidation through SIRT1/PGC-1alpha. EMBO J. 26 (2007) 1913-1923
56. Rodgers J.T., Lerin C., Haas W., Gygi S.P., Spiegelman B.M., and Puigserver P. Nutrient control of glucose homeostasis through a complex of PGC-1alpha and SIRT1. Nature 434 (2005) 113-118
57. Rodgers J.T., Lerin C., Gerhart-Hines Z., and Puigserver P. Metabolic adaptations through the PGC-1 alpha and SIRT1 pathways. FEBS Lett. 582 (2008) 46-53
58. Cohen H.Y., Miller C., Bitterman K.J., Wall N.R., Hekking B., Kessler B., Howitz K.T., Gorospe M., de Cabo R., and Sinclair D.A. Calorie restriction promotes mammalian cell survival by inducing the SIRT1 deacetylase. Science 305 (2004) 390-392
59. Tang B.L., and Chua C.E. SIRT1 and neuronal diseases. Mol. Aspects Med. 29 (2008) 187-200
60. Michan S., and Sinclair D. Sirtuins in mammals: insights into their biological function. Biochem. J. 404 (2007) 1-13
61. Giannakou M.E., and Partridge L. The interaction between FOXO and SIRT1: tipping the balance towards survival. Trends Cell. Biol. 14 (2004) 408-412
62. Grimaldi B., Nakahata Y., Kaluzova M., Masubuchi S., and Sassone-Corsi P. Chromatin remodeling, metabolism and circadian clocks: the interplay of CLOCK and SIRT1. Int. J. Biochem. Cell Biol. 41 (2009) 81-86
63. Handschin C., and Spiegelman B.M. Peroxisome proliferator-activated receptor gamma coactivator 1 coactivators, energy homeostasis, and metabolism. Endocr. Rev. 27 (2006) 728-735
64. Canto C., and Auwerx J. PGC-1alpha, SIRT1 and AMPK, an energy sensing network that controls energy expenditure. Curr. Opin. Lipidol. 20 (2009) 98-105
65. Puigserver P., Rhee J., Donovan J., Walkey C.J., Yoon J.C., Oriente F., Kitamura Y., Altomonte J., Dong H., Accili D., and Spiegelman B.M. Insulin-regulated hepatic gluconeogenesis through FOXO1-PGC-1alpha interaction. Nature 423 (2003) 550-555
66. Michael L.F., Wu Z., Cheatham R.B., Puigserver P., Adelmant G., Lehman J.J., Kelly D.P., and Spiegelman B.M. Restoration of insulin-sensitive glucose transporter (GLUT4) gene expression in muscle cells by the transcriptional coactivator PGC-1. Proc. Natl. Acad. Sci. U. S. A. 98 (2001) 3820-3825
67. Schreiber S.N., Knutti D., Brogli K., Uhlmann T., and Kralli A. The transcriptional coactivator PGC-1 regulates the expression and activity of the orphan nuclear receptor estrogen-related receptor alpha (ERRalpha). J. Biol. Chem. 278 (2003) 9013-9018
68. Huss J.M., Kopp R.P., and Kelly D.P. Peroxisome proliferator-activated receptor coactivator-1alpha (PGC-1alpha) coactivates the cardiac-enriched nuclear receptors estrogen-related receptor-alpha and -gamma. Identification. of. novel. leucine-rich. interaction. motif. within. PGC-1alpha. J. Biol. Chem. 277 (2002) 40265-40274
69. Wang Y.X., Lee C.H., Tiep S., Yu R.T., Ham J., Kang H., and Evans R.M. Peroxisome-proliferator-activated receptor delta activates fat metabolism to prevent obesity. Cell 113 (2003) 159-170
70. Vega R.B., Huss J.M., and Kelly D.P. The coactivator PGC-1 cooperates with peroxisome proliferator-activated receptor alpha in transcriptional control of nuclear genes encoding mitochondrial fatty acid oxidation enzymes. Mol. Cell. Biol. 20 (2000) 1868-1876
71. Puigserver P., Wu Z., Park C.W., Graves R., Wright M., and Spiegelman B.M. A cold-inducible coactivator of nuclear receptors linked to adaptive thermogenesis. Cell 92 (1998) 829-839
72. Coste A., Louet J.F., Lagouge M., Lerin C., Antal M.C., Meziane H., Schoonjans K., Puigserver P., O'Malley B.W., and Auwerx J. The genetic ablation of SRC-3 protects against obesity and improves insulin sensitivity by reducing the acetylation of PGC-1{alpha}. Proc. Natl. Acad. Sci. U. S. A. 105 (2008) 17187-17192
73. Lerin C., Rodgers J.T., Kalume D.E., Kim S.H., Pandey A., and Puigserver P. GCN5 acetyltransferase complex controls glucose metabolism through transcriptional repression of PGC-1alpha. Cell Metab. 3 (2006) 429-438
74. Zhang W., Patil S., Chauhan B., Guo S., Powell D.R., Le J., Klotsas A., Matika R., Xiao X., Franks R., Heidenreich K.A., Sajan M.P., Farese R.V., Stolz D.B., Tso P., Koo S.H., Montminy M., and Unterman T.G. FoxO1 regulates multiple metabolic pathways in the liver: effects on gluconeogenic, glycolytic, and lipogenic gene expression. J. Biol. Chem. 281 (2006) 10105-10117
75. Matsumoto M., Pocai A., Rossetti L., Depinho R.A., and Accili D. Impaired regulation of hepatic glucose production in mice lacking the forkhead transcription factor Foxo1 in liver. Cell Metab. 6 (2007) 208-216
76. Frescas D., Valenti L., and Accili D. Nuclear trapping of the forkhead transcription factor FoxO1 via Sirt-dependent deacetylation promotes expression of glucogenetic genes. J. Biol. Chem. 280 (2005) 20589-20595
77. Lavu S., Boss O., Elliott P.J., and Lambert P.D. Sirtuins-novel therapeutic targets to treat age-associated diseases. Nat. Rev. Drug Discov. 7 (2008) 841-853
78. Sauve A.A., and Schramm V.L. Sir2 regulation by nicotinamide results from switching between base exchange and deacetylation chemistry. Biochemistry 42 (2003) 9249-9256
79. Landry J., Slama J.T., and Sternglanz R. Role of NAD(+) in the deacetylase activity of the SIR2-like proteins. Biochem. Biophys. Res. Commun. 278 (2000) 685-690
80. Bitterman K.J., Anderson R.M., Cohen H.Y., Latorre-Esteves M., and Sinclair D.A. Inhibition of silencing and accelerated aging by nicotinamide, a putative negative regulator of yeast sir2 and human SIRT1. J. Biol. Chem. 277 (2002) 45099-45107
81. Lin S.J., Defossez P.A., and Guarente L. Requirement of NAD and SIR2 for life-span extension by calorie restriction in Saccharomyces cerevisiae. Science 289 (2000) 2126-2128
82. Anderson R.M., Bitterman K.J., Wood J.G., Medvedik O., and Sinclair D.A. Nicotinamide and PNC1 govern lifespan extension by calorie restriction in Saccharomyces cerevisiae. Nature 423 (2003) 181-185
83. Fulco M., Cen Y., Zhao P., Hoffman E.P., McBurney M.W., Sauve A.A., and Sartorelli V. Glucose restriction inhibits skeletal myoblast differentiation by activating SIRT1 through AMPK-mediated regulation of Nampt. Dev. Cell 14 (2008) 661-673
84. van der Veer E., Nong Z., O'Neil C., Urquhart B., Freeman D., and Pickering J.G. Pre-B-cell colony-enhancing factor regulates NAD+-dependent protein deacetylase activity and promotes vascular smooth muscle cell maturation. Circ. Res. 97 (2005) 25-34
85. Nakahata Y., Sahar S., Astarita G., Kaluzova M., and Sassone-Corsi P. Circadian control of the NAD+ salvage pathway by CLOCK-SIRT1. Science 324 (2009) 654-657
86. Ramsey K.M., Yoshino J., Brace C.S., Abrassart D., Kobayashi Y., Marcheva B., Hong H.K., Chong J.L., Buhr E.D., Lee C., Takahashi J.S., Imai S., and Bass J. Circadian clock feedback cycle through NAMPT-mediated NAD+ biosynthesis. Science 324 (2009) 651-654
87. Anderson R.M., Bitterman K.J., Wood J.G., Medvedik O., Cohen H., Lin S.S., Manchester J.K., Gordon J.I., and Sinclair D.A. Manipulation of a nuclear NAD+ salvage pathway delays aging without altering steady-state NAD+ levels. J. Biol. Chem. 277 (2002) 18881-18890
88. Lin S.J., Ford E., Haigis M., Liszt G., and Guarente L. Calorie restriction extends yeast life span by lowering the level of NADH. Genes Dev. 18 (2004) 12-16
89. Lin S.J., Kaeberlein M., Andalis A.A., Sturtz L.A., Defossez P.A., Culotta V.C., Fink G.R., and Guarente L. Calorie restriction extends Saccharomyces cerevisiae lifespan by increasing respiration. Nature 418 (2002) 344-348
90. Anderson R.M., Latorre-Esteves M., Neves A.R., Lavu S., Medvedik O., Taylor C., Howitz K.T., Santos H., and Sinclair D.A. Yeast life-span extension by calorie restriction is independent of NAD fluctuation. Science 302 (2003) 2124-2126
91. Garten A., Petzold S., Korner A., Imai S., and Kiess W. Nampt: linking NAD biology, metabolism and cancer. Trends Endocrinol. Metab. 20 (2009) 130-138
92. Kitani T., Okuno S., and Fujisawa H. Growth phase-dependent changes in the subcellular localization of pre-B-cell colony-enhancing factor. FEBS Lett. 544 (2003) 74-78
93. Rongvaux A., Shea R.J., Mulks M.H., Gigot D., Urbain J., Leo O., and Andris F. Pre-B-cell colony-enhancing factor, whose expression is up-regulated in activated lymphocytes, is a nicotinamide phosphoribosyltransferase, a cytosolic enzyme involved in NAD biosynthesis. Eur. J. Immunol. 32 (2002) 3225-3234
94. Revollo J.R., Korner A., Mills K.F., Satoh A., Wang T., Garten A., Dasgupta B., Sasaki Y., Wolberger C., Townsend R.R., Milbrandt J., Kiess W., and Imai S. Nampt/PBEF/Visfatin regulates insulin secretion in beta cells as a systemic NAD biosynthetic enzyme. Cell Metab. 6 (2007) 363-375
95. Imai S. The NAD World: a new systemic regulatory network for metabolism and aging-Sirt1, systemic NAD biosynthesis, and their importance. Cell Biochem. Biophys. 53 (2009) 65-74
96. Samal B., Sun Y., Stearns G., Xie C., Suggs S., and McNiece I. Cloning and characterization of the cDNA encoding a novel human pre-B-cell colony-enhancing factor. Mol. Cell. Biol. 14 (1994) 1431-1437
97. Fukuhara A., Matsuda M., Nishizawa M., Segawa K., Tanaka M., Kishimoto K., Matsuki Y., Murakami M., Ichisaka T., Murakami H., Watanabe E., Takagi T., Akiyoshi M., Ohtsubo T., Kihara S., Yamashita S., Makishima M., Funahashi T., Yamanaka S., Hiramatsu R., Matsuzawa Y., and Shimomura I. Visfatin: a protein secreted by visceral fat that mimics the effects of insulin. Science 307 (2005) 426-430
98. Fukuhara A., Matsuda M., Nishizawa M., Segawa K., Tanaka M., Kishimoto K., Matsuki Y., Murakami M., Ichisaka T., Murakami H., Watanabe E., Takagi T., Akiyoshi M., Ohtsubo T., Kihara S., Yamashita S., Makishima M., Funahashi T., Yamanaka S., Hiramatsu R., Matsuzawa Y., and Shimomura I. Retraction. Science 318 (2007) 565
99. Revollo J.R., Grimm A.A., and Imai S. The NAD biosynthesis pathway mediated by nicotinamide phosphoribosyltransferase regulates Sir2 activity in mammalian cells. J. Biol. Chem. 279 (2004) 50754-50763
100. Rongvaux A., Galli M., Denanglaire S., Van Gool F., Dreze P.L., Szpirer C., Bureau F., Andris F., and Leo O. Nicotinamide phosphoribosyl transferase/pre-B cell colony-enhancing factor/visfatin is required for lymphocyte development and cellular resistance to genotoxic stress. J. Immunol. 181 (2008) 4685-4695
101. van der Veer E., Ho C., O'Neil C., Barbosa N., Scott R., Cregan S.P., and Pickering J.G. Extension of human cell lifespan by nicotinamide phosphoribosyltransferase. J. Biol. Chem. 282 (2007) 10841-10845
102. Yang H., Yang T., Baur J.A., Perez E., Matsui T., Carmona J.J., Lamming D.W., Souza-Pinto N.C., Bohr V.A., Rosenzweig A., de Cabo R., Sauve A.A., and Sinclair D.A. Nutrient-sensitive mitochondrial NAD+ levels dictate cell survival. Cell 130 (2007) 1095-1107
103. Dvir-Ginzberg M., Gagarina V., Lee E.J., and Hall D.J. Regulation of cartilage-specific gene expression in human chondrocytes by SirT1 and nicotinamide phosphoribosyltransferase. J. Biol. Chem. 283 (2008) 36300-36310
104. Doi M., Hirayama J., and Sassone-Corsi P. Circadian regulator CLOCK is a histone acetyltransferase. Cell 125 (2006) 497-508
105. Hirayama J., Sahar S., Grimaldi B., Tamaru T., Takamatsu K., Nakahata Y., and Sassone-Corsi P. CLOCK-mediated acetylation of BMAL1 controls circadian function. Nature 450 (2007) 1086-1090
106. Asher G., Gatfield D., Stratmann M., Reinke H., Dibner C., Kreppel F., Mostoslavsky R., Alt F.W., and Schibler U. SIRT1 regulates circadian clock gene expression through PER2 deacetylation. Cell 134 (2008) 317-328
107. Wijnen H. Circadian rhythms. A circadian loop asSIRTs itself. Science 324 (2009) 598-599
108. Lau C., Niere M., and Ziegler M. The NMN/NaMN adenylyltransferase (NMNAT) protein family. Front. Biosci. 14 (2009) 410-431
109. Berger F., Lau C., Dahlmann M., and Ziegler M. Subcellular compartmentation and differential catalytic properties of the three human nicotinamide mononucleotide adenylyltransferase isoforms. J. Biol. Chem. 280 (2005) 36334-36341
110. Mack T.G., Reiner M., Beirowski B., Mi W., Emanuelli M., Wagner D., Thomson D., Gillingwater T., Court F., Conforti L., Fernando F.S., Tarlton A., Andressen C., Addicks K., Magni G., Ribchester R.R., Perry V.H., and Coleman M.P. Wallerian degeneration of injured axons and synapses is delayed by a Ube4b/Nmnat chimeric gene. Nat. Neurosci. 4 (2001) 1199-1206
111. Conforti L., Tarlton A., Mack T.G., Mi W., Buckmaster E.A., Wagner D., Perry V.H., and Coleman M.P. A Ufd2/D4Cole1e chimeric protein and overexpression of Rbp7 in the slow Wallerian degeneration (WldS) mouse. Proc. Natl. Acad. Sci. U. S. A. 97 (2000) 11377-11382
112. Araki T., Sasaki Y., and Milbrandt J. Increased nuclear NAD biosynthesis and SIRT1 activation prevent axonal degeneration. Science 305 (2004) 1010-1013
113. Wang J., Zhai Q., Chen Y., Lin E., Gu W., McBurney M.W., and He Z. A local mechanism mediates NAD-dependent protection of axon degeneration. J. Cell. Biol. 170 (2005) 349-355
114. Zhai R.G., Cao Y., Hiesinger P.R., Zhou Y., Mehta S.Q., Schulze K.L., Verstreken P., and Bellen H.J. Drosophila NMNAT maintains neural integrity independent of its NAD synthesis activity. PLoS Biol. 4 (2006) e416
115. Zhai R.G., Zhang F., Hiesinger P.R., Cao Y., Haueter C.M., and Bellen H.J. NAD synthase NMNAT acts as a chaperone to protect against neurodegeneration. Nature 452 (2008) 887-891
116. Conforti L., Fang G., Beirowski B., Wang M.S., Sorci L., Asress S., Adalbert R., Silva A., Bridge K., Huang X.P., Magni G., Glass J.D., and Coleman M.P. NAD(+) and axon degeneration revisited: Nmnat1 cannot substitute for Wld(S) to delay Wallerian degeneration. Cell Death Differ. 14 (2007) 116-127
117. Fainzilber M., and Twiss J.L. Tracking in the Wlds-the hunting of the SIRT and the luring of the Draper. Neuron 50 (2006) 819-821
118. Zhang T., Berrocal J.G., Frizzell K.M., Gamble M.J., Dumond M.E., Krishnakumar R., Yang T., Sauve A.A., and Kraus W.L. Enzymes in the NAD+ salvage pathway regulate SIRT1 activity at target gene promoters. J. Biol. Chem. 284 (2009) 20408-20417
119. Srere P.A. Complexes of sequential metabolic enzymes. Annu. Rev. Biochem. 56 (1987) 89-124
120. Grubisha O., Smith B.C., and Denu J.M. Small molecule regulation of Sir2 protein deacetylases. FEBS J. 272 (2005) 4607-4616
121. Berger F., Lau C., and Ziegler M. Regulation of poly(ADP-ribose) polymerase 1 activity by the phosphorylation state of the nuclear NAD biosynthetic enzyme NMN adenylyl transferase 1. Proc. Natl. Acad. Sci. U. S. A. 104 (2007) 3765-3770
122. Kim M.Y., Zhang T., and Kraus W.L. Poly(ADP-ribosyl)ation by PARP-1: 'PAR-laying' NAD+ into a nuclear signal. Genes Dev. 19 (2005) 1951-1967
123. Kraus W.L. Transcriptional control by PARP-1: chromatin modulation, enhancer-binding, coregulation, and insulation. Curr. Opin. Cell Biol. 20 (2008) 294-302
124. Pillai J.B., Isbatan A., Imai S., and Gupta M.P. Poly(ADP-ribose) polymerase-1-dependent cardiac myocyte cell death during heart failure is mediated by NAD+ depletion and reduced Sir2alpha deacetylase activity. J. Biol. Chem. 280 (2005) 43121-43130
125. Zhang J. Are poly(ADP-ribosyl)ation by PARP-1 and deacetylation by Sir2 linked?. BioEssays 25 (2003) 808-814
126. Ame J.C., Spenlehauer C., and de Murcia G. The PARP superfamily. BioEssays 26 (2004) 882-893
127. Kolthur-Seetharam U., Dantzer F., McBurney M.W., de Murcia G., and Sassone-Corsi P. Control of AIF-mediated cell death by the functional interplay of SIRT1 and PARP-1 in response to DNA damage. Cell Cycle 5 (2006) 873-877
128. Rajamohan S.B., Pillai V.B., Gupta M., Sundaresan N.R., Birukov K.G., Samant S., Hottiger M.O., and Gupta M.P. SIRT1 promotes cell survival under stress by deacetylation-dependent deactivation of poly(ADP-ribose) polymerase 1. Mol. Cell. Biol. 29 (2009) 4116-4129
129. Wang C., Chen L., Hou X., Li Z., Kabra N., Ma Y., Nemoto S., Finkel T., Gu W., Cress W.D., and Chen J. Interactions between E2F1 and SirT1 regulate apoptotic response to DNA damage. Nat. Cell Biol. 8 (2006) 1025-1031
130. van der Horst A., Tertoolen L.G., de Vries-Smits L.M., Frye R.A., Medema R.H., and Burgering B.M. FOXO4 is acetylated upon peroxide stress and deacetylated by the longevity protein hSir2(SIRT1). J. Biol. Chem. 279 (2004) 28873-28879
131. Daitoku H., Hatta M., Matsuzaki H., Aratani S., Ohshima T., Miyagishi M., Nakajima T., and Fukamizu A. Silent information regulator 2 potentiates Foxo1-mediated transcription through its deacetylase activity. Proc. Natl. Acad. Sci. U. S. A. 101 (2004) 10042-10047
132. Qiao L., and Shao J. SIRT1 regulates adiponectin gene expression through Foxo1-C/enhancer-binding protein alpha transcriptional complex. J. Biol. Chem. 281 (2006) 39915-39924
133. Potente M., Ghaeni L., Baldessari D., Mostoslavsky R., Rossig L., Dequiedt F., Haendeler J., Mione M., Dejana E., Alt F.W., Zeiher A.M., and Dimmeler S. SIRT1 controls endothelial angiogenic functions during vascular growth. Genes Dev. 21 (2007) 2644-2658
134. Zhao X., Sternsdorf T., Bolger T.A., Evans R.M., and Yao T.P. Regulation of MEF2 by histone deacetylase 4- and SIRT1 deacetylase-mediated lysine modifications. Mol. Cell. Biol. 25 (2005) 8456-8464
135. Fulco M., Schiltz R.L., Iezzi S., King M.T., Zhao P., Kashiwaya Y., Hoffman E., Veech R.L., and Sartorelli V. Sir2 regulates skeletal muscle differentiation as a potential sensor of the redox state. Mol. Cell 12 (2003) 51-62
136. Langley E., Pearson M., Faretta M., Bauer U.M., Frye R.A., Minucci S., Pelicci P.G., and Kouzarides T. Human SIR2 deacetylates p53 and antagonizes PML/p53-induced cellular senescence. EMBO J. 21 (2002) 2383-2396
137. Cheng H.L., Mostoslavsky R., Saito S., Manis J.P., Gu Y., Patel P., Bronson R., Appella E., Alt F.W., and Chua K.F. Developmental defects and p53 hyperacetylation in Sir2 homolog (SIRT1)-deficient mice. Proc. Natl. Acad. Sci. U. S. A. 100 (2003) 10794-10799
138. Dai J.M., Wang Z.Y., Sun D.C., Lin R.X., and Wang S.Q. SIRT1 interacts with p73 and suppresses p73-dependent transcriptional activity. J. Cell. Physiol. 210 (2007) 161-166
139. Pediconi N., Guerrieri F., Vossio S., Bruno T., Belloni L., Schinzari V., Scisciani C., Fanciulli M., and Levrero M. hSirT1-dependent regulation of the PCAF-E2F1-p73 apoptotic pathway in response to DNA damage. Mol. Cell. Biol. 29 (2009) 1989-1998
140. Yeung F., Hoberg J.E., Ramsey C.S., Keller M.D., Jones D.R., Frye R.A., and Mayo M.W. Modulation of NF-kappaB-dependent transcription and cell survival by the SIRT1 deacetylase. EMBO J. 23 (2004) 2369-2380
141. Chen J., Zhou Y., Mueller-Steiner S., Chen L.F., Kwon H., Yi S., Mucke L., and Gan L. SIRT1 protects against microglia-dependent amyloid-beta toxicity through inhibiting NF-kappaB signaling. J. Biol. Chem. 280 (2005) 40364-40374
142. Kume S., Haneda M., Kanasaki K., Sugimoto T., Araki S., Isshiki K., Isono M., Uzu T., Guarente L., Kashiwagi A., and Koya D. SIRT1 inhibits transforming growth factor beta-induced apoptosis in glomerular mesangial cells via Smad7 deacetylation. J. Biol. Chem. 282 (2007) 151-158
143. Muth V., Nadaud S., Grummt I., and Voit R. Acetylation of TAF(I)68, a subunit of TIF-IB/SL1, activates RNA polymerase I transcription. EMBO J. 20 (2001) 1353-1362
144. Senawong T., Peterson V.J., and Leid M. BCL11A-dependent recruitment of SIRT1 to a promoter template in mammalian cells results in histone deacetylation and transcriptional repression. Arch. Biochem. Biophys. 434 (2005) 316-325
145. Senawong T., Peterson V.J., Avram D., Shepherd D.M., Frye R.A., Minucci S., and Leid M. Involvement of the histone deacetylase SIRT1 in chicken ovalbumin upstream promoter transcription factor (COUP-TF)-interacting protein 2-mediated transcriptional repression. J. Biol. Chem. 278 (2003) 43041-43050
146. Takata T., and Ishikawa F. Human Sir2-related protein SIRT1 associates with the bHLH repressors HES1 and HEY2 and is involved in HES1- and HEY2-mediated transcriptional repression. Biochem. Biophys. Res. Commun. 301 (2003) 250-257
147. Prozorovski T., Schulze-Topphoff U., Glumm R., Baumgart J., Schroter F., Ninnemann O., Siegert E., Bendix I., Brustle O., Nitsch R., Zipp F., and Aktas O. Sirt1 contributes critically to the redox-dependent fate of neural progenitors. Nat. Cell Biol. 10 (2008) 385-394
148. Chen W.Y., Wang D.H., Yen R.C., Luo J., Gu W., and Baylin S.B. Tumor suppressor HIC1 directly regulates SIRT1 to modulate p53-dependent DNA-damage responses. Cell 123 (2005) 437-448
149. Picard F., Kurtev M., Chung N., Topark-Ngarm A., Senawong T., Machado De Oliveira R., Leid M., McBurney M.W., and Guarente L. Sirt1 promotes fat mobilization in white adipocytes by repressing PPAR-gamma. Nature 429 (2004) 771-776
150. Pagans S., Pedal A., North B.J., Kaehlcke K., Marshall B.L., Dorr A., Hetzer-Egger C., Henklein P., Frye R., McBurney M.W., Hruby H., Jung M., Verdin E., and Ott M. SIRT1 regulates HIV transcription via Tat deacetylation. PLoS Biol. 3 (2005) e41