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Volumn 259, Issue , 2004, Pages 197-207

Dynamics of the p53 acetylation pathway

Author keywords

[No Author keywords available]

Indexed keywords

ACYLTRANSFERASE; DNA; MDM2 PROTEIN, HUMAN; NUCLEAR PROTEIN; ONCOPROTEIN; PROTEIN MDM2; PROTEIN P53; UBIQUITIN;

EID: 2942731801     PISSN: None     EISSN: None     Source Type: Book Series    
DOI: None     Document Type: Article
Times cited : (52)

References (37)
  • 1
    • 0035694469 scopus 로고    scopus 로고
    • Acetylation of p53 activates transcription through recruitment of coactivators/histone acetyltransferases
    • Barlev NA, Liu L, Chehab NH et al 2001 Acetylation of p53 activates transcription through recruitment of coactivators/histone acetyltransferases. Mol Cell 8:1243-1254
    • (2001) Mol Cell , vol.8 , pp. 1243-1254
    • Barlev, N.A.1    Liu, L.2    Chehab, N.H.3
  • 2
    • 0037377060 scopus 로고    scopus 로고
    • Ubiquitination, phosphorylation and acetylation: The molecular basis for p53 regulation
    • Brooks CL, Gu W 2003 Ubiquitination, phosphorylation and acetylation: the molecular basis for p53 regulation. Curr Opin Cell Biol 15:164-171
    • (2003) Curr Opin Cell Biol , vol.15 , pp. 164-171
    • Brooks, C.L.1    Gu, W.2
  • 3
    • 0034665461 scopus 로고    scopus 로고
    • p53 transcriptional activity is essential for p53-dependent apoptosis following DNA damage
    • Chao C, Saito S, Kang J, Anderson CW, Appella E, Xu Y 2000 p53 transcriptional activity is essential for p53-dependent apoptosis following DNA damage. EMBO J 19:4967-4975
    • (2000) EMBO J , vol.19 , pp. 4967-4975
    • Chao, C.1    Saito, S.2    Kang, J.3    Anderson, C.W.4    Appella, E.5    Xu, Y.6
  • 6
    • 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 RA 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
  • 7
    • 0034234237 scopus 로고    scopus 로고
    • CBP/p300 in cell growth, transformation, and development
    • Goodman RH, Smolik S 2000 CBP/p300 in cell growth, transformation, and development. Genes Dev 14:1553-1577
    • (2000) Genes Dev , vol.14 , pp. 1553-1577
    • Goodman, R.H.1    Smolik, S.2
  • 8
    • 0035862199 scopus 로고    scopus 로고
    • The human histone deacetylase family
    • Gray SG, Ekstrom TJ 2001 The human histone deacetylase family. Exp Cell Res 262:75-83
    • (2001) Exp Cell Res , vol.262 , pp. 75-83
    • Gray, S.G.1    Ekstrom, T.J.2
  • 9
    • 0030797585 scopus 로고    scopus 로고
    • Activation of p53 sequence-specific DNA binding by acetylation of the p53 C-terminal domain
    • Gu W, Roeder RG 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
  • 10
    • 0030996361 scopus 로고    scopus 로고
    • Synergistic activation of transcription by CBP and p53
    • Gu W, Shi XL, Roeder RG 1997 Synergistic activation of transcription by CBP and p53. Nature 387:819-823
    • (1997) Nature , vol.387 , pp. 819-823
    • Gu, W.1    Shi, X.L.2    Roeder, R.G.3
  • 11
    • 0034193776 scopus 로고    scopus 로고
    • Sir2 links chromatin silencing, metabolism, and aging
    • Guarente L 2000 Sir2 links chromatin silencing, metabolism, and aging. Genes Dev 14:1021-1026
    • (2000) Genes Dev , vol.14 , pp. 1021-1026
    • Guarente, L.1
  • 12
    • 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
  • 13
    • 0033521621 scopus 로고    scopus 로고
    • Association of p19(ARF) with Mdm2 inhibits ubiquitin ligase activity of Mdm2 for tumor suppressor p53
    • Honda R, Yasuda H 1999 Association of p19(ARF) with Mdm2 inhibits ubiquitin ligase activity of Mdm2 for tumor suppressor p53. EMBO J 18:22-27
    • (1999) EMBO J , vol.18 , pp. 22-27
    • Honda, R.1    Yasuda, H.2
  • 14
    • 0028845158 scopus 로고
    • Small peptides activate the latent sequence-specific DNA binding function of p53
    • Hupp TR, Sparks A, Lane DP 1995 Small peptides activate the latent sequence-specific DNA binding function of p53. Cell 83:237-245
    • (1995) Cell , vol.83 , pp. 237-245
    • Hupp, T.R.1    Sparks, A.2    Lane, D.P.3
  • 15
    • 0034677535 scopus 로고    scopus 로고
    • Transcriptional silencing and longevity protein Sir2 is a NAD-dependent histone deacetylase
    • Imai S, Armstrong CM, Kaeberlein M, Guarente L 2000 Transcriptional silencing and longevity protein Sir2 is a 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
  • 16
    • 0035868964 scopus 로고    scopus 로고
    • p300/CBP-mediated p53 acetylation is commonly induced by p53-activating agents and inhibited by MDM2
    • Ito A, Lai C, Zhao X et al 2001 p300/CBP-mediated p53 acetylation is commonly induced by p53-activating agents and inhibited by MDM2. EMBO J 20:1331-1340
    • (2001) EMBO J , vol.20 , pp. 1331-1340
    • Ito, A.1    Lai, C.2    Zhao, X.3
  • 17
    • 0028834902 scopus 로고
    • Rescue of embryonic lethality in Mdm2-deficient mice by absence of p53
    • Jones SN, Roe AE, Donehower LA, Bradley A 1995 Rescue of embryonic lethality in Mdm2-deficient mice by absence of p53. Nature 378:206-208
    • (1995) Nature , vol.378 , pp. 206-208
    • Jones, S.N.1    Roe, A.E.2    Donehower, L.A.3    Bradley, A.4
  • 18
    • 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
  • 19
    • 0037093346 scopus 로고    scopus 로고
    • Human SIR2 deacetylates p53 and antagonizes PML/p53-induced cellular senescence
    • Langley E, Pearson M, Faretta M 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    Pearson, M.2    Faretta, M.3
  • 20
    • 0037184969 scopus 로고    scopus 로고
    • Acetylation of p53 inhibits its ubiquitination by Mdm2
    • Li M, Luo J, Brooks CL, Gu W 2002 Acetylation of p53 inhibits its ubiquitination by Mdm2. J Biol Chem 277:50607-50611
    • (2002) J Biol Chem , vol.277 , pp. 50607-50611
    • Li, M.1    Luo, J.2    Brooks, C.L.3    Gu, W.4
  • 21
    • 0032906633 scopus 로고    scopus 로고
    • p53 sites acetylated in vitro by PCAF and p300 are acetylated in vivo in response to DNA damage
    • Liu L, Scolnick DM, Trievel RC et al 1999 p53 sites acetylated in vitro by PCAF and p300 are acetylated in vivo in response to DNA damage. Mol Cell Biol 19:1202-1209
    • (1999) Mol Cell Biol , vol.19 , pp. 1202-1209
    • Liu, L.1    Scolnick, D.M.2    Trievel, R.C.3
  • 22
    • 0034676439 scopus 로고    scopus 로고
    • Deacetylation of p53 modulates its effect on cell growth and apoptosis
    • Luo J, Su F, Chen D, Shiloh A, Gu W 2000 Deacetylation of p53 modulates its effect on cell growth and apoptosis. Nature 408:377-381
    • (2000) Nature , vol.408 , pp. 377-381
    • Luo, J.1    Su, F.2    Chen, D.3    Shiloh, A.4    Gu, W.5
  • 23
    • 0035913911 scopus 로고    scopus 로고
    • Negative control of p53 by Sir2alpha promotes cell survival under stress
    • Luo J, Nikolaev AY, Imai S et al W 2001 Negative control of p53 by Sir2alpha 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
  • 24
    • 0035313756 scopus 로고    scopus 로고
    • Enzymatic activities of Sir2 and chromatin silencing
    • Moazed D 2001 Enzymatic activities of Sir2 and chromatin silencing. Curr Opin Cell Biol 13:232-238
    • (2001) Curr Opin Cell Biol , vol.13 , pp. 232-238
    • Moazed, D.1
  • 25
    • 0028823020 scopus 로고
    • Rescue of early embryonic lethality in mdm2-deficient mice by deletion of p53
    • Montes de Oca Luna R, Wagner DS, Lozano G 1995 Rescue of early embryonic lethality in mdm2-deficient mice by deletion of p53. Nature 378:203-206
    • (1995) Nature , vol.378 , pp. 203-206
    • Montes De Oca Luna, R.1    Wagner, D.S.2    Lozano, G.3
  • 26
    • 0034644274 scopus 로고    scopus 로고
    • PML regulates p53 acetylation and premature senescence induced by oncogenic Ras
    • Pearson M, Carbone R, Sebastiani C et al 2000 PML regulates p53 acetylation and premature senescence induced by oncogenic Ras. Nature 406:207-210
    • (2000) Nature , vol.406 , pp. 207-210
    • Pearson, M.1    Carbone, R.2    Sebastiani, C.3
  • 27
    • 0034915764 scopus 로고    scopus 로고
    • Mechanisms underlying ubiquitination
    • Pickart CM 2001 Mechanisms underlying ubiquitination. Annu Rev Biochem 70:503-533
    • (2001) Annu Rev Biochem , vol.70 , pp. 503-533
    • Pickart, C.M.1
  • 28
    • 0032931517 scopus 로고    scopus 로고
    • The p53 pathway
    • Prives C, Hall PA 1999 The p53 pathway. J Pathol 187:112-126
    • (1999) J Pathol , vol.187 , pp. 112-126
    • Prives, C.1    Hall, P.A.2
  • 29
    • 0035966316 scopus 로고    scopus 로고
    • Why is p53 acetylated?
    • Prives C, Manley JL 2001 Why is p53 acetylated? Cell 107:815-818
    • (2001) Cell , vol.107 , pp. 815-818
    • Prives, C.1    Manley, J.L.2
  • 30
    • 0033767235 scopus 로고    scopus 로고
    • Multiple C-terminal lysine residues target p53 for ubiquitin-proteasome- mediated degradation
    • Rodriguez MS, Desterro JM, Lain S, Lane DP, Hay RT 2000 Multiple C-terminal lysine residues target p53 for ubiquitin-proteasome-mediated degradation. Mol Cell Biol 20:8458-8467
    • (2000) Mol Cell Biol , vol.20 , pp. 8458-8467
    • Rodriguez, M.S.1    Desterro, J.M.2    Lain, S.3    Lane, D.P.4    Hay, R.T.5
  • 31
    • 0032530486 scopus 로고    scopus 로고
    • DNA damage activates p53 through a phosphorylation-acetylation cascade
    • Sakaguchi K, Herrera JE, Saito S et al 1998 DNA damage activates p53 through a phosphorylation-acetylation cascade. Genes Dev 12:2831-2841
    • (1998) Genes Dev , vol.12 , pp. 2831-2841
    • Sakaguchi, K.1    Herrera, J.E.2    Saito, S.3
  • 32
    • 0030961889 scopus 로고    scopus 로고
    • Restoration of the growth suppression function of mutant p53 by a synthetic peptide derived from the p53 C-terminal domain
    • Selivanova G, Iotsova V, Okan I et al 1997 Restoration of the growth suppression function of mutant p53 by a synthetic peptide derived from the p53 C-terminal domain. Nat Med 6:632-638
    • (1997) Nat Med , vol.6 , pp. 632-638
    • Selivanova, G.1    Iotsova, V.2    Okan, I.3
  • 35
    • 0035913903 scopus 로고    scopus 로고
    • hSIR2(SIRT1) functions as an NAD-dependent p53 deacetylase
    • Vaziri H, Dessain SK, Ng Eaton E 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    Dessain, S.K.2    Ng Eaton, E.3
  • 37
    • 0033634972 scopus 로고    scopus 로고
    • Activation of p53 or loss of the Cockayne syndrome group B repair protein causes metaphase fragility of human U1, U2, and 5S genes
    • Yu A, Fan H, Lao D, Bailey AD, Weiner AM 2000 Activation of p53 or loss of the Cockayne syndrome group B repair protein causes metaphase fragility of human U1, U2, and 5S genes. Mol Cell 5:801-810
    • (2000) Mol Cell , vol.5 , pp. 801-810
    • Yu, A.1    Fan, H.2    Lao, D.3    Bailey, A.D.4    Weiner, A.M.5


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