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Volumn 32, Issue 14, 2012, Pages 2823-2836

SIRT1 Negatively Regulates the Activities, Functions, and Protein Levels of hmof and TIP60

Author keywords

[No Author keywords available]

Indexed keywords

ACYLTRANSFERASE; ARGININE; HMOF PROTEIN; LYSINE; SIRTUIN 1; TIP60 PROTEIN; UNCLASSIFIED DRUG;

EID: 84864020743     PISSN: 02707306     EISSN: 10985549     Source Type: Journal    
DOI: 10.1128/MCB.00496-12     Document Type: Article
Times cited : (81)

References (90)
  • 1
    • 0033866836 scopus 로고    scopus 로고
    • Activation of transcription through histone H4 acetylation by MOF, an acetyltransferase essential for dosage compensation in Drosophila
    • Akhtar A, Becker PB. 2000. Activation of transcription through histone H4 acetylation by MOF, an acetyltransferase essential for dosage compensation in Drosophila. Mol. Cell 5:367-375.
    • (2000) Mol. Cell , vol.5 , pp. 367-375
    • Akhtar, A.1    Becker, P.B.2
  • 2
    • 34547896549 scopus 로고    scopus 로고
    • The MYST family of histone acetyltransferases and their intimate links to cancer
    • Avvakumov N, Cote J. 2007. The MYST family of histone acetyltransferases and their intimate links to cancer. Oncogene 26:5395-5407.
    • (2007) Oncogene , vol.26 , pp. 5395-5407
    • Avvakumov, N.1    Cote, J.2
  • 3
    • 3943054839 scopus 로고    scopus 로고
    • The Sir2 family of protein deacetylases
    • Blander G, Guarente L. 2004. The Sir2 family of protein deacetylases. Annu. Rev. Biochem. 73:417- 435.
    • (2004) Annu. Rev. Biochem. , vol.73 , pp. 417-435
    • Blander, G.1    Guarente, L.2
  • 4
    • 15444377466 scopus 로고    scopus 로고
    • SIRT1 deacetylation and repression of p300 involves lysine residues 1020/1024 within the cell cycle regulatory domain 1
    • Bouras T, et al. 2005. SIRT1 deacetylation and repression of p300 involves lysine residues 1020/1024 within the cell cycle regulatory domain 1. J. Biol. Chem. 280:10264 -10276.
    • (2005) J. Biol. Chem. , vol.280 , pp. 10264-10276
    • Bouras, T.1
  • 5
    • 12144290563 scopus 로고    scopus 로고
    • Stress-dependent regulation of FOXO transcription factors by the SIRT1 deacetylase
    • Brunet A, et al. 2004. Stress-dependent regulation of FOXO transcription factors by the SIRT1 deacetylase. Science 303:2011-2015.
    • (2004) Science , vol.303 , pp. 2011-2015
    • Brunet, A.1
  • 6
    • 80053168829 scopus 로고    scopus 로고
    • Absence of effects of Sir2 overexpression on lifespan in C. elegans and Drosophila
    • Burnett C, et al. 2011. Absence of effects of Sir2 overexpression on lifespan in C. elegans and Drosophila. Nature 477:482- 485.
    • (2011) Nature , vol.477 , pp. 482-485
    • Burnett, C.1
  • 7
    • 77951182263 scopus 로고    scopus 로고
    • Subunit composition and substrate specificity of a MOF-containing histone acetyltransferase distinct from the male-specific lethal MSL complex
    • Cai Y, et al. 2010. Subunit composition and substrate specificity of a MOF-containing histone acetyltransferase distinct from the male-specific lethal MSL complex. J. Biol. Chem. 285:4268-4272.
    • (2010) J. Biol. Chem. , vol.285 , pp. 4268-4272
    • Cai, Y.1
  • 8
    • 0242322038 scopus 로고    scopus 로고
    • Identification of new subunits of the multiprotein mammalian TRRAP/TIP60-containing histone acetyltransferase complex
    • Cai Y, et al. 2003. Identification of new subunits of the multiprotein mammalian TRRAP/TIP60-containing histone acetyltransferase complex. J. Biol. Chem. 278:42733- 42736.
    • (2003) J. Biol. Chem. , vol.278 , pp. 42733-42736
    • Cai, Y.1
  • 9
    • 17844385784 scopus 로고    scopus 로고
    • Regulatory cross-talk between lysine acetylation and ubiquitination: role in the control of protein stability
    • Caron C, Boyault C, Khochbin S. 2005. Regulatory cross-talk between lysine acetylation and ubiquitination: role in the control of protein stability. BioEssays 27:408-415.
    • (2005) BioEssays , vol.27 , pp. 408-415
    • Caron, C.1    Boyault, C.2    Khochbin, S.3
  • 10
    • 79958068204 scopus 로고    scopus 로고
    • Phosphorylation of Tip60 by GSK-3 determines the induction of PUMA and apoptosis by p53
    • Charvet C, et al. 2011. Phosphorylation of Tip60 by GSK-3 determines the induction of PUMA and apoptosis by p53. Mol. Cell 42:584 -596.
    • (2011) Mol. Cell , vol.42 , pp. 584-596
    • Charvet, C.1
  • 11
    • 34248640428 scopus 로고    scopus 로고
    • Lysine propionylation and butyrylation are novel post-translational modifications in histones
    • Chen Y, et al. 2007. Lysine propionylation and butyrylation are novel post-translational modifications in histones. Mol. Cell. Proteomics 6:812- 819.
    • (2007) Mol. Cell. Proteomics , vol.6 , pp. 812-819
    • Chen, Y.1
  • 12
    • 0141814680 scopus 로고    scopus 로고
    • Developmental defects and p53 hyperacetylation in Sir2 homolog (SIRT1)-deficient mice
    • Cheng HL, et al. 2003. Developmental defects and p53 hyperacetylation in Sir2 homolog (SIRT1)-deficient mice. Proc. Natl. Acad. Sci. U. S. A. 100:10794 -10799.
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 10794-10799
    • Cheng, H.L.1
  • 13
    • 38949206260 scopus 로고    scopus 로고
    • Functional characterization of TIP60 sumoylation in UV-irradiated DNA damage response
    • Cheng Z, et al. 2008. Functional characterization of TIP60 sumoylation in UV-irradiated DNA damage response. Oncogene 27:931-941.
    • (2008) Oncogene , vol.27 , pp. 931-941
    • Cheng, Z.1
  • 14
    • 3142740860 scopus 로고    scopus 로고
    • Calorie restriction promotes mammalian cell survival by inducing the SIRT1 deacetylase
    • Cohen HY, et al. 2004. Calorie restriction promotes mammalian cell survival by inducing the SIRT1 deacetylase. Science 305:390 -392.
    • (2004) Science , vol.305 , pp. 390-392
    • Cohen, H.Y.1
  • 15
    • 23044476198 scopus 로고    scopus 로고
    • HIV- 1 Tat targets Tip60 to impair the apoptotic cell response to genotoxic stresses
    • Col E, et al. 2005. HIV-1 Tat targets Tip60 to impair the apoptotic cell response to genotoxic stresses. EMBO J. 24:2634 -2645.
    • (2005) EMBO J , vol.24 , pp. 2634-2645
    • Col, E.1
  • 16
    • 57449099865 scopus 로고    scopus 로고
    • MaxQuant enables high peptide identification rates, individualized p.p.b -range mass accuracies and proteome-wide protein quantification
    • Cox J, Mann M. 2008. MaxQuant enables high peptide identification rates, individualized p.p.b.-range mass accuracies and proteome-wide protein quantification. Nat. Biotechnol. 26:1367-1372.
    • (2008) Nat. Biotechnol. , vol.26 , pp. 1367-1372
    • Cox, J.1    Mann, M.2
  • 17
    • 67649400942 scopus 로고    scopus 로고
    • A practical guide to the MaxQuant computational platform for SILAC-based quantitative proteomics
    • Cox J, et al. 2009. A practical guide to the MaxQuant computational platform for SILAC-based quantitative proteomics. Nat. Protoc. 4:698- 705.
    • (2009) Nat. Protoc. , vol.4 , pp. 698-705
    • Cox, J.1
  • 18
    • 67149099680 scopus 로고    scopus 로고
    • Histone H4 lysine 16 acetylation regulates cellular lifespan
    • Dang W, et al. 2009. Histone H4 lysine 16 acetylation regulates cellular lifespan. Nature 459:802- 807.
    • (2009) Nature , vol.459 , pp. 802-807
    • Dang, W.1
  • 19
    • 66749129781 scopus 로고    scopus 로고
    • Regulation of hypoxia-inducible factor 2α signaling by the stress-responsive deacetylase sirtuin 1
    • Dioum EM, et al. 2009. Regulation of hypoxia-inducible factor 2α signaling by the stress-responsive deacetylase sirtuin 1. Science 324:1289- 1293.
    • (2009) Science , vol.324 , pp. 1289-1293
    • Dioum, E.M.1
  • 20
    • 20444397430 scopus 로고    scopus 로고
    • Physical association and coordinate function of the H3 K4 methyltransferase MLL1 and the H4 K16 acetyltransferase MOF
    • Dou Y, et al. 2005. Physical association and coordinate function of the H3 K4 methyltransferase MLL1 and the H4 K16 acetyltransferase MOF. Cell 121:873- 885.
    • (2005) Cell , vol.121 , pp. 873-885
    • Dou, Y.1
  • 21
    • 1342346531 scopus 로고    scopus 로고
    • Structural and functional conservation of the NuA4 histone acetyltransferase complex from yeast to humans
    • Doyon Y, Selleck W, Lane WS, Tan S, Cote J. 2004. Structural and functional conservation of the NuA4 histone acetyltransferase complex from yeast to humans. Mol. Cell. Biol. 24:1884 -1896.
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 1884-1896
    • Doyon, Y.1    Selleck, W.2    Lane, W.S.3    Tan, S.4    Cote, J.5
  • 22
    • 77955501963 scopus 로고    scopus 로고
    • SIRT1 regulates UV-induced DNA repair through deacetylating XPA
    • Fan W, Luo J. 2010. SIRT1 regulates UV-induced DNA repair through deacetylating XPA. Mol. Cell 39:247-258.
    • (2010) Mol. Cell , vol.39 , pp. 247-258
    • Fan, W.1    Luo, J.2
  • 23
    • 67949102053 scopus 로고    scopus 로고
    • Recent progress in the biology and physiology of sirtuins
    • Finkel T, Deng CX, Mostoslavsky R. 2009. Recent progress in the biology and physiology of sirtuins. Nature 460:587-591.
    • (2009) Nature , vol.460 , pp. 587-591
    • Finkel, T.1    Deng, C.X.2    Mostoslavsky, R.3
  • 24
    • 37549014206 scopus 로고    scopus 로고
    • The mammalian ortholog of Drosophila MOF that acetylates histone H4 lysine 16 is essential for embryogenesis and oncogenesis
    • Gupta A, et al. 2008. The mammalian ortholog of Drosophila MOF that acetylates histone H4 lysine 16 is essential for embryogenesis and oncogenesis. Mol. Cell. Biol. 28:397- 409.
    • (2008) Mol. Cell. Biol. , vol.28 , pp. 397-409
    • Gupta, A.1
  • 25
    • 33751113602 scopus 로고    scopus 로고
    • Mammalian sirtuins-emerging roles in physiology, aging, and calorie restriction
    • Haigis MC, Guarente LP. 2006. Mammalian sirtuins- emerging roles in physiology, aging, and calorie restriction. Genes Dev. 20:2913-2921.
    • (2006) Genes Dev , vol.20 , pp. 2913-2921
    • Haigis, M.C.1    Guarente, L.P.2
  • 26
    • 77949887506 scopus 로고    scopus 로고
    • Mammalian sirtuins: biological insights and disease relevance
    • Haigis MC, Sinclair DA. 2010. Mammalian sirtuins: biological insights and disease relevance. Annu. Rev. Pathol. 5:253-295.
    • (2010) Annu. Rev. Pathol. , vol.5 , pp. 253-295
    • Haigis, M.C.1    Sinclair, D.A.2
  • 27
    • 78649482634 scopus 로고    scopus 로고
    • SIRT1: recent lessons from mouse models
    • Herranz D, Serrano M. 2010. SIRT1: recent lessons from mouse models. Nat. Rev. Cancer. 10:819-823.
    • (2010) Nat. Rev. Cancer. , vol.10 , pp. 819-823
    • Herranz, D.1    Serrano, M.2
  • 28
    • 0030891858 scopus 로고    scopus 로고
    • mof, a putative acetyl transferase gene related to the Tip60 and MOZ human genes and to the SAS genes of yeast, is required for dosage compensation in Drosophila
    • Hilfiker A, Hilfiker-Kleiner D, Pannuti A, Lucchesi JC. 1997. mof, a putative acetyl transferase gene related to the Tip60 and MOZ human genes and to the SAS genes of yeast, is required for dosage compensation in Drosophila. EMBO J. 16:2054 -2060.
    • (1997) EMBO J , vol.16 , pp. 2054-2060
    • Hilfiker, A.1    Hilfiker-Kleiner, D.2    Pannuti, A.3    Lucchesi, J.C.4
  • 29
    • 0034682736 scopus 로고    scopus 로고
    • Involvement of the TIP60 histone acetylase complex in DNA repair and apoptosis
    • Ikura T, et al. 2000. Involvement of the TIP60 histone acetylase complex in DNA repair and apoptosis. Cell 102:463- 473.
    • (2000) Cell , vol.102 , pp. 463-473
    • Ikura, T.1
  • 30
    • 0034677535 scopus 로고    scopus 로고
    • Transcriptional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase
    • Imai S, Armstrong CM, Kaeberlein M, Guarente L. 2000. Transcriptional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase. Nature 403:795- 800.
    • (2000) Nature , vol.403 , pp. 795-800
    • Imai, S.1    Armstrong, C.M.2    Kaeberlein, M.3    Guarente, L.4
  • 31
    • 33847647624 scopus 로고    scopus 로고
    • SIRT1 promotes DNA repair activity and deacetylation of Ku70
    • Jeong J, et al. 2007. SIRT1 promotes DNA repair activity and deacetylation of Ku70. Exp. Mol. Med. 39:8 -13.
    • (2007) Exp. Mol. Med. , vol.39 , pp. 8-13
    • Jeong, J.1
  • 32
    • 79551625231 scopus 로고    scopus 로고
    • Structural basis for MOF and MSL3 recruitment into the dosage compensation complex by MSL1
    • Kadlec J, et al. 2011. Structural basis for MOF and MSL3 recruitment into the dosage compensation complex by MSL1. Nat. Struct. Mol. Biol. 18: 142-149.
    • (2011) Nat. Struct. Mol. Biol. , vol.18 , pp. 142-149
    • Kadlec, J.1
  • 33
    • 19344374925 scopus 로고    scopus 로고
    • Sir2-independent life span extension by calorie restriction in yeast
    • doi: 10.1371/journal.pbio.0020296
    • Kaeberlein M, Kirkland KT, Fields S, Kennedy BK. 2004. Sir2-independent life span extension by calorie restriction in yeast. PLoS Biol. 2:E296. doi:10.1371/journal.pbio.0020296.
    • (2004) PLoS Biol , vol.2
    • Kaeberlein, M.1    Kirkland, K.T.2    Fields, S.3    Kennedy, B.K.4
  • 34
    • 0033214237 scopus 로고    scopus 로고
    • The SIR2/3/4 complex and SIR2 alone promote longevity in Saccharomyces cerevisiae by two different mechanisms
    • Kaeberlein M, McVey M, Guarente L. 1999. The SIR2/3/4 complex and SIR2 alone promote longevity in Saccharomyces cerevisiae by two different mechanisms. Genes Dev. 13:2570 -2580.
    • (1999) Genes Dev , vol.13 , pp. 2570-2580
    • Kaeberlein, M.1    McVey, M.2    Guarente, L.3
  • 35
    • 10844233155 scopus 로고    scopus 로고
    • Acetylation by Tip60 is required for selective histone variant exchange at DNA lesions
    • Kusch T, et al. 2004. Acetylation by Tip60 is required for selective histone variant exchange at DNA lesions. Science 306:2084 -2087.
    • (2004) Science , vol.306 , pp. 2084-2087
    • Kusch, T.1
  • 36
    • 0037093346 scopus 로고    scopus 로고
    • Human SIR2 deacetylates p53 and antagonizes PML/p53-induced cellular senescence
    • Langley E, et al. 2002. Human SIR2 deacetylates p53 and antagonizes PML/p53-induced cellular senescence. EMBO J. 21:2383-2396.
    • (2002) EMBO J , vol.21 , pp. 2383-2396
    • Langley, E.1
  • 37
    • 0033565609 scopus 로고    scopus 로고
    • Role of yeast SIR genes and mating type in directing DNA double-strand breaks to homologous and non-homologous repair paths
    • Lee SE, Paques F, Sylvan J, Haber JE. 1999. Role of yeast SIR genes and mating type in directing DNA double-strand breaks to homologous and non-homologous repair paths. Curr. Biol. 9:767-770.
    • (1999) Curr. Biol. , vol.9 , pp. 767-770
    • Lee, S.E.1    Paques, F.2    Sylvan, J.3    Haber, J.E.4
  • 38
    • 0037007236 scopus 로고    scopus 로고
    • Tip60 is targeted to proteasome-mediated degradation by Mdm2 and accumulates after UV irradiation
    • Legube G, et al. 2002. Tip60 is targeted to proteasome-mediated degradation by Mdm2 and accumulates after UV irradiation. EMBO J. 21: 1704-1712.
    • (2002) EMBO J , vol.21 , pp. 1704-1712
    • Legube, G.1
  • 39
    • 0038576279 scopus 로고    scopus 로고
    • Tip60 acetyltransferase activity is controlled by phosphorylation
    • Lemercier C, et al. 2003. Tip60 acetyltransferase activity is controlled by phosphorylation. J. Biol. Chem. 278:4713- 4718.
    • (2003) J. Biol. Chem. , vol.278 , pp. 4713-4718
    • Lemercier, C.1
  • 40
    • 43149118368 scopus 로고    scopus 로고
    • Regulation of WRN protein cellular localization and enzymatic activities by SIRT1-mediated deacetylation
    • Li K, et al. 2008. Regulation of WRN protein cellular localization and enzymatic activities by SIRT1-mediated deacetylation. J. Biol. Chem. 283: 7590-7598.
    • (2008) J. Biol. Chem. , vol.283 , pp. 7590-7598
    • Li, K.1
  • 41
    • 70350012477 scopus 로고    scopus 로고
    • Two mammalian MOF complexes regulate transcription activation by distinct mechanisms
    • Li X, Wu L, Corsa CA, Kunkel S, Dou Y. 2009. Two mammalian MOF complexes regulate transcription activation by distinct mechanisms. Mol. Cell 36:290 -301.
    • (2009) Mol. Cell , vol.36 , pp. 290-301
    • Li, X.1    Wu, L.2    Corsa, C.A.3    Kunkel, S.4    Dou, Y.5
  • 42
    • 77955499804 scopus 로고    scopus 로고
    • Sirtuin 1 modulates cellular responses to hypoxia by deacetylating hypoxia-inducible factor 1α
    • Lim JH, et al. 2010. Sirtuin 1 modulates cellular responses to hypoxia by deacetylating hypoxia-inducible factor 1α. Mol. Cell 38:864-878.
    • (2010) Mol. Cell , vol.38 , pp. 864-878
    • Lim, J.H.1
  • 43
    • 85027946003 scopus 로고    scopus 로고
    • Modulations of hMOF autoacetylation by SIRT1 regulatehMOFrecruitment and activities on the chromatin
    • Lu L, et al. 2011. Modulations of hMOF autoacetylation by SIRT1 regulatehMOFrecruitment and activities on the chromatin. Cell Res. 21:1182- 1195.
    • (2011) Cell Res , vol.21 , pp. 1182-1195
    • Lu, L.1
  • 44
    • 0035913911 scopus 로고    scopus 로고
    • Negative control of p53 by Sir2α promotes cell survival under stress
    • Luo J, et al. 2001. Negative control of p53 by Sir2α promotes cell survival under stress. Cell 107:137-148.
    • (2001) Cell , vol.107 , pp. 137-148
    • Luo, J.1
  • 45
    • 0037207475 scopus 로고    scopus 로고
    • The mammalian SIR2α protein has a role in embryogenesis and gametogenesis
    • McBurney MW, et al. 2003. The mammalian SIR2α protein has a role in embryogenesis and gametogenesis. Mol. Cell. Biol. 23:38 -54.
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 38-54
    • McBurney, M.W.1
  • 46
    • 34249083199 scopus 로고    scopus 로고
    • Sirtuins in mammals: insights into their biological function
    • Michan S, Sinclair D. 2007. Sirtuins in mammals: insights into their biological function. Biochem. J. 404:1-13.
    • (2007) Biochem. J. , vol.404 , pp. 1-13
    • Michan, S.1    Sinclair, D.2
  • 47
    • 0034791301 scopus 로고    scopus 로고
    • Common themes in mechanisms of gene silencing
    • Moazed D. 2001. Common themes in mechanisms of gene silencing. Mol. Cell 8:489-498.
    • (2001) Mol. Cell , vol.8 , pp. 489-498
    • Moazed, D.1
  • 48
    • 1342264308 scopus 로고    scopus 로고
    • Mammalian SIRT1 represses forkhead transcription factors
    • Motta MC, et al. 2004. Mammalian SIRT1 represses forkhead transcription factors. Cell 116:551-563.
    • (2004) Cell , vol.116 , pp. 551-563
    • Motta, M.C.1
  • 49
    • 79958037576 scopus 로고    scopus 로고
    • A SIRT1-LSD1 corepressor complex regulates Notch target gene expression and development
    • Mulligan P, et al. 2011. A SIRT1-LSD1 corepressor complex regulates Notch target gene expression and development. Mol. Cell 42:689-699.
    • (2011) Mol. Cell , vol.42 , pp. 689-699
    • Mulligan, P.1
  • 50
    • 0033973262 scopus 로고    scopus 로고
    • A new human member of the MYST family of histone acetyl transferases with high sequence similarity to Drosophila MOF
    • Neal KC, Pannuti A, Smith ER, Lucchesi JC. 2000. A new human member of the MYST family of histone acetyl transferases with high sequence similarity to Drosophila MOF. Biochim. Biophys. Acta 1490:170- 174.
    • (2000) Biochim. Biophys. Acta , vol.1490 , pp. 170-174
    • Neal, K.C.1    Pannuti, A.2    Smith, E.R.3    Lucchesi, J.C.4
  • 51
    • 56749156405 scopus 로고    scopus 로고
    • SIRT1 redistribution on chromatin promotes genomic stability but alters gene expression during aging
    • Oberdoerffer P, et al. 2008. SIRT1 redistribution on chromatin promotes genomic stability but alters gene expression during aging. Cell 135:907- 918.
    • (2008) Cell , vol.135 , pp. 907-918
    • Oberdoerffer, P.1
  • 52
    • 0036583926 scopus 로고    scopus 로고
    • Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics
    • Ong SE, et al. 2002. Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics. Mol. Cell. Proteomics 1:376 -386.
    • (2002) Mol. Cell. Proteomics , vol.1 , pp. 376-386
    • Ong, S.E.1
  • 53
    • 34247396011 scopus 로고    scopus 로고
    • A practical recipe for stable isotope labeling by amino acids in cell culture SILAC
    • Ong SE, Mann M. 2006. A practical recipe for stable isotope labeling by amino acids in cell culture SILAC. Nat. Protoc. 1:2650 -2660.
    • (2006) Nat. Protoc. , vol.1 , pp. 2650-2660
    • Ong, S.E.1    Mann, M.2
  • 54
    • 0037184965 scopus 로고    scopus 로고
    • MRG15, a novel chromodomain protein, is present in two distinct multiprotein complexes involved in transcriptional activation
    • Pardo PS, Leung JK, Lucchesi JC, Pereira-Smith OM. 2002. MRG15, a novel chromodomain protein, is present in two distinct multiprotein complexes involved in transcriptional activation. J. Biol. Chem. 277: 50860-50866.
    • (2002) J. Biol. Chem. , vol.277 , pp. 50860-50866
    • Pardo, P.S.1    Leung, J.K.2    Lucchesi, J.C.3    Pereira-Smith, O.M.4
  • 55
    • 64649092913 scopus 로고    scopus 로고
    • hSirT1-dependent regulation of the PCAF-E2F1-p73 apoptotic pathway in response to DNA damage
    • Pediconi N, et al. 2009. hSirT1-dependent regulation of the PCAF-E2F1-p73 apoptotic pathway in response to DNA damage. Mol. Cell. Biol. 29: 1989-1998.
    • (2009) Mol. Cell. Biol. , vol.29 , pp. 1989-1998
    • Pediconi, N.1
  • 56
    • 83255186739 scopus 로고    scopus 로고
    • SIRT1 deacetylates the DNA methyltransferase 1 (DNMT1) protein and alters its activities
    • Peng L, et al. 2011. SIRT1 deacetylates the DNA methyltransferase 1 (DNMT1) protein and alters its activities. Mol. Cell. Biol. 31:4720-4734.
    • (2011) Mol. Cell. Biol. , vol.31 , pp. 4720-4734
    • Peng, L.1
  • 57
    • 34547913733 scopus 로고    scopus 로고
    • Males absent on the first MOF: from flies to humans
    • Rea S, Xouri G, Akhtar A. 2007. Males absent on the first MOF: from flies to humans. Oncogene 26:5385-5394.
    • (2007) Oncogene , vol.26 , pp. 5385-5394
    • Rea, S.1    Xouri, G.2    Akhtar, A.3
  • 58
    • 0023340731 scopus 로고
    • Four genes responsible for a position effect on expression from HML and HMR in Saccharomyces cerevisiae
    • Rine J, Herskowitz I. 1987. Four genes responsible for a position effect on expression from HML and HMR in Saccharomyces cerevisiae. Genetics 116:9 -22.
    • (1987) Genetics , vol.116 , pp. 9-22
    • Rine, J.1    Herskowitz, I.2
  • 59
    • 14544282413 scopus 로고    scopus 로고
    • Nutrient control of glucose homeostasis through a complex of PGC-1α and SIRT1
    • Rodgers JT, et al. 2005. Nutrient control of glucose homeostasis through a complex of PGC-1α and SIRT1. Nature 434:113-118.
    • (2005) Nature , vol.434 , pp. 113-118
    • Rodgers, J.T.1
  • 60
    • 80054771657 scopus 로고    scopus 로고
    • The role of mammalian sirtuins in the regulation of metabolism, aging, and longevity
    • Satoh A, Stein L, Imai S. 2011. The role of mammalian sirtuins in the regulation of metabolism, aging, and longevity. Handb. Exp. Pharmacol. 206:125-162.
    • (2011) Handb. Exp. Pharmacol. , vol.206 , pp. 125-162
    • Satoh, A.1    Stein, L.2    Imai, S.3
  • 61
    • 61849177618 scopus 로고    scopus 로고
    • Chromatin state marks cell-type-and genderspecific replication of the Drosophila genome
    • Schwaiger M, et al. 2009. Chromatin state marks cell-type- and genderspecific replication of the Drosophila genome. Genes Dev. 23:589-601.
    • (2009) Genes Dev , vol.23 , pp. 589-601
    • Schwaiger, M.1
  • 62
    • 32444434989 scopus 로고    scopus 로고
    • Histone H4-K16 acetylation controls chromatin structure and protein interactions
    • Shogren-Knaak M, et al. 2006. Histone H4-K16 acetylation controls chromatin structure and protein interactions. Science 311:844-847.
    • (2006) Science , vol.311 , pp. 844-847
    • Shogren-Knaak, M.1
  • 63
    • 27144546434 scopus 로고    scopus 로고
    • A human protein complex homologous to the Drosophila MSL complex is responsible for the majority of histone H4 acetylation at lysine 16
    • Smith ER, et al. 2005. A human protein complex homologous to the Drosophila MSL complex is responsible for the majority of histone H4 acetylation at lysine 16. Mol. Cell. Biol. 25:9175-9188.
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 9175-9188
    • Smith, E.R.1
  • 64
    • 79961209537 scopus 로고    scopus 로고
    • Regulation of the histone acetyltransferase activity of hMOF via autoacetylation of Lys274
    • Sun B, et al. 2011. Regulation of the histone acetyltransferase activity of hMOF via autoacetylation of Lys274. Cell Res. 21:1262-1266.
    • (2011) Cell Res , vol.21 , pp. 1262-1266
    • Sun, B.1
  • 65
    • 24944516931 scopus 로고    scopus 로고
    • A role for the Tip60 histone acetyltransferase in the acetylation and activation of ATM
    • Sun Y, Jiang X, Chen S, Fernandes N, Price BD. 2005. A role for the Tip60 histone acetyltransferase in the acetylation and activation of ATM. Proc. Natl. Acad. Sci. U. S. A. 102:13182-13187.
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 13182-13187
    • Sun, Y.1    Jiang, X.2    Chen, S.3    Fernandes, N.4    Price, B.D.5
  • 66
    • 70449518412 scopus 로고    scopus 로고
    • Histone H3 methylation links DNA damage detection to activation of the tumour suppressor Tip60
    • Sun Y, et al. 2009. Histone H3 methylation links DNA damage detection to activation of the tumour suppressor Tip60. Nat. Cell Biol. 11:1376- 1382.
    • (2009) Nat. Cell Biol. , vol.11 , pp. 1376-1382
    • Sun, Y.1
  • 67
    • 33845656738 scopus 로고    scopus 로고
    • Acetylation of the p53 DNA-binding domain regulates apoptosis induction
    • Sykes SM, et al. 2006. Acetylation of the p53 DNA-binding domain regulates apoptosis induction. Mol. Cell 24:841- 851.
    • (2006) Mol. Cell , vol.24 , pp. 841-851
    • Sykes, S.M.1
  • 68
    • 80052942443 scopus 로고    scopus 로고
    • Identification of 67 histone marks and histone lysine crotonylation as a new type of histone modification
    • Tan M, et al. 2011. Identification of 67 histone marks and histone lysine crotonylation as a new type of histone modification. Cell 146:1016 -1028.
    • (2011) Cell , vol.146 , pp. 1016-1028
    • Tan, M.1
  • 69
    • 33845668241 scopus 로고    scopus 로고
    • Tip60- dependent acetylation of p53 modulates the decision between cell-cycle arrest and apoptosis
    • Tang Y, Luo J, Zhang W, Gu W. 2006. Tip60-dependent acetylation of p53 modulates the decision between cell-cycle arrest and apoptosis. Mol. Cell 24:827- 839.
    • (2006) Mol. Cell , vol.24 , pp. 827-839
    • Tang, Y.1    Luo, J.2    Zhang, W.3    Gu, W.4
  • 70
    • 2942620920 scopus 로고    scopus 로고
    • E2F-dependent histone acetylation and recruitment of the Tip60 acetyltransferase complex to chromatin in late G1
    • Taubert S, et al. 2004. E2F-dependent histone acetylation and recruitment of the Tip60 acetyltransferase complex to chromatin in late G1. Mol. Cell. Biol. 24:4546-4556.
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 4546-4556
    • Taubert, S.1
  • 71
    • 49449109503 scopus 로고    scopus 로고
    • Mof (MYST1 or KAT8) is essential for progression of embryonic development past the blastocyst stage and required for normal chromatin architecture
    • Thomas T, Dixon MP, Kueh AJ, Voss AK. 2008. Mof (MYST1 or KAT8) is essential for progression of embryonic development past the blastocyst stage and required for normal chromatin architecture. Mol. Cell. Biol. 28:5093-5105.
    • (2008) Mol. Cell. Biol. , vol.28 , pp. 5093-5105
    • Thomas, T.1    Dixon, M.P.2    Kueh, A.J.3    Voss, A.K.4
  • 72
    • 80054736119 scopus 로고    scopus 로고
    • Characterization of nuclear sirtuins: molecular mechanisms and physiological relevance
    • Toiber D, Sebastian C, Mostoslavsky R. 2011. Characterization of nuclear sirtuins: molecular mechanisms and physiological relevance. Handb. Exp. Pharmacol. 206:189 -224.
    • (2011) Handb. Exp. Pharmacol. , vol.206 , pp. 189-224
    • Toiber, D.1    Sebastian, C.2    Mostoslavsky, R.3
  • 73
    • 0030964526 scopus 로고    scopus 로고
    • Silencing factors participate in DNA repair and recombination in Saccharomyces cerevisiae
    • Tsukamoto Y, Kato J, Ikeda H. 1997. Silencing factors participate in DNA repair and recombination in Saccharomyces cerevisiae. Nature 388: 900-903.
    • (1997) Nature , vol.388 , pp. 900-903
    • Tsukamoto, Y.1    Kato, J.2    Ikeda, H.3
  • 74
    • 77649225958 scopus 로고    scopus 로고
    • Regulation of Treg functionality by acetylation-mediated Foxp3 protein stabilization
    • van Loosdregt J, et al. 2010. Regulation of Treg functionality by acetylation-mediated Foxp3 protein stabilization. Blood 115:965-974.
    • (2010) Blood , vol.115 , pp. 965-974
    • van Loosdregt, J.1
  • 75
    • 4944245398 scopus 로고    scopus 로고
    • Human SirT1 interacts with histone H1 and promotes formation of facultative heterochromatin
    • Vaquero A, et al. 2004. Human SirT1 interacts with histone H1 and promotes formation of facultative heterochromatin. Mol. Cell 16:93-105.
    • (2004) Mol. Cell , vol.16 , pp. 93-105
    • Vaquero, A.1
  • 76
    • 34547875013 scopus 로고    scopus 로고
    • NADα-dependent deacetylation of H4 lysine 16 by class III HDACs
    • Vaquero A, Sternglanz R, Reinberg D. 2007. NADα-dependent deacetylation of H4 lysine 16 by class III HDACs. Oncogene 26:5505-5520.
    • (2007) Oncogene , vol.26 , pp. 5505-5520
    • Vaquero, A.1    Sternglanz, R.2    Reinberg, D.3
  • 77
    • 0035913903 scopus 로고    scopus 로고
    • hSIR2SIRT1 functions as an NAD-dependent p53 deacetylase
    • Vaziri H, et al. 2001. hSIR2SIRT1 functions as an NAD-dependent p53 deacetylase. Cell 107:149 -159.
    • (2001) Cell , vol.107 , pp. 149-159
    • Vaziri, H.1
  • 78
    • 77951217683 scopus 로고    scopus 로고
    • SIRT1 regulates autoacetylation and histone acetyltransferase activity of TIP60
    • Wang J, Chen J. 2010. SIRT1 regulates autoacetylation and histone acetyltransferase activity of TIP60. J. Biol. Chem. 285:11458 -11464.
    • (2010) J. Biol. Chem. , vol.285 , pp. 11458-11464
    • Wang, J.1    Chen, J.2
  • 79
    • 60749101582 scopus 로고    scopus 로고
    • Stress-inducible regulation of heat shock factor 1 by the deacetylase SIRT1
    • Westerheide SD, Anckar J, Stevens SM, Sistonen L, Morimoto RI. 2009. Stress-inducible regulation of heat shock factor 1 by the deacetylase SIRT1. Science 323:1063-1066.
    • (2009) Science , vol.323 , pp. 1063-1066
    • Westerheide, S.D.1    Anckar, J.2    Stevens, S.M.3    Sistonen, L.4    Morimoto, R.I.5
  • 80
    • 79959864524 scopus 로고    scopus 로고
    • The RING finger protein MSL2 in the MOF complex is an E3 ubiquitin ligase for H2B K34 and is involved in crosstalk with H3 K4 and K79 methylation
    • Wu L, Zee BM, Wang Y, Garcia BA, Dou Y. 2011. The RING finger protein MSL2 in the MOF complex is an E3 ubiquitin ligase for H2B K34 and is involved in crosstalk with H3 K4 and K79 methylation. Mol. Cell 43:132-144.
    • (2011) Mol. Cell , vol.43 , pp. 132-144
    • Wu, L.1    Zee, B.M.2    Wang, Y.3    Garcia, B.A.4    Dou, Y.5
  • 81
    • 70450233493 scopus 로고    scopus 로고
    • Sirt1 physically interacts with Tip60 and negatively regulates Tip60-mediated acetylation of H2AX
    • Yamagata K, Kitabayashi I. 2009. Sirt1 physically interacts with Tip60 and negatively regulates Tip60-mediated acetylation of H2AX. Biochem. Biophys. Res. Commun. 390:1355-1360.
    • (2009) Biochem. Biophys. Res. Commun. , vol.390 , pp. 1355-1360
    • Yamagata, K.1    Kitabayashi, I.2
  • 82
    • 0037304718 scopus 로고    scopus 로고
    • Interaction of histone acetylases and deacetylases in vivo
    • Yamagoe S, et al. 2003. Interaction of histone acetylases and deacetylases in vivo. Mol. Cell. Biol. 23:1025-1033.
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 1025-1033
    • Yamagoe, S.1
  • 83
    • 2342599619 scopus 로고    scopus 로고
    • The diverse superfamily of lysine acetyltransferases and their roles in leukemia and other diseases
    • Yang XJ. 2004. The diverse superfamily of lysine acetyltransferases and their roles in leukemia and other diseases. Nucleic Acids Res. 32:959 -976.
    • (2004) Nucleic Acids Res , vol.32 , pp. 959-976
    • Yang, X.J.1
  • 84
    • 3242719545 scopus 로고    scopus 로고
    • Modulation of NF-αB-dependent transcription and cell survival by the SIRT1 deacetylase
    • Yeung F, et al. 2004. Modulation of NF-αB-dependent transcription and cell survival by the SIRT1 deacetylase. EMBO J. 23:2369 -2380.
    • (2004) EMBO J , vol.23 , pp. 2369-2380
    • Yeung, F.1
  • 85
    • 61749095297 scopus 로고    scopus 로고
    • SIRT1 exerts anti-inflammatory effects and improves insulin sensitivity in adipocytes
    • Yoshizaki T, et al. 2009. SIRT1 exerts anti-inflammatory effects and improves insulin sensitivity in adipocytes. Mol. Cell. Biol. 29:1363-1374.
    • (2009) Mol. Cell. Biol. , vol.29 , pp. 1363-1374
    • Yoshizaki, T.1
  • 86
    • 77952876986 scopus 로고    scopus 로고
    • Protein deacetylation by SIRT1: an emerging key post-translational modification in metabolic regulation
    • Yu J, Auwerx J. 2010. Protein deacetylation by SIRT1: an emerging key post-translational modification in metabolic regulation. Pharmacol. Res. 62:35- 41.
    • (2010) Pharmacol. Res. , vol.62 , pp. 35-41
    • Yu, J.1    Auwerx, J.2
  • 87
    • 84855341934 scopus 로고    scopus 로고
    • MYST protein acetyltransferase activity requires active site lysine autoacetylation
    • Yuan H, et al. 2012. MYST protein acetyltransferase activity requires active site lysine autoacetylation. EMBO J. 31:58 -70.
    • (2012) EMBO J , vol.31 , pp. 58-70
    • Yuan, H.1
  • 88
    • 34250897968 scopus 로고    scopus 로고
    • SIRT1 regulates the function of the Nijmegen breakage syndrome protein
    • Yuan Z, Zhang X, Sengupta N, Lane WS, Seto E. 2007. SIRT1 regulates the function of the Nijmegen breakage syndrome protein. Mol. Cell 27: 149-162.
    • (2007) Mol. Cell , vol.27 , pp. 149-162
    • Yuan, Z.1    Zhang, X.2    Sengupta, N.3    Lane, W.S.4    Seto, E.5
  • 89
    • 70349440053 scopus 로고    scopus 로고
    • The type III histone deacetylase Sirt1 is essential for maintenance of T cell tolerance in mice
    • Zhang J, et al. 2009. The type III histone deacetylase Sirt1 is essential for maintenance of T cell tolerance in mice. J. Clin. Invest. 119:3048 -3058.
    • (2009) J. Clin. Invest. , vol.119 , pp. 3048-3058
    • Zhang, J.1
  • 90
    • 34447315270 scopus 로고    scopus 로고
    • HDAC6 modulates cell motility by altering the acetylation level of cortactin
    • Zhang X, et al. 2007. HDAC6 modulates cell motility by altering the acetylation level of cortactin. Mol. Cell 27:197-213.
    • (2007) Mol. Cell , vol.27 , pp. 197-213
    • Zhang, X.1


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