메뉴 건너뛰기




Volumn 289, Issue 8, 2014, Pages 5208-5216

A novel sirtuin 2 (SIRT2) inhibitor with p53-dependent pro-apoptotic activity in non-small cell lung cancer

Author keywords

[No Author keywords available]

Indexed keywords

ACETYLATION; CELL DEATH;

EID: 84894490851     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.487736     Document Type: Article
Times cited : (126)

References (49)
  • 1
    • 0033600176 scopus 로고    scopus 로고
    • Characterization of five human cDNAs with homology to the yeast SIR2 gene: Sir2-like proteins (sirtuins) metabolize NAD and may have protein ADP-ribosyltransferase activity
    • Frye, R. A. (1999) Characterization of five human cDNAs with homology to the yeast SIR2 gene: Sir2-like proteins (sirtuins) metabolize NAD and may have protein ADP-ribosyltransferase activity. Biochem. Biophys. Res. Commun. 260, 273-279
    • (1999) Biochem. Biophys. Res. Commun. , vol.260 , pp. 273-279
    • Frye, R.A.1
  • 2
    • 0033887456 scopus 로고    scopus 로고
    • Phylogenetic classification of prokaryotic and eukaryotic Sir2-like proteins
    • Frye, R. A. (2000) Phylogenetic classification of prokaryotic and eukaryotic Sir2-like proteins. Biochem. Biophys. Res. Commun. 273, 793-798
    • (2000) Biochem. Biophys. Res. Commun. , vol.273 , pp. 793-798
    • Frye, R.A.1
  • 3
    • 0034677535 scopus 로고    scopus 로고
    • Transcriptional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase
    • Imai, S., Armstrong, C. M., Kaeberlein, M., and 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
  • 6
    • 40849135481 scopus 로고    scopus 로고
    • The Sirtuin family: Therapeutic targets to treat diseases of aging
    • Milne, J. C., and Denu, J. M. (2008) The Sirtuin family: therapeutic targets to treat diseases of aging. Curr. Opin. Chem. Biol. 12, 11-17
    • (2008) Curr. Opin. Chem. Biol. , vol.12 , pp. 11-17
    • Milne, J.C.1    Denu, J.M.2
  • 7
    • 77949887506 scopus 로고    scopus 로고
    • Mammalian sirtuins: Biological insights and disease relevance
    • Haigis, M. C., and Sinclair, D. A. (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
  • 8
    • 33746228121 scopus 로고    scopus 로고
    • Sirtuins in aging and age-related disease
    • Longo, V. D., and Kennedy, B. K. (2006) Sirtuins in aging and age-related disease. Cell 126, 257-268
    • (2006) Cell , vol.126 , pp. 257-268
    • Longo, V.D.1    Kennedy, B.K.2
  • 9
    • 0035863153 scopus 로고    scopus 로고
    • A cytosolic NAD-dependent deacetylase, Hst2p, can modulate nucleolar and telomeric silencing in yeast
    • Perrod, S., Cockell, M. M., Laroche, T., Renauld, H., Ducrest, A. L., Bonnard, C., and Gasser, S. M. (2001) A cytosolic NAD-dependent deacetylase, Hst2p, can modulate nucleolar and telomeric silencing in yeast. EMBO J. 20, 197-209
    • (2001) EMBO J. , vol.20 , pp. 197-209
    • Perrod, S.1    Cockell, M.M.2    Laroche, T.3    Renauld, H.4    Ducrest, A.L.5    Bonnard, C.6    Gasser, S.M.7
  • 10
    • 0242626891 scopus 로고    scopus 로고
    • Structure of the yeast Hst2 protein deacetylase in ternary complex with 2-O-acetyl ADP ribose and histone peptide
    • Zhao, K., Chai, X., and Marmorstein, R. (2003) Structure of the yeast Hst2 protein deacetylase in ternary complex with 2-O-acetyl ADP ribose and histone peptide. Structure 11, 1403-1411
    • (2003) Structure , vol.11 , pp. 1403-1411
    • Zhao, K.1    Chai, X.2    Marmorstein, R.3
  • 12
    • 65549113750 scopus 로고    scopus 로고
    • CBP/p300-mediated acetylation of histone H3 on lysine
    • Das, C., Lucia, M. S., Hansen, K. C., and Tyler, J. K. (2009) CBP/p300-mediated acetylation of histone H3 on lysine. 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
  • 15
    • 78649738291 scopus 로고    scopus 로고
    • SIRT2 regulates NF-κB-dependent gene expression through deacetylation of p65 Lys-310
    • Rothgiesser, K. M., Erener, S., Waibel, S., Lüscher, B., and Hottiger, M. O. (2010) SIRT2 regulates NF-κB-dependent gene expression through deacetylation of p65 Lys-310. J. Cell Sci. 123, 4251-4258
    • (2010) J. Cell Sci. , vol.123 , pp. 4251-4258
    • Rothgiesser, K.M.1    Erener, S.2    Waibel, S.3    Lüscher, B.4    Hottiger, M.O.5
  • 16
    • 34547397081 scopus 로고    scopus 로고
    • SIRT2 regulates adipocyte differentiation through FoxO1 acetylation/deacetylation
    • Jing, E., Gesta, S., and Kahn, C. R. (2007) SIRT2 regulates adipocyte differentiation through FoxO1 acetylation/deacetylation. Cell Metab. 6, 105-114
    • (2007) Cell Metab. , vol.6 , pp. 105-114
    • Jing, E.1    Gesta, S.2    Kahn, C.R.3
  • 17
    • 34447626095 scopus 로고    scopus 로고
    • SIRT2 deacetylates FOXO3a in response to oxidative stress and caloric restriction
    • Wang, F., Nguyen, M., Qin, F. X., and Tong, Q. (2007) SIRT2 deacetylates FOXO3a in response to oxidative stress and caloric restriction. Aging Cell 6, 505-514
    • (2007) Aging Cell , vol.6 , pp. 505-514
    • Wang, F.1    Nguyen, M.2    Qin, F.X.3    Tong, Q.4
  • 18
    • 0037291214 scopus 로고    scopus 로고
    • The human Sir2 ortholog, SIRT2, is an NADdependent tubulin deacetylase
    • North, B. J., Marshall, B. L., Borra, M. T., Denu, J. M., and Verdin, E. (2003) The human Sir2 ortholog, SIRT2, is an NADdependent 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
  • 20
    • 39149122568 scopus 로고    scopus 로고
    • Interphase nucleo-cytoplasmic shuttling and localization of SIRT2 during mitosis
    • North, B. J., and Verdin, E. (2007) Interphase nucleo-cytoplasmic shuttling and localization of SIRT2 during mitosis. PloS One 2, e784
    • (2007) PloS One , vol.2
    • North, B.J.1    Verdin, E.2
  • 21
    • 0037405043 scopus 로고    scopus 로고
    • Role for human SIRT2 NAD-dependent deacetylase activity in control of mitotic exit in the cell cycle
    • Dryden, S. C., Nahhas, F. A., Nowak, J. E., Goustin, A. S., and Tainsky, M. A. (2003) Role for human SIRT2 NAD-dependent deacetylase activity in control of mitotic exit in the cell cycle. Mol. Cell. Biol. 23, 3173-3185
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 3173-3185
    • Dryden, S.C.1    Nahhas, F.A.2    Nowak, J.E.3    Goustin, A.S.4    Tainsky, M.A.5
  • 22
    • 34248151365 scopus 로고    scopus 로고
    • The molecular biology of mammalian SIRT proteins: SIRT2 in cell cycle regulation
    • Inoue, T., Hiratsuka, M., Osaki, M., and Oshimura, M. (2007) The molecular biology of mammalian SIRT proteins: SIRT2 in cell cycle regulation. Cell Cycle 6, 1011-1018
    • (2007) Cell Cycle , vol.6 , pp. 1011-1018
    • Inoue, T.1    Hiratsuka, M.2    Osaki, M.3    Oshimura, M.4
  • 23
    • 80054782483 scopus 로고    scopus 로고
    • The dual role of sirtuins in cancer
    • Bosch-Presegué, L., and Vaquero, A. (2011) The dual role of sirtuins in cancer. Genes Cancer 2, 648-662
    • (2011) Genes Cancer , vol.2 , pp. 648-662
    • Bosch-Presegué, L.1    Vaquero, A.2
  • 25
    • 0035913911 scopus 로고    scopus 로고
    • Negative control of p53 by Sir2 promotes cell survival under stress
    • Luo, J., Nikolaev, A. Y., Imai, S., Chen, D., Su, F., Shiloh, A., Guarente, L., and Gu, W. (2001) Negative control of p53 by Sir2 promotes cell survival under stress. Cell 107, 137-148
    • (2001) Cell , vol.107 , pp. 137-148
    • Luo, J.1    Nikolaev, A.Y.2    Imai, S.3    Chen, D.4    Su, F.5    Shiloh, A.6    Guarente, L.7    Gu, W.8
  • 27
    • 78650638268 scopus 로고    scopus 로고
    • SIRT2 down-regulation in HeLa can induce p53 accumulation via p38 MAPK activation-dependent p300 decrease, eventually leading to apoptosis
    • Li, Y., Matsumori, H., Nakayama, Y., Osaki, M., Kojima, H., Kurimasa, A., Ito, H., Mori, S., Katoh, M., Oshimura, M., and Inoue, T. (2011) SIRT2 down-regulation in HeLa can induce p53 accumulation via p38 MAPK activation-dependent p300 decrease, eventually leading to apoptosis. Genes Cells 16, 34-45
    • (2011) Genes Cells , vol.16 , pp. 34-45
    • Li, Y.1    Matsumori, H.2    Nakayama, Y.3    Osaki, M.4    Kojima, H.5    Kurimasa, A.6    Ito, H.7    Mori, S.8    Katoh, M.9    Oshimura, M.10    Inoue, T.11
  • 32
    • 53249114029 scopus 로고    scopus 로고
    • Inhibition of specific HDACs and sirtuins suppresses pathogenesis in a Drosophila model of Huntington's disease
    • Pallos, J., Bodai, L., Lukacsovich, T., Purcell, J. M., Steffan, J. S., Thompson, L. M., and Marsh, J. L. (2008) Inhibition of specific HDACs and sirtuins suppresses pathogenesis in a Drosophila model of Huntington's disease. Hum. Mol. Genet. 17, 3767-3775
    • (2008) Hum. Mol. Genet. , vol.17 , pp. 3767-3775
    • Pallos, J.1    Bodai, L.2    Lukacsovich, T.3    Purcell, J.M.4    Steffan, J.S.5    Thompson, L.M.6    Marsh, J.L.7
  • 33
    • 0029002136 scopus 로고
    • A modified oestrogen receptor ligand-binding domain as an improved switch for the regulation of heterologous proteins
    • Littlewood, T. D., Hancock, D. C., Danielian, P. S., Parker, M. G., and Evan, G. I. (1995) A modified oestrogen receptor ligand-binding domain as an improved switch for the regulation of heterologous proteins. Nucleic Acids Res. 23, 1686-1690
    • (1995) Nucleic Acids Res. , vol.23 , pp. 1686-1690
    • Littlewood, T.D.1    Hancock, D.C.2    Danielian, P.S.3    Parker, M.G.4    Evan, G.I.5
  • 35
    • 0025726216 scopus 로고
    • A rapid and simple method for measuring thymocyte apoptosis by propidium iodide staining and flow cytometry
    • Nicoletti, I., Migliorati, G., Pagliacci, M. C., Grignani, F., and Riccardi, C. (1991) A rapid and simple method for measuring thymocyte apoptosis by propidium iodide staining and flow cytometry. J. Immunol. Methods 139, 271-279
    • (1991) J. Immunol. Methods , vol.139 , pp. 271-279
    • Nicoletti, I.1    Migliorati, G.2    Pagliacci, M.C.3    Grignani, F.4    Riccardi, C.5
  • 38
    • 84856076413 scopus 로고    scopus 로고
    • SIRT1 contains N-and C-terminal regions that potentiate deacetylase activity
    • Pan, M., Yuan, H., Brent, M., Ding, E. C., and Marmorstein, R. (2012) SIRT1 contains N-and C-terminal regions that potentiate deacetylase activity. J. Biol. Chem. 287, 2468-2476
    • (2012) J. Biol. Chem. , vol.287 , pp. 2468-2476
    • Pan, M.1    Yuan, H.2    Brent, M.3    Ding, E.C.4    Marmorstein, R.5
  • 39
    • 34447625911 scopus 로고    scopus 로고
    • Epigenetics and aging: The targets and the marks
    • Fraga, M. F., and Esteller, M. (2007) Epigenetics and aging: the targets and the marks. Trends Genet. 23, 413-418
    • (2007) Trends Genet. , vol.23 , pp. 413-418
    • Fraga, M.F.1    Esteller, M.2
  • 40
    • 84864331749 scopus 로고    scopus 로고
    • Individual dose and scheduling determine the efficacy of combining cytotoxic anticancer agents with a kinase inhibitor in non-small cell lung cancer
    • Meiler, J., Guyot, M., Hoffarth, S., Wesarg, E., Höhn, Y., Breitenbuecher, F., and Schuler, M. (2012) Individual dose and scheduling determine the efficacy of combining cytotoxic anticancer agents with a kinase inhibitor in non-small cell lung cancer. J. Cancer Res. Clin. Oncol. 138, 1385-1394
    • (2012) J. Cancer Res. Clin. Oncol. , vol.138 , pp. 1385-1394
    • Meiler, J.1    Guyot, M.2    Hoffarth, S.3    Wesarg, E.4    Höhn, Y.5    Breitenbuecher, F.6    Schuler, M.7
  • 41
    • 0029784962 scopus 로고    scopus 로고
    • Induction of apoptosis by tamoxifen-activation of a p53-estrogen receptor fusion protein expressed in E1A and T24 H-ras transformed p53-/-mouse embryo fibroblasts
    • Vater, C. A., Bartle, L. M., Dionne, C. A., Littlewood, T. D., and Goldmacher, V. S. (1996) Induction of apoptosis by tamoxifen-activation of a p53-estrogen receptor fusion protein expressed in E1A and T24 H-ras transformed p53-/-mouse embryo fibroblasts. Oncogene 13, 739-748
    • (1996) Oncogene , vol.13 , pp. 739-748
    • Vater, C.A.1    Bartle, L.M.2    Dionne, C.A.3    Littlewood, T.D.4    Goldmacher, V.S.5
  • 44
    • 0035265823 scopus 로고    scopus 로고
    • PUMA induces the rapid apoptosis of colorectal cancer cells
    • Yu, J., Zhang, L., Hwang, P. M., Kinzler, K. W., and Vogelstein, B. (2001) PUMA induces the rapid apoptosis of colorectal cancer cells. Mol. Cell 7, 673-682
    • (2001) Mol. Cell , vol.7 , pp. 673-682
    • Yu, J.1    Zhang, L.2    Hwang, P.M.3    Kinzler, K.W.4    Vogelstein, B.5
  • 45
    • 67650444786 scopus 로고    scopus 로고
    • Identification of a small molecule SIRT2 inhibitor with selective tumor cytotoxicity
    • Zhang, Y., Au, Q., Zhang, M., Barber, J. R., Ng, S. C., and Zhang, B. (2009) Identification of a small molecule SIRT2 inhibitor with selective tumor cytotoxicity. Biochem. Biophys. Res. Commun. 386, 729-733
    • (2009) Biochem. Biophys. Res. Commun. , vol.386 , pp. 729-733
    • Zhang, Y.1    Au, Q.2    Zhang, M.3    Barber, J.R.4    Ng, S.C.5    Zhang, B.6
  • 46
    • 0030797585 scopus 로고    scopus 로고
    • Activation of p53 sequence-specific DNA binding by acetylation of the p53 C-terminal domain
    • Gu, W., and Roeder, R. G. (1997) Activation of p53 sequence-specific DNA binding by acetylation of the p53 C-terminal domain. Cell 90, 595-606
    • (1997) Cell , vol.90 , pp. 595-606
    • Gu, W.1    Roeder, R.G.2
  • 47
    • 84869869682 scopus 로고    scopus 로고
    • HDAC inhibitorbased therapies: Can we interpret the code?
    • New, M., Olzscha, H., and La Thangue, N. B. (2012) HDAC inhibitorbased therapies: can we interpret the code? Mol. Oncol. 6, 637-656
    • (2012) Mol. Oncol. , vol.6 , pp. 637-656
    • New, M.1    Olzscha, H.2    La Thangue, N.B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.