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Volumn 32, Issue 3, 2012, Pages 704-716

Correction: A deacetylase-deficient SIRT1 variant opposes full-length SIRT1 in regulating tumor suppressor p53 and governs expression of cancer-related genes[Molecular and Cellular Biology,(2012),(704-716), 32, 3] https://doi.org/10.1128/MCB.06448-11;A deacetylase-deficient SIRT1 variant opposes full-length SIRT1 in regulating tumor suppressor p53 and governs expression of cancer-related genes

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN P53; SIRTUIN 1; TUMOR SUPPRESSOR PROTEIN;

EID: 84856809261     PISSN: 02707306     EISSN: 10985549     Source Type: Journal    
DOI: 10.1128/MCB.00238-17     Document Type: Erratum
Times cited : (26)

References (54)
  • 1
    • 70350233314 scopus 로고    scopus 로고
    • Basal cancer cell survival involves JNK2 suppression of a novel JNK1/c-Jun/Bcl-3 apoptotic network
    • Ahmed SU, Milner J. 2009. Basal cancer cell survival involves JNK2 suppression of a novel JNK1/c-Jun/Bcl-3 apoptotic network. PLoS One 4:e7305.
    • (2009) PLoS One , vol.4
    • Ahmed, S.U.1    Milner, J.2
  • 2
    • 0029162425 scopus 로고
    • Synthesisand secretion of recombinant tick-borne encephalitis virus protein E in soluble and particulate form
    • Allison SL, Stadler K, Mandl CW, Kunz C, Heinz FX. 1995. Synthesisand secretion of recombinant tick-borne encephalitis virus protein E in soluble and particulate form. J. Virol. 69:5816 -5820.
    • (1995) J. Virol. , vol.69 , pp. 5816-5820
    • Allison, S.L.1    Stadler, K.2    Mandl, C.W.3    Kunz, C.4    Heinz, F.X.5
  • 3
    • 47749140333 scopus 로고    scopus 로고
    • SIRT1 regulates circadian clock gene expression through PER2 deacetylation
    • Asher G, et al. 2008. SIRT1 regulates circadian clock gene expression through PER2 deacetylation. Cell 134:317-328.
    • (2008) Cell , vol.134 , pp. 317-328
    • Asher, G.1
  • 4
    • 52749091816 scopus 로고    scopus 로고
    • SirT1 gain of function increases energy efficiency and prevents diabetes in mice
    • Banks AS, et al. 2008. SirT1 gain of function increases energy efficiency and prevents diabetes in mice. Cell Metab. 8:333-341.
    • (2008) Cell Metab , vol.8 , pp. 333-341
    • Banks, A.S.1
  • 5
    • 20444503356 scopus 로고    scopus 로고
    • Formation of a large, complex domain of histone hyperacetylation at human 14q32 1 requires the serpin locus control region
    • Baxter EW, Cummings WJ, Fournier RE. 2005. Formation of a large, complex domain of histone hyperacetylation at human 14q32.1 requires the serpin locus control region. Nucleic Acids Res. 33:3313-3322.
    • (2005) Nucleic Acids Res , vol.33 , pp. 3313-3322
    • Baxter, E.W.1    Cummings, W.J.2    Fournier, R.E.3
  • 6
    • 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
  • 7
    • 0031026001 scopus 로고    scopus 로고
    • Further characterisation of the p53 responsive element: identification of new candidate genes for trans-activation by p53
    • Bourdon JC, et al. 1997. Further characterisation of the p53 responsive element: identification of new candidate genes for trans-activation by p53. Oncogene 14:85-94.
    • (1997) Oncogene , vol.14 , pp. 85-94
    • Bourdon, J.C.1
  • 8
    • 27144475816 scopus 로고    scopus 로고
    • Histone deacetylases in acute myeloid leukaemia show a distinctive pattern of expression that changes selectively in response to deacetylase inhibitors
    • Bradbury CA, et al. 2005. Histone deacetylases in acute myeloid leukaemia show a distinctive pattern of expression that changes selectively in response to deacetylase inhibitors. Leukemia 19:1751-1759.
    • (2005) Leukemia , vol.19 , pp. 1751-1759
    • Bradbury, C.A.1
  • 9
    • 58849158388 scopus 로고    scopus 로고
    • How does SIRT1 affect metabolism, senescence and cancer? Nat
    • Brooks CL, Gu W. 2009. How does SIRT1 affect metabolism, senescence and cancer? Nat. Rev. Cancer 9:123-128.
    • (2009) Rev. Cancer , vol.9 , pp. 123-128
    • Brooks, C.L.1    Gu, W.2
  • 10
    • 0028864667 scopus 로고
    • Induction of the growth inhibitor IGF-binding protein 3 by p53
    • Buckbinder L, et al. 1995. Induction of the growth inhibitor IGF-binding protein 3 by p53. Nature 377:646-649.
    • (1995) Nature , vol.377 , pp. 646-649
    • Buckbinder, L.1
  • 11
    • 46249100836 scopus 로고    scopus 로고
    • Tissue-specific regulation of SIRT1 by calorie restriction
    • Chen D, et al. 2008. Tissue-specific regulation of SIRT1 by calorie restriction. Genes Dev. 22:1753-1757.
    • (2008) Genes Dev , vol.22 , pp. 1753-1757
    • Chen, D.1
  • 12
    • 0027222956 scopus 로고
    • Mapping of the p53 and mdm-2 interaction domains
    • Chen J, Marechal V, Levine AJ. 1993. Mapping of the p53 and mdm-2 interaction domains. Mol. Cell. Biol. 13:4107- 4114.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 4107-4114
    • Chen, J.1    Marechal, V.2    Levine, A.J.3
  • 13
    • 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
  • 15
    • 65549113750 scopus 로고    scopus 로고
    • CBP/p300-mediated acetylation of histone H3 on lysine 56
    • Das C, Lucia MS, Hansen KC, Tyler JK. 2009. CBP/p300-mediated acetylation of histone H3 on lysine 56. Nature 459:113-117.
    • (2009) Nature , vol.459 , pp. 113-117
    • Das, C.1    Lucia, M.S.2    Hansen, K.C.3    Tyler, J.K.4
  • 16
    • 78049416081 scopus 로고    scopus 로고
    • Alternative pre-mRNA splicing regulation in cancer: pathways and programs unhinged
    • David CJ, Manley JL. 2010. Alternative pre-mRNA splicing regulation in cancer: pathways and programs unhinged. Genes Dev. 24:2343-2364.
    • (2010) Genes Dev , vol.24 , pp. 2343-2364
    • David, C.J.1    Manley, J.L.2
  • 17
    • 77955046461 scopus 로고    scopus 로고
    • SIRT1 suppresses beta-amyloid production by activating the alpha-secretase gene ADAM10
    • Donmez G, Wang D, Cohen DE, Guarente L. 2010. SIRT1 suppresses beta-amyloid production by activating the alpha-secretase gene ADAM10. Cell 142:320 -332.
    • (2010) Cell , vol.142 , pp. 320-332
    • Donmez, G.1    Wang, D.2    Cohen, D.E.3    Guarente, L.4
  • 18
    • 44849096876 scopus 로고    scopus 로고
    • The SIRT1 deacetylase suppresses intestinal tumorigenesis and colon cancer growth
    • Firestein R, et al. 2008. The SIRT1 deacetylase suppresses intestinal tumorigenesis and colon cancer growth. PLoS One 3:e2020.
    • (2008) PLoS One , vol.3
    • Firestein, R.1
  • 19
    • 53649100104 scopus 로고    scopus 로고
    • JNK2-dependent regulation of SIRT1 protein stability
    • Ford J, Ahmed S, Allison S, Jiang M, Milner J. 2008. JNK2-dependent regulation of SIRT1 protein stability. Cell Cycle 7:3091-3097.
    • (2008) Cell Cycle , vol.7 , pp. 3091-3097
    • Ford, J.1    Ahmed, S.2    Allison, S.3    Jiang, M.4    Milner, J.5
  • 20
    • 28544444366 scopus 로고    scopus 로고
    • Cancer-specific functions of SIRT1 enable human epithelial cancer cell growth and survival
    • Ford J, Jiang M, Milner J. 2005. Cancer-specific functions of SIRT1 enable human epithelial cancer cell growth and survival. Cancer Res. 65: 10457-10463.
    • (2005) Cancer Res , vol.65 , pp. 10457-10463
    • Ford, J.1    Jiang, M.2    Milner, J.3
  • 21
    • 0035889087 scopus 로고    scopus 로고
    • APAF1 is a key transcriptional target for p53 in the regulation of neuronal cell death
    • Fortin A, et al. 2001. APAF1 is a key transcriptional target for p53 in the regulation of neuronal cell death. J. Cell Biol. 155:207-216.
    • (2001) J. Cell Biol. , vol.155 , pp. 207-216
    • Fortin, A.1
  • 22
    • 53049092131 scopus 로고    scopus 로고
    • The anti-aging, metabolism potential of SIRT1
    • Ghosh HS. 2008. The anti-aging, metabolism potential of SIRT1. Curr. Opin. Invest. Drugs 9:1095-1102.
    • (2008) Curr. Opin. Invest. Drugs , vol.9 , pp. 1095-1102
    • Ghosh, H.S.1
  • 23
    • 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
  • 24
    • 0030905284 scopus 로고    scopus 로고
    • Mdm2 promotes the rapid degradation of p53
    • Haupt Y, Maya R, Kazaz A, Oren M. 1997. Mdm2 promotes the rapid degradation of p53. Nature 387:296-299.
    • (1997) Nature , vol.387 , pp. 296-299
    • Haupt, Y.1    Maya, R.2    Kazaz, A.3    Oren, M.4
  • 25
    • 34247570492 scopus 로고    scopus 로고
    • Strong expression of a longevity-related protein, SIRT1, in Bowen's disease
    • Hida Y, Kubo Y, Murao K, Arase S. 2007. Strong expression of a longevity-related protein, SIRT1, in Bowen's disease. Arch. Dermatol. Res. 299:103-106.
    • (2007) Arch. Dermatol. Res. , vol.299 , pp. 103-106
    • Hida, Y.1    Kubo, Y.2    Murao, K.3    Arase, S.4
  • 26
    • 34547100073 scopus 로고    scopus 로고
    • SIRT1 is significantly elevated in mouse and human prostate cancer
    • Huffman DM, et al. 2007. SIRT1 is significantly elevated in mouse and human prostate cancer. Cancer Res. 67:6612-6618.
    • (2007) Cancer Res , vol.67 , pp. 6612-6618
    • Huffman, D.M.1
  • 28
  • 29
    • 0029144441 scopus 로고
    • Differential regulation of plasminogen activator and inhibitor gene transcription by the tumor suppressor p53
    • Kunz C, Pebler S, Otte J, von der Ahe D. 1995. Differential regulation of plasminogen activator and inhibitor gene transcription by the tumor suppressor p53. Nucleic Acids Res. 23:3710-3717.
    • (1995) Nucleic Acids Res , vol.23 , pp. 3710-3717
    • Kunz, C.1    Pebler, S.2    Otte, J.3    von der Ahe, D.4
  • 30
    • 53249121556 scopus 로고    scopus 로고
    • Sirtuins: novel therapeutic targets to treat age-associated diseases
    • Lavu S, Boss O, Elliott PJ, Lambert PD. 2008. Sirtuins: novel therapeutic targets to treat age-associated diseases. Nat. Rev. Drug Discov. 7:841-853.
    • (2008) Nat. Rev. Drug Discov. , vol.7 , pp. 841-853
    • Lavu, S.1    Boss, O.2    Elliott, P.J.3    Lambert, P.D.4
  • 31
    • 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
  • 32
    • 33745020716 scopus 로고    scopus 로고
    • Loss of one p53 allele results in four-fold reduction of p53 mRNA and protein: a basis for p53 haplo-insufficiency
    • Lynch CJ, Milner J. 2006. Loss of one p53 allele results in four-fold reduction of p53 mRNA and protein: a basis for p53 haplo-insufficiency. Oncogene 25:3463-3470.
    • (2006) Oncogene , vol.25 , pp. 3463-3470
    • Lynch, C.J.1    Milner, J.2
  • 33
    • 78149421022 scopus 로고    scopus 로고
    • SIRT1 undergoes alternative splicing in a novel auto-regulatory loop with p53
    • Lynch CJ, et al. 2010. SIRT1 undergoes alternative splicing in a novel auto-regulatory loop with p53. PLoS One 5:e13502.
    • (2010) PLoS One , vol.5
    • Lynch, C.J.1
  • 34
    • 0037207475 scopus 로고    scopus 로고
    • The mammalian SIR2α protein has a role in embryogenesis and gametogenesis
    • . 2003. The mammalian SIR2 α 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
  • 35
    • 36749016679 scopus 로고    scopus 로고
    • p53 dependent stimulation of redox-related genes in the lymphoid organs of gamma-irradiated: mice identification of haeme-oxygenase 1 as a direct p53 target gene
    • Meiller A, et al. 2007. p53-dependent stimulation of redox-related genes in the lymphoid organs of gamma-irradiated: mice identification of haeme-oxygenase 1 as a direct p53 target gene. Nucleic Acids Res. 35: 6924-6934.
    • (2007) Nucleic Acids Res , vol.35 , pp. 6924-6934
    • Meiller, A.1
  • 36
    • 36749087548 scopus 로고    scopus 로고
    • Small molecule activators of SIRT1 as therapeutics for the treatment of type 2 diabetes
    • Milne JC, et al. 2007. Small molecule activators of SIRT1 as therapeutics for the treatment of type 2 diabetes. Nature 450:712-716.
    • (2007) Nature , vol.450 , pp. 712-716
    • Milne, J.C.1
  • 37
    • 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
  • 38
    • 0027325132 scopus 로고
    • Oncoprotein MDM2 conceals the activation domain of tumour suppressor p53
    • Oliner JD, et al. 1993. Oncoprotein MDM2 conceals the activation domain of tumour suppressor p53. Nature 362:857-860.
    • (1993) Nature , vol.362 , pp. 857-860
    • Oliner, J.D.1
  • 39
    • 34548180483 scopus 로고    scopus 로고
    • Immunoprecipitation of mRNA-protein complexes
    • Peritz T, et al. 2006. Immunoprecipitation of mRNA-protein complexes. Nat. Protoc. 1:577-580.
    • (2006) Nat. Protoc. , vol.1 , pp. 577-580
    • Peritz, T.1
  • 40
    • 77954861244 scopus 로고    scopus 로고
    • Matrix metalloproteinase-induced epithelial-mesenchymal transition in breast cancer
    • Radisky ES, Radisky DC. 2010. Matrix metalloproteinase-induced epithelial-mesenchymal transition in breast cancer. J. Mammary Gland Biol. Neoplasia 15:201-212.
    • (2010) J. Mammary Gland Biol. Neoplasia , vol.15 , pp. 201-212
    • Radisky, E.S.1    Radisky, D.C.2
  • 41
    • 65549103855 scopus 로고    scopus 로고
    • + biosynthesis
    • + biosynthesis. Science 324:651-654.
    • (2009) Science , vol.324 , pp. 651-654
    • Ramsey, K.M.1
  • 42
    • 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
  • 43
    • 8644224064 scopus 로고    scopus 로고
    • Sir2 mediates longevity in the fly through a pathway related to calorie restriction
    • Rogina B, Helfand SL. 2004. Sir2 mediates longevity in the fly through a pathway related to calorie restriction. Proc. Natl. Acad. Sci. U. S. A. 101: 15998-16003.
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 15998-16003
    • Rogina, B.1    Helfand, S.L.2
  • 44
    • 0344011603 scopus 로고    scopus 로고
    • Disruption of the nucleolus mediates stabilization of p53 in response to DNA damage and other stresses
    • Rubbi CP, Milner J. 2003. Disruption of the nucleolus mediates stabilization of p53 in response to DNA damage and other stresses. EMBO J. 22:6068-6077.
    • (2003) EMBO J , vol.22 , pp. 6068-6077
    • Rubbi, C.P.1    Milner, J.2
  • 45
    • 0030667702 scopus 로고    scopus 로고
    • DNA damage-induced phosphorylation of p53 alleviates inhibition by MDM2
    • Shieh SY, Ikeda M, Taya Y, Prives C. 1997. DNA damage-induced phosphorylation of p53 alleviates inhibition by MDM2. Cell 91:325-334.
    • (1997) Cell , vol.91 , pp. 325-334
    • Shieh, S.Y.1    Ikeda, M.2    Taya, Y.3    Prives, C.4
  • 46
    • 0031435944 scopus 로고    scopus 로고
    • DNA damage induces phosphorylation of the amino terminus of p53
    • Siliciano JD, et al. 1997. DNA damage induces phosphorylation of the amino terminus of p53. Genes Dev. 11:3471-3481.
    • (1997) Genes Dev , vol.11 , pp. 3471-3481
    • Siliciano, J.D.1
  • 47
    • 0031459980 scopus 로고    scopus 로고
    • Extrachromosomal rDNA circles: a cause of aging in yeast
    • Sinclair DA, Guarente L. 1997. Extrachromosomal rDNA circles: a cause of aging in yeast. Cell 91:1033-1042.
    • (1997) Cell , vol.91 , pp. 1033-1042
    • Sinclair, D.A.1    Guarente, L.2
  • 48
    • 36549044009 scopus 로고    scopus 로고
    • Function of the SIRT1 protein deacetylase in cancer
    • Stunkel W, et al. 2007. Function of the SIRT1 protein deacetylase in cancer. Biotechnol. J. 2:1360-1368.
    • (2007) Biotechnol. J. , vol.2 , pp. 1360-1368
    • Stunkel, W.1
  • 49
    • 0033597213 scopus 로고    scopus 로고
    • p53 down-regulates human matrix metalloproteinase-1 (collagenase-1) gene expression
    • Sun Y, Wenger L, Rutter JL, Brinckerhoff CE, Cheung HS. 1999. p53 down-regulates human matrix metalloproteinase-1 (collagenase-1) gene expression. J. Biol. Chem. 274:11535-11540.
    • (1999) J. Biol. Chem. , vol.274 , pp. 11535-11540
    • Sun, Y.1    Wenger, L.2    Rutter, J.L.3    Brinckerhoff, C.E.4    Cheung, H.S.5
  • 50
    • 67649359888 scopus 로고    scopus 로고
    • Up regulation of the alpha-secretase ADAM10 by retinoic acid receptors and acitretin
    • Tippmann F, Hundt J, Schneider A, Endres K, Fahrenholz F. 2009. Up-regulation of the alpha-secretase ADAM10 by retinoic acid receptors and acitretin. FASEB J. 23:1643-1654.
    • (2009) FASEB J , vol.23 , pp. 1643-1654
    • Tippmann, F.1    Hundt, J.2    Schneider, A.3    Endres, K.4    Fahrenholz, F.5
  • 51
    • 0035826271 scopus 로고    scopus 로고
    • Increased dosage of a sir-2 gene extends lifespan in Caenorhabditis elegans
    • Tissenbaum HA, Guarente L. 2001. Increased dosage of a sir-2 gene extends lifespan in Caenorhabditis elegans. Nature 410:227-230.
    • (2001) Nature , vol.410 , pp. 227-230
    • Tissenbaum, H.A.1    Guarente, L.2
  • 52
    • 3142742707 scopus 로고    scopus 로고
    • FOXO4 is acetylated upon peroxide stress and deacetylated by the longevity protein hSir2(SIRT1)
    • van der Horst A, et al. 2004. FOXO4 is acetylated upon peroxide stress and deacetylated by the longevity protein hSir2(SIRT1). J. Biol. Chem. 279:28873-28879.
    • (2004) J. Biol. Chem. , vol.279 , pp. 28873-28879
    • van der Horst, A.1
  • 53
    • 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
  • 54
    • 53149137486 scopus 로고    scopus 로고
    • Impaired DNA damage response, genome instability, and tumorigenesis in SIRT1 mutant mice
    • Wang RH, et al. 2008. Impaired DNA damage response, genome instability, and tumorigenesis in SIRT1 mutant mice. Cancer Cell 14:312-323.
    • (2008) Cancer Cell , vol.14 , pp. 312-323
    • Wang, R.H.1


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