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Volumn 31, Issue 23, 2011, Pages 4720-4734

SIRT1 deacetylates the DNA methyltransferase 1 (DNMT1) protein and alters its activities

Author keywords

[No Author keywords available]

Indexed keywords

DNA METHYLTRANSFERASE 1; LYSINE; SIRTUIN 1;

EID: 83255186739     PISSN: 02707306     EISSN: 10985549     Source Type: Journal    
DOI: 10.1128/MCB.06147-11     Document Type: Article
Times cited : (170)

References (81)
  • 2
    • 0346969980 scopus 로고    scopus 로고
    • Dendrite development regulated by CREST, a calcium-regulated transcriptional activator
    • Aizawa, H., et al. 2004. Dendrite development regulated by CREST, a calcium-regulated transcriptional activator. Science 303:197-202.
    • (2004) Science , vol.303 , pp. 197-202
    • Aizawa, H.1
  • 3
    • 0035444277 scopus 로고    scopus 로고
    • Enzymatic properties of de novo-type mouse DNA (cytosine-5) methyltransferases
    • Aoki, A., et al. 2001. Enzymatic properties of de novo-type mouse DNA (cytosine-5) methyltransferases. Nucleic Acids Res. 29:3506-3512.
    • (2001) Nucleic Acids Res. , vol.29 , pp. 3506-3512
    • Aoki, A.1
  • 4
    • 0028786951 scopus 로고
    • Loss of methylation activates Xist in somatic but not in embryonic cells
    • Beard, C., E. Li, and R. Jaenisch. 1995. Loss of methylation activates Xist in somatic but not in embryonic cells. Genes Dev. 9:2325-2334.
    • (1995) Genes Dev. , vol.9 , pp. 2325-2334
    • Beard, C.1    Li, E.2    Jaenisch, R.3
  • 5
    • 0031964055 scopus 로고    scopus 로고
    • Inhibition of DNA methylation by 5-aza-2'-deoxycytidine suppresses the growth of human tumor cell lines
    • Bender, C. M., M. M. Pao, and P. A. Jones. 1998. Inhibition of DNA methylation by 5-aza-2'-deoxycytidine suppresses the growth of human tumor cell lines. Cancer Res. 58:95-101.
    • (1998) Cancer Res. , vol.58 , pp. 95-101
    • Bender, C.M.1    Pao, M.M.2    Jones, P.A.3
  • 6
    • 0023701018 scopus 로고
    • Cloning and sequencing of a cDNA encoding DNA methyltransferase of mouse cells. The carboxyl-terminal domain of the mammalian enzymes is related to bacterial restriction methyltransferases
    • Bestor, T., A. Laudano, R. Mattaliano, and V. Ingram. 1988. Cloning and sequencing of a cDNA encoding DNA methyltransferase of mouse cells. The carboxyl-terminal domain of the mammalian enzymes is related to bacterial restriction methyltransferases. J. Mol. Biol. 203:971-983.
    • (1988) J. Mol. Biol. , vol.203 , pp. 971-983
    • Bestor, T.1    Laudano, A.2    Mattaliano, R.3    Ingram, V.4
  • 7
    • 0026697174 scopus 로고
    • Activation of mammalian DNA methyltransferase by cleavage of a Zn binding regulatory domain
    • Bestor, T. H. 1992. Activation of mammalian DNA methyltransferase by cleavage of a Zn binding regulatory domain. EMBO J. 11:2611-2617.
    • (1992) EMBO J. , vol.11 , pp. 2611-2617
    • Bestor, T.H.1
  • 8
    • 0033753779 scopus 로고    scopus 로고
    • The DNA methyltransferases of mammals
    • Bestor, T. H. 2000. The DNA methyltransferases of mammals. Hum. Mol. Genet. 9:2395-2402.
    • (2000) Hum. Mol. Genet. , vol.9 , pp. 2395-2402
    • Bestor, T.H.1
  • 9
    • 0036144048 scopus 로고    scopus 로고
    • DNA methylation patterns and epigenetic memory
    • Bird, A. 2002. DNA methylation patterns and epigenetic memory. Genes Dev. 16:6-21.
    • (2002) Genes Dev. , vol.16 , pp. 6-21
    • Bird, A.1
  • 10
    • 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
  • 11
    • 0032948005 scopus 로고    scopus 로고
    • Synergy of demethylation and histone deacetylase inhibition in the re-expression of genes silenced in cancer
    • Cameron, E. E., K. E. Bachman, S. Myohanen, J. G. Herman, and S. B. Baylin. 1999. Synergy of demethylation and histone deacetylase inhibition in the re-expression of genes silenced in cancer. Nat. Genet. 21:103-107.
    • (1999) Nat. Genet. , vol.21 , pp. 103-107
    • Cameron, E.E.1    Bachman, K.E.2    Myohanen, S.3    Herman, J.G.4    Baylin, S.B.5
  • 12
    • 33847293264 scopus 로고    scopus 로고
    • Complete inactivation of DNMT1 leads to mitotic catastrophe in human cancer cells
    • Chen, T., et al. 2007. Complete inactivation of DNMT1 leads to mitotic catastrophe in human cancer cells. Nat. Genet. 39:391-396.
    • (2007) Nat. Genet. , vol.39 , pp. 391-396
    • Chen, T.1
  • 13
    • 29644440388 scopus 로고    scopus 로고
    • Establishment and maintenance of DNA methylation patterns in mammals
    • Chen, T., and E. Li. 2006. Establishment and maintenance of DNA methylation patterns in mammals. Curr. Top. Microbiol. Immunol. 301:179-201.
    • (2006) Curr. Top. Microbiol. Immunol. , vol.301 , pp. 179-201
    • Chen, T.1    Li, E.2
  • 14
    • 68949212379 scopus 로고    scopus 로고
    • Lysine acetylation targets protein complexes and co-regulates major cellular functions
    • Choudhary, C., et al. 2009. Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science 325:834-840.
    • (2009) Science , vol.325 , pp. 834-840
    • Choudhary, C.1
  • 15
    • 34347334590 scopus 로고    scopus 로고
    • Biological functions of DNA methyltransferase 1 requires its methyltransferase activity
    • Damelin, M., and T. H. Bestor. 2007. Biological functions of DNA methyltransferase 1 requires its methyltransferase activity. Mol. Cell. Biol. 27:3891-3899.
    • (2007) Mol. Cell. Biol. , vol.27 , pp. 3891-3899
    • Damelin, M.1    Bestor, T.H.2
  • 16
    • 79953178935 scopus 로고    scopus 로고
    • Alpha-synuclein sequesters Dnmt1 from the nucleus: a novel mechanism for epigenetic alterations in Lewy body diseases
    • Desplats, P., et al. 2011. Alpha-synuclein sequesters Dnmt1 from the nucleus: a novel mechanism for epigenetic alterations in Lewy body diseases. J. Biol. Chem. 286:9031-9037.
    • (2011) J. Biol. Chem. , vol.286 , pp. 9031-9037
    • Desplats, P.1
  • 17
    • 78049510229 scopus 로고    scopus 로고
    • DNMT1 stability is regulated by proteins coordinating deubiquitination and acetylation-driven ubiquitination
    • Du, Z., et al. 2010. DNMT1 stability is regulated by proteins coordinating deubiquitination and acetylation-driven ubiquitination. Sci. Signal. 3:ra80.
    • (2010) Sci. Signal. , vol.3
    • Du, Z.1
  • 18
    • 0033563083 scopus 로고    scopus 로고
    • CpG island hypermethylation in human colorectal tumors is not associated with DNA methyltransferase overexpression
    • Eads, C. A., et al. 1999. CpG island hypermethylation in human colorectal tumors is not associated with DNA methyltransferase overexpression. Cancer Res. 59:2302-2306.
    • (1999) Cancer Res. , vol.59 , pp. 2302-2306
    • Eads, C.A.1
  • 19
    • 33748998743 scopus 로고    scopus 로고
    • Identification of DNMT1 (DNA methyltransferase 1) hypomorphs in somatic knockouts suggests an essential role for DNMT1 in cell survival
    • Egger, G., et al. 2006. Identification of DNMT1 (DNA methyltransferase 1) hypomorphs in somatic knockouts suggests an essential role for DNMT1 in cell survival. Proc. Natl. Acad. Sci. U. S. A. 103:14080-14085.
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 14080-14085
    • Egger, G.1
  • 20
    • 34249681648 scopus 로고    scopus 로고
    • Epigenetic disruption of ribosomal RNA genes and nucleolar architecture in DNA methyltransferase 1 (Dnmt1) deficient cells
    • Espada, J., et al. 2007. Epigenetic disruption of ribosomal RNA genes and nucleolar architecture in DNA methyltransferase 1 (Dnmt1) deficient cells. Nucleic Acids Res. 35:2191-2198.
    • (2007) Nucleic Acids Res. , vol.35 , pp. 2191-2198
    • Espada, J.1
  • 21
    • 65249102251 scopus 로고    scopus 로고
    • Regulation of DNMT1 stability through SET7- mediated lysine methylation in mammalian cells
    • Esteve, P. O., et al. 2009. Regulation of DNMT1 stability through SET7- mediated lysine methylation in mammalian cells. Proc. Natl. Acad. Sci. U. S. A. 106:5076-5081.
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 5076-5081
    • Esteve, P.O.1
  • 22
    • 44749085668 scopus 로고    scopus 로고
    • ER alpha negative breast cancer cells restore response to endocrine therapy by combination treatment with both HDAC inhibitor and DNMT inhibitor
    • Fan, J., et al. 2008. ER alpha negative breast cancer cells restore response to endocrine therapy by combination treatment with both HDAC inhibitor and DNMT inhibitor. J. Cancer Res. Clin. Oncol. 134:883-890.
    • (2008) J. Cancer Res. Clin. Oncol. , vol.134 , pp. 883-890
    • Fan, J.1
  • 23
    • 0030006949 scopus 로고    scopus 로고
    • 5 methyltransferase: pre-steady and steady-state kinetic analysis with regulatory DNA sequences
    • 5 methyltransferase: pre-steady and steady-state kinetic analysis with regulatory DNA sequences. Biochemistry 35:7308-7315.
    • (1996) Biochemistry , vol.35 , pp. 7308-7315
    • Flynn, J.1    Glickman, J.F.2    Reich, N.O.3
  • 24
    • 0032573129 scopus 로고    scopus 로고
    • Murine DNA (cytosine-5-)-methyltransferase: steady-state and substrate trapping analyses of the kinetic mechanism
    • Flynn, J., and N. Reich. 1998. Murine DNA (cytosine-5-)-methyltransferase: steady-state and substrate trapping analyses of the kinetic mechanism. Biochemistry 37:15162-15169.
    • (1998) Biochemistry , vol.37 , pp. 15162-15169
    • Flynn, J.1    Reich, N.2
  • 25
    • 0033988813 scopus 로고    scopus 로고
    • DNA methyltransferase Dnmt1 associates with histone deacetylase activity
    • Fuks, F., W. A. Burgers, A. Brehm, L. Hughes-Davies, and T. Kouzarides. 2000. DNA methyltransferase Dnmt1 associates with histone deacetylase activity. Nat. Genet. 24:88-91.
    • (2000) Nat. Genet. , vol.24 , pp. 88-91
    • Fuks, F.1    Burgers, W.A.2    Brehm, A.3    Hughes-Davies, L.4    Kouzarides, T.5
  • 26
    • 28044471827 scopus 로고    scopus 로고
    • Acetylation and deacetylation of non-histone proteins
    • Glozak, M. A., N. Sengupta, X. Zhang, and E. Seto. 2005. Acetylation and deacetylation of non-histone proteins. Gene 363:15-23.
    • (2005) Gene , vol.363 , pp. 15-23
    • Glozak, M.A.1    Sengupta, N.2    Zhang, X.3    Seto, E.4
  • 27
    • 0028849277 scopus 로고
    • E-cadherin expression is silenced by DNA hyper-methylation in human breast and prostate carcinomas
    • Graff, J. R., et al. 1995. E-cadherin expression is silenced by DNA hyper-methylation in human breast and prostate carcinomas. Cancer Res. 55:5195-5199.
    • (1995) Cancer Res. , vol.55 , pp. 5195-5199
    • Graff, J.R.1
  • 28
    • 33751113602 scopus 로고    scopus 로고
    • Mammalian sirtuins-emerging roles in physiology, aging, and calorie restriction
    • Haigis, M. C., and L. P. Guarente. 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
  • 29
    • 9744251005 scopus 로고    scopus 로고
    • Biochemistry and biology of mammalian DNA methyltransferases
    • Hermann, A., H. Gowher, and A. Jeltsch. 2004. Biochemistry and biology of mammalian DNA methyltransferases. Cell. Mol. Life Sci. 61:2571-2587.
    • (2004) Cell. Mol. Life Sci. , vol.61 , pp. 2571-2587
    • Hermann, A.1    Gowher, H.2    Jeltsch, A.3
  • 30
    • 0027198976 scopus 로고
    • Increased cytosine DNA-methyltransferase activity during colon cancer progression
    • Issa, J. P., et al. 1993. Increased cytosine DNA-methyltransferase activity during colon cancer progression. J. Natl. Cancer Inst. 85:1235-1240.
    • (1993) J. Natl. Cancer Inst. , vol.85 , pp. 1235-1240
    • Issa, J.P.1
  • 31
    • 0035158704 scopus 로고    scopus 로고
    • Loss of genomic methylation causes p53- dependent apoptosis and epigenetic deregulation
    • Jackson-Grusby, L., et al. 2001. Loss of genomic methylation causes p53- dependent apoptosis and epigenetic deregulation. Nat. Genet. 27:31-39.
    • (2001) Nat. Genet. , vol.27 , pp. 31-39
    • Jackson-Grusby, L.1
  • 32
    • 67649624689 scopus 로고    scopus 로고
    • Cytoplasmic localization of oocyte-specific variant of porcine DNA methyltransferase-1 during early development
    • Jeong, Y. S., K. B. Oh, J. S. Park, J.-S. Kim, and Y.-K. Kang. 2009. Cytoplasmic localization of oocyte-specific variant of porcine DNA methyltransferase-1 during early development. Dev. Dyn. 238:1666-1673.
    • (2009) Dev. Dyn. , vol.238 , pp. 1666-1673
    • Jeong, Y.S.1    Oh, K.B.2    Park, J.S.3    Kim, J.-S.4    Kang, Y.-K.5
  • 33
    • 0036274359 scopus 로고    scopus 로고
    • The fundamental role of epigenetic events in cancer
    • Jones, P. A., and S. B. Baylin. 2002. The fundamental role of epigenetic events in cancer. Nat. Rev. Genet. 3:415-428.
    • (2002) Nat. Rev. Genet. , vol.3 , pp. 415-428
    • Jones, P.A.1    Baylin, S.B.2
  • 34
    • 0035839057 scopus 로고    scopus 로고
    • The role of DNA methylation in mammalian epigenetics
    • Jones, P. A., and D. Takai. 2001. The role of DNA methylation in mammalian epigenetics. Science 293:1068-1070.
    • (2001) Science , vol.293 , pp. 1068-1070
    • Jones, P.A.1    Takai, D.2
  • 35
    • 0033214237 scopus 로고    scopus 로고
    • The SIR2/3/4 complex and SIR2 alone promote longevity in Saccharomyces cerevisiae by two different mechanisms
    • Kaeberlein, M., M. McVey, and L. Guarente. 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
  • 36
    • 0022971594 scopus 로고
    • DNA methyltransferase levels in tumorigenic and nontumorigenic cells in culture
    • Kautiainen, T. L., and P. A. Jones. 1986. DNA methyltransferase levels in tumorigenic and nontumorigenic cells in culture. J. Biol. Chem. 261:1594-1598.
    • (1986) J. Biol. Chem. , vol.261 , pp. 1594-1598
    • Kautiainen, T.L.1    Jones, P.A.2
  • 37
    • 33746992118 scopus 로고    scopus 로고
    • Substrate and functional diversity of lysine acetylation revealed by a proteomics survey
    • Kim, S. C., et al. 2006. Substrate and functional diversity of lysine acetylation revealed by a proteomics survey. Mol. Cell 23:607-618.
    • (2006) Mol. Cell , vol.23 , pp. 607-618
    • Kim, S.C.1
  • 38
    • 0038136913 scopus 로고    scopus 로고
    • Methyl-CpG-binding protein, MeCP2, is a target molecule for maintenance DNA methyltransferase, Dnmt1
    • Kimura, H., and K. Shiota. 2003. Methyl-CpG-binding protein, MeCP2, is a target molecule for maintenance DNA methyltransferase, Dnmt1. J. Biol. Chem. 278:4806-4812.
    • (2003) J. Biol. Chem. , vol.278 , pp. 4806-4812
    • Kimura, H.1    Shiota, K.2
  • 39
    • 0034654011 scopus 로고    scopus 로고
    • Acetylation: a regulatory modification to rival phosphorylation?
    • Kouzarides, T. 2000. Acetylation: a regulatory modification to rival phosphorylation? EMBO J. 19:1176-1179.
    • (2000) EMBO J , vol.19 , pp. 1176-1179
    • Kouzarides, T.1
  • 40
    • 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
  • 41
    • 69249241855 scopus 로고    scopus 로고
    • SUMOylation enhances DNA methyltransferase 1 activity
    • Lee, B., and M. T. Muller. 2009. SUMOylation enhances DNA methyltransferase 1 activity. Biochem. J. 421:449-461.
    • (2009) Biochem. J. , vol.421 , pp. 449-461
    • Lee, B.1    Muller, M.T.2
  • 42
    • 0027342752 scopus 로고
    • Structure, function and regulation of mammalian DNA methyltransferase
    • Leonhardt, H., and T. H. Bestor. 1993. Structure, function and regulation of mammalian DNA methyltransferase. EXS 64:109-119.
    • (1993) EXS , vol.64 , pp. 109-119
    • Leonhardt, H.1    Bestor, T.H.2
  • 43
    • 0034446542 scopus 로고    scopus 로고
    • DNA methylation, nuclear structure, gene expression and cancer
    • Leonhardt, H., and M. C. Cardoso. 2000. DNA methylation, nuclear structure, gene expression and cancer. J. Cell. Biochem. Suppl. 35:78-83.
    • (2000) J. Cell. Biochem. Suppl. , vol.35 , pp. 78-83
    • Leonhardt, H.1    Cardoso, M.C.2
  • 44
    • 0026439115 scopus 로고
    • A targeting sequence directs DNA methyltransferase to sites of DNA replication in mammalian nuclei
    • Leonhardt, H., A. W. Page, H. U. Weier, and T. H. Bestor. 1992. A targeting sequence directs DNA methyltransferase to sites of DNA replication in mammalian nuclei. Cell 71:865-873.
    • (1992) Cell , vol.71 , pp. 865-873
    • Leonhardt, H.1    Page, A.W.2    Weier, H.U.3    Bestor, T.H.4
  • 45
    • 0025806910 scopus 로고
    • DNA methylation and chromatin structure
    • Lewis, J., and A. Bird. 1991. DNA methylation and chromatin structure. FEBS Lett. 285:155-159.
    • (1991) FEBS Lett. , vol.285 , pp. 155-159
    • Lewis, J.1    Bird, A.2
  • 46
    • 0027378582 scopus 로고
    • Role for DNA methylation in genomic imprinting
    • Li, E., C. Beard, and R. Jaenisch. 1993. Role for DNA methylation in genomic imprinting. Nature 366:362-365.
    • (1993) Nature , vol.366 , pp. 362-365
    • Li, E.1    Beard, C.2    Jaenisch, R.3
  • 47
    • 0026708177 scopus 로고
    • Targeted mutation of the DNA methyltransferase gene results in embryonic lethality
    • Li, E., T. H. Bestor, and R. Jaenisch. 1992. Targeted mutation of the DNA methyltransferase gene results in embryonic lethality. Cell 69:915-926.
    • (1992) Cell , vol.69 , pp. 915-926
    • Li, E.1    Bestor, T.H.2    Jaenisch, R.3
  • 48
    • 74549153191 scopus 로고    scopus 로고
    • Localization of DNA methyltransferase-1 during oocyte differentiation, in vitro maturation and early embryonic development in cow
    • Lodde, V., et al. 2009. Localization of DNA methyltransferase-1 during oocyte differentiation, in vitro maturation and early embryonic development in cow. Eur. J. Histochem. 53:199-207.
    • (2009) Eur. J. Histochem. , vol.53 , pp. 199-207
    • Lodde, V.1
  • 49
    • 67349195506 scopus 로고    scopus 로고
    • Traumatic brain injury induces relocalization of DNA-methyltransferase 1
    • Lundberg, J., et al. 2009. Traumatic brain injury induces relocalization of DNA-methyltransferase 1. Neurosci. Lett. 457:8-11.
    • (2009) Neurosci. Lett. , vol.457 , pp. 8-11
    • Lundberg, J.1
  • 50
    • 0038304456 scopus 로고    scopus 로고
    • pRb2/p130-E2F4/5-HDAC1-SUV39H1-p300 and pRb2/p130-E2F4/5-HDAC1- SUV39H1-DNMT1 multimolecular complexes mediate the transcription of estrogen receptor-alpha in breast cancer
    • Macaluso, M., C. Cinti, G. Russo, A. Russo, and A. Giordano. 2003. pRb2/p130-E2F4/5-HDAC1-SUV39H1-p300 and pRb2/p130-E2F4/5-HDAC1- SUV39H1-DNMT1 multimolecular complexes mediate the transcription of estrogen receptor-alpha in breast cancer. Oncogene 22:3511-3517.
    • (2003) Oncogene , vol.22 , pp. 3511-3517
    • Macaluso, M.1    Cinti, C.2    Russo, G.3    Russo, A.4    Giordano, A.5
  • 51
    • 26244436281 scopus 로고    scopus 로고
    • Evolutionarily conserved and nonconserved cellular localizations and functions of human SIRT proteins
    • Michishita, E., J. Y. Park, J. M. Burneskis, J. C. Barrett, and I. Horikawa. 2005. Evolutionarily conserved and nonconserved cellular localizations and functions of human SIRT proteins. Mol. Biol. Cell 16:4623-4635.
    • (2005) Mol. Biol. Cell , vol.16 , pp. 4623-4635
    • Michishita, E.1    Park, J.Y.2    Burneskis, J.M.3    Barrett, J.C.4    Horikawa, I.5
  • 52
    • 0034054673 scopus 로고    scopus 로고
    • DNA methyltransferase inhibition induces the transcription of the tumor suppressor p21(WAF1/ CIP1/sdi1)
    • Milutinovic, S., J. D. Knox, and M. Szyf. 2000. DNA methyltransferase inhibition induces the transcription of the tumor suppressor p21(WAF1/CIP1/sdi1). J. Biol. Chem. 275:6353-6359.
    • (2000) J. Biol. Chem. , vol.275 , pp. 6353-6359
    • Milutinovic, S.1    Knox, J.D.2    Szyf, M.3
  • 53
    • 0032574977 scopus 로고    scopus 로고
    • Transcriptional repression by the methyl-CpG-binding protein MeCP2 involves a histone deacetylase complex
    • Nan, X., et al. 1998. Transcriptional repression by the methyl-CpG-binding protein MeCP2 involves a histone deacetylase complex. Nature 393:386-389.
    • (1998) Nature , vol.393 , pp. 386-389
    • Nan, X.1
  • 54
    • 0037291214 scopus 로고    scopus 로고
    • The human Sir2 ortholog, SIRT2, is an NAD+-dependent tubulin deacetylase
    • North, B. J., B. L. Marshall, M. T. Borra, J. M. Denu, and E. Verdin. 2003. The human Sir2 ortholog, SIRT2, is an NAD+-dependent tubulin deacetylase. Mol. Cell 11:437-444.
    • (2003) Mol. Cell , vol.11 , pp. 437-444
    • North, B.J.1    Marshall, B.L.2    Borra, M.T.3    Denu, J.M.4    Verdin, E.5
  • 55
    • 0028318783 scopus 로고
    • Methylation of the estrogen receptor gene CpG island marks loss of estrogen receptor expression in human breast cancer cells
    • Ottaviano, Y. L., et al. 1994. Methylation of the estrogen receptor gene CpG island marks loss of estrogen receptor expression in human breast cancer cells. Cancer Res. 54:2552-2555.
    • (1994) Cancer Res. , vol.54 , pp. 2552-2555
    • Ottaviano, Y.L.1
  • 56
    • 33645768490 scopus 로고    scopus 로고
    • Inhibition of SIRT1 reactivates silenced cancer genes without loss of promoter DNA hypermethylation
    • Pruitt, K., et al. 2006. Inhibition of SIRT1 reactivates silenced cancer genes without loss of promoter DNA hypermethylation. PLoS Genet. 2:e40.
    • (2006) PLoS Genet. , vol.2
    • Pruitt, K.1
  • 57
    • 0034720284 scopus 로고    scopus 로고
    • CpG methylation is maintained in human cancer cells lacking DNMT1
    • Rhee, I., et al. 2000. CpG methylation is maintained in human cancer cells lacking DNMT1. Nature 404:1003-1007.
    • (2000) Nature , vol.404 , pp. 1003-1007
    • Rhee, I.1
  • 58
    • 0033919595 scopus 로고    scopus 로고
    • DNMT1 forms a complex with Rb, E2F1 and HDAC1 and represses transcription from E2F-responsive promoters
    • Robertson, K. D., et al. 2000. DNMT1 forms a complex with Rb, E2F1 and HDAC1 and represses transcription from E2F-responsive promoters. Nat. Genet. 25:338-342.
    • (2000) Nat. Genet. , vol.25 , pp. 338-342
    • Robertson, K.D.1
  • 59
    • 0033945861 scopus 로고    scopus 로고
    • DNMT1 binds HDAC2 and a new co-repressor, DMAP1, to form a complex at replication foci
    • Rountree, M. R., K. E. Bachman, and S. B. Baylin. 2000. DNMT1 binds HDAC2 and a new co-repressor, DMAP1, to form a complex at replication foci. Nat. Genet. 25:269-277.
    • (2000) Nat. Genet. , vol.25 , pp. 269-277
    • Rountree, M.R.1    Bachman, K.E.2    Baylin, S.B.3
  • 60
    • 0037130479 scopus 로고    scopus 로고
    • The expression of DNA methyltransferases and methyl- CpG-binding proteins is not associated with the methylation status of p14(ARF), p16(INK4a) and RASSF1A in human lung cancer cell lines
    • Sato, M., et al. 2002. The expression of DNA methyltransferases and methyl- CpG-binding proteins is not associated with the methylation status of p14(ARF), p16(INK4a) and RASSF1A in human lung cancer cell lines. Oncogene 21:4822-4829.
    • (2002) Oncogene , vol.21 , pp. 4822-4829
    • Sato, M.1
  • 61
    • 34547875773 scopus 로고    scopus 로고
    • Sirtuins: critical regulators at the crossroads between cancer and aging
    • Saunders, L. R., and E. Verdin. 2007. Sirtuins: critical regulators at the crossroads between cancer and aging. Oncogene 26:5489-5504.
    • (2007) Oncogene , vol.26 , pp. 5489-5504
    • Saunders, L.R.1    Verdin, E.2
  • 62
    • 33847348016 scopus 로고    scopus 로고
    • DNMT1 but not its interaction with the replication machinery is required for maintenance of DNA methylation in human cells
    • Spada, F., et al. 2007. DNMT1 but not its interaction with the replication machinery is required for maintenance of DNA methylation in human cells. J. Cell Biol. 176:565-571.
    • (2007) J. Cell Biol. , vol.176 , pp. 565-571
    • Spada, F.1
  • 63
    • 77951244142 scopus 로고    scopus 로고
    • The DNA-binding activity of mouse DNA methyltransferase 1 is regulated by phosphorylation with casein kinase 1delta/epsilon
    • Sugiyama, Y., et al. 2010. The DNA-binding activity of mouse DNA methyltransferase 1 is regulated by phosphorylation with casein kinase 1delta/epsilon. Biochem. J. 427:489-497.
    • (2010) Biochem. J. , vol.427 , pp. 489-497
    • Sugiyama, Y.1
  • 64
    • 0025266610 scopus 로고
    • Alternative chromatin structure at CpG islands
    • Tazi, J., and A. Bird. 1990. Alternative chromatin structure at CpG islands. Cell 60:909-920.
    • (1990) Cell , vol.60 , pp. 909-920
    • Tazi, J.1    Bird, A.2
  • 65
    • 2642574054 scopus 로고    scopus 로고
    • CpG island hypermethylation is maintained in human colorectal cancer cells after RNAi-mediated depletion of DNMT1
    • Ting, A. H., et al. 2004. CpG island hypermethylation is maintained in human colorectal cancer cells after RNAi-mediated depletion of DNMT1. Nat. Genet. 36:582-584.
    • (2004) Nat. Genet. , vol.36 , pp. 582-584
    • Ting, A.H.1
  • 66
    • 0029935327 scopus 로고    scopus 로고
    • Germ-line passage is required for establishment of methylation and expression patterns of imprinted but not of nonimprinted genes
    • Tucker, K. L., et al. 1996. Germ-line passage is required for establishment of methylation and expression patterns of imprinted but not of nonimprinted genes. Genes Dev. 10:1008-1020.
    • (1996) Genes Dev. , vol.10 , pp. 1008-1020
    • Tucker, K.L.1
  • 67
    • 31544456085 scopus 로고    scopus 로고
    • The role of mammalian DNA methyltransferases in the regulation of gene expression
    • Turek-Plewa, J., and P. P. Jagodzinski. 2005. The role of mammalian DNA methyltransferases in the regulation of gene expression. Cell. Mol. Biol. Lett. 10:631-647.
    • (2005) Cell. Mol. Biol. Lett. , vol.10 , pp. 631-647
    • Turek-Plewa, J.1    Jagodzinski, P.P.2
  • 68
    • 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
  • 69
    • 0035913903 scopus 로고    scopus 로고
    • hSIR2 (SIRT1) functions as an NAD-dependent p53 deacetylase
    • Vaziri, H., et al. 2001. hSIR2 (SIRT1) functions as an NAD-dependent p53 deacetylase. Cell 107:149-159.
    • (2001) Cell , vol.107 , pp. 149-159
    • Vaziri, H.1
  • 70
    • 33748200050 scopus 로고    scopus 로고
    • Interactions between E2F1 and SirT1 regulate apoptotic response to DNA damage
    • Wang, C., et al. 2006. Interactions between E2F1 and SirT1 regulate apoptotic response to DNA damage. Nat. Cell Biol. 8:1025-1031.
    • (2006) Nat. Cell Biol. , vol.8 , pp. 1025-1031
    • Wang, C.1
  • 71
    • 47549090640 scopus 로고    scopus 로고
    • Estrogen receptor alpha, BRCA1, and FANCF promoter methylation occur in distinct subsets of sporadic breast cancers
    • Wei, M., et al. 2008. Estrogen receptor alpha, BRCA1, and FANCF promoter methylation occur in distinct subsets of sporadic breast cancers. Breast Cancer Res. Treat. 111:113-120.
    • (2008) Breast Cancer Res. Treat. , vol.111 , pp. 113-120
    • Wei, M.1
  • 72
    • 0027504621 scopus 로고
    • Expression of an exogenous eukaryotic DNA methyltransferase gene induces transformation of NIH 3T3 cells
    • Wu, J., et al. 1993. Expression of an exogenous eukaryotic DNA methyltransferase gene induces transformation of NIH 3T3 cells. Proc. Natl. Acad. Sci. U. S. A. 90:8891-8895.
    • (1993) Proc. Natl. Acad. Sci. U. S. A. , vol.90 , pp. 8891-8895
    • Wu, J.1
  • 73
    • 0030834976 scopus 로고    scopus 로고
    • Isolation and characterization of cDNAs corresponding to an additional member of the human histone deacetylase gene family
    • Yang, W. M., Y. L. Yao, J. M. Sun, J. R. Davie, and E. Seto. 1997. Isolation and characterization of cDNAs corresponding to an additional member of the human histone deacetylase gene family. J. Biol. Chem. 272:28001-28007.
    • (1997) J. Biol. Chem. , vol.272 , pp. 28001-28007
    • Yang, W.M.1    Yao, Y.L.2    Sun, J.M.3    Davie, J.R.4    Seto, E.5
  • 74
    • 0034671304 scopus 로고    scopus 로고
    • Transcriptional activation of estrogen receptor alpha in human breast cancer cells by histone deacetylase inhibition
    • Yang, X., et al. 2000. Transcriptional activation of estrogen receptor alpha in human breast cancer cells by histone deacetylase inhibition. Cancer Res. 60:6890-6894.
    • (2000) Cancer Res. , vol.60 , pp. 6890-6894
    • Yang, X.1
  • 75
    • 0035477320 scopus 로고    scopus 로고
    • Synergistic activation of functional estrogen receptor (ER)-alpha by DNA methyltransferase and histone deacetylase inhibition in human ER-alpha-negative breast cancer cells
    • Yang, X., et al. 2001. Synergistic activation of functional estrogen receptor (ER)-alpha by DNA methyltransferase and histone deacetylase inhibition in human ER-alpha-negative breast cancer cells. Cancer Res. 61:7025-7029.
    • (2001) Cancer Res. , vol.61 , pp. 7025-7029
    • Yang, X.1
  • 76
    • 0029665857 scopus 로고    scopus 로고
    • A p300/CBP-associated factor that competes with the adenoviral oncoprotein E1A
    • Yang, X. J., V. V. Ogryzko, J. Nishikawa, B. H. Howard, and Y. Nakatani. 1996. A p300/CBP-associated factor that competes with the adenoviral oncoprotein E1A. Nature 382:319-324.
    • (1996) Nature , vol.382 , pp. 319-324
    • Yang, X.J.1    Ogryzko, V.V.2    Nishikawa, J.3    Howard, B.H.4    Nakatani, Y.5
  • 77
    • 49349107518 scopus 로고    scopus 로고
    • Lysine acetylation: codified crosstalk with other posttranslational modifications
    • Yang, X. J., and E. Seto. 2008. Lysine acetylation: codified crosstalk with other posttranslational modifications. Mol. Cell 31:449-461.
    • (2008) Mol. Cell , vol.31 , pp. 449-461
    • Yang, X.J.1    Seto, E.2
  • 78
    • 39749127166 scopus 로고    scopus 로고
    • The Rpd3/Hda1 family of lysine deacetylases: from bacteria and yeast to mice and men
    • Yang, X. J., and E. Seto. 2008. The Rpd3/Hda1 family of lysine deacetylases: from bacteria and yeast to mice and men. Nat. Rev. Mol. Cell Biol. 9:206-218.
    • (2008) Nat. Rev. Mol. Cell Biol. , vol.9 , pp. 206-218
    • Yang, X.J.1    Seto, E.2
  • 79
    • 0037023761 scopus 로고    scopus 로고
    • Preferential methylation of unmethylated DNA by mammalian de novo DNA methyltransferase Dnmt3a
    • Yokochi, T., and K. D. Robertson. 2002. Preferential methylation of unmethylated DNA by mammalian de novo DNA methyltransferase Dnmt3a. J. Biol. Chem. 277:11735-11745.
    • (2002) J. Biol. Chem. , vol.277 , pp. 11735-11745
    • Yokochi, T.1    Robertson, K.D.2
  • 80
    • 34250897968 scopus 로고    scopus 로고
    • SIRT1 regulates the function of the Nijmegen breakage syndrome protein
    • Yuan, Z., X. Zhang, N. Sengupta, W. S. Lane, and E. Seto. 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
  • 81
    • 51049117752 scopus 로고    scopus 로고
    • Inhibition of histone deacetylases promotes ubiquitin-dependent proteasomal degradation of DNA methyltransferase 1 in human breast cancer cells
    • Zhou, Q., A. T. Agoston, P. Atadja, W. G. Nelson, and N. E. Davidson. 2008. Inhibition of histone deacetylases promotes ubiquitin-dependent proteasomal degradation of DNA methyltransferase 1 in human breast cancer cells. Mol. Cancer Res. 6:873-883.
    • (2008) Mol. Cancer Res. , vol.6 , pp. 873-883
    • Zhou, Q.1    Agoston, A.T.2    Atadja, P.3    Nelson, W.G.4    Davidson, N.E.5


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