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Volumn 21, Issue 22, 2002, Pages 6236-6245

MDM2-HDAC1-mediated deacetylation of p53 is required for its degradation

Author keywords

Acetylation; HDAC1; MDM2; p53; Ubiquitylation

Indexed keywords

HISTONE DEACETYLASE; LYSINE; PROTEIN MDM2; PROTEIN P53;

EID: 0037112901     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/cdf616     Document Type: Article
Times cited : (483)

References (33)
  • 1
    • 0034818446 scopus 로고    scopus 로고
    • Post-translational modifications and activation of p53 by genotoxic stresses
    • Appella, E. and Anderson, C.W. (2001) Post-translational modifications and activation of p53 by genotoxic stresses. Eur. J. Biochem., 268, 2764-2772.
    • (2001) Eur. J. Biochem. , vol.268 , pp. 2764-2772
    • Appella, E.1    Anderson, C.W.2
  • 2
    • 0034003005 scopus 로고    scopus 로고
    • Stress signals utilize multiple pathways to stabilize p53
    • Ashcroft, M., Taya, Y. and Vousden, K.H. (2000) Stress signals utilize multiple pathways to stabilize p53. Mol. Cell. Biol., 20, 3224-3233.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 3224-3233
    • Ashcroft, M.1    Taya, Y.2    Vousden, K.H.3
  • 3
    • 0035694469 scopus 로고    scopus 로고
    • Acetylation of p53 activates transcription through recruitment of coactivators/histone acetyltransferases
    • Barlev, N.A., Liu, L., Chehab, N.H., Mansfield, K., Harris, K.G., Halazonetis, T.D. and Berger, S.L. (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    Mansfield, K.4    Harris, K.G.5    Halazonetis, T.D.6    Berger, S.L.7
  • 4
    • 0034282102 scopus 로고    scopus 로고
    • An intact HDM2 RING-finger domain is required for nuclear exclusion of p53
    • Boyd, S.D., Tsai, K.Y. and Jacks, T. (2000) An intact HDM2 RING-finger domain is required for nuclear exclusion of p53. Nat. Cell Biol., 2, 563-568.
    • (2000) Nat. Cell Biol. , vol.2 , pp. 563-568
    • Boyd, S.D.1    Tsai, K.Y.2    Jacks, T.3
  • 7
    • 0034282220 scopus 로고    scopus 로고
    • The MDM2 RING-finger domain is required to promote p53 nuclear export
    • Geyer, R.K., Yu, Z.K. and Maki, C.G. (2000) The MDM2 RING-finger domain is required to promote p53 nuclear export. Nat. Cell Biol., 2, 569-573.
    • (2000) Nat. Cell Biol. , vol.2 , pp. 569-573
    • Geyer, R.K.1    Yu, Z.K.2    Maki, C.G.3
  • 8
    • 0032192140 scopus 로고    scopus 로고
    • The complexity of p53 modulation: Emerging patterns from divergent signals
    • Giaccia, A.J. and Kastan, M.B. (1998) The complexity of p53 modulation: Emerging patterns from divergent signals. Genes Dev., 12, 2973-2983.
    • (1998) Genes Dev. , vol.12 , pp. 2973-2983
    • Giaccia, A.J.1    Kastan, M.B.2
  • 9
    • 0033609055 scopus 로고    scopus 로고
    • Three proteins define a class of human histone deacetylases related to yeast Hda1p
    • Grozinger, C.M., Hassig, C.A. and Schreiber, S.L. (1999) Three proteins define a class of human histone deacetylases related to yeast Hda1p. Proc. Natl Acad. Sci. USA, 96, 4868-4873.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 4868-4873
    • Grozinger, C.M.1    Hassig, C.A.2    Schreiber, S.L.3
  • 10
    • 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
  • 12
    • 0033521621 scopus 로고    scopus 로고
    • Association of p19(ARF) with Mdm2 inhibits ubiquitin ligase activity of Mdm2 for tumor suppressor p53
    • Honda, R. and 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
  • 13
    • 0031583962 scopus 로고    scopus 로고
    • Oncoprotein MDM2 is a ubiquitin ligase E3 for tumor suppressor p53
    • Honda, R., Tanaka, H. and Yasuda, H. (1997) Oncoprotein MDM2 is a ubiquitin ligase E3 for tumor suppressor p53. FEBS Lett., 420, 25-27.
    • (1997) FEBS Lett. , vol.420 , pp. 25-27
    • Honda, R.1    Tanaka, H.2    Yasuda, H.3
  • 14
    • 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.H., Zhao, X., Saito, S., Hamilton, M.H., Appella, E. and Yao, T.P. (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.H.2    Zhao, X.3    Saito, S.4    Hamilton, M.H.5    Appella, E.6    Yao, T.P.7
  • 15
    • 0033732303 scopus 로고    scopus 로고
    • MDM2 inhibits p300-mediated p53 acetylation and activation by forming a ternary complex with the two proteins
    • Kobet, E., Zeng, X., Zhu, Y., Keller, D. and Lu, H. (2000) MDM2 inhibits p300-mediated p53 acetylation and activation by forming a ternary complex with the two proteins. Proc. Natl Acad. Sci. USA, 97, 12547-12552.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 12547-12552
    • Kobet, E.1    Zeng, X.2    Zhu, Y.3    Keller, D.4    Lu, H.5
  • 17
    • 0034676439 scopus 로고    scopus 로고
    • Deacetylation of p53 modulates its effect on cell growth and apoptosis
    • Luo, J., Su, F., Chen, D., Shiloh, A. and 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
  • 18
    • 0035913911 scopus 로고    scopus 로고
    • Negative control of p53 by Sir2α 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 Sir2α 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
  • 19
    • 0028823020 scopus 로고
    • Rescue of early embryonic lethality in mdm2-deficient mice by deletion of p53
    • Montes de Oca Luna, R., Wagner, D.S. and 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
  • 20
    • 0034458966 scopus 로고    scopus 로고
    • Multiple lysine mutations in the C-terminal domain of p53 interfere with MDM2-dependent protein degradation and ubiquitination
    • Nakamura, S., Roth, J.A. and Mukhopadhyay, T. (2000) Multiple lysine mutations in the C-terminal domain of p53 interfere with MDM2-dependent protein degradation and ubiquitination. Mol. Cell. Biol., 20, 9391-9398.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 9391-9398
    • Nakamura, S.1    Roth, J.A.2    Mukhopadhyay, T.3
  • 21
    • 0034644274 scopus 로고    scopus 로고
    • PML regulates p53 acetylation and premature senescence induced by oncogenic Ras
    • Pearson, M. 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
  • 22
    • 0032549704 scopus 로고    scopus 로고
    • The Ink4a tumor suppressor gene product, pl9Arf, interacts with MDM2 and neutralizes MDM2's inhibition of p53
    • Pomerantz, J. et al. (1998) The Ink4a tumor suppressor gene product, pl9Arf, interacts with MDM2 and neutralizes MDM2's inhibition of p53. Cell, 92, 713-723.
    • (1998) Cell , vol.92 , pp. 713-723
    • Pomerantz, J.1
  • 23
    • 0033767235 scopus 로고    scopus 로고
    • Multiple C-terminal lysine residues target p53 for ubiquitin-proteasome-mediated degradation
    • Rodriguez, M.S., Desterro, J.M., Lain, S., Lane, D.P. and Hay, R.T. (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
  • 25
    • 0035834428 scopus 로고    scopus 로고
    • Regulation of receptor fate by ubiquitination of activated β2-adrenergic receptor and β-arrestin
    • Shenoy, S.K., McDonald, P.H., Kohout, T.A. and Lefkowitz, R.J. (2001) Regulation of receptor fate by ubiquitination of activated β2-adrenergic receptor and β-arrestin. Science, 294, 1307-1313.
    • (2001) Science , vol.294 , pp. 1307-1313
    • Shenoy, S.K.1    McDonald, P.H.2    Kohout, T.A.3    Lefkowitz, R.J.4
  • 26
    • 0030667702 scopus 로고    scopus 로고
    • DNA damage-induced phosphorylation of p53 alleviates inhibition by MDM2
    • Shieh, S.Y., Ikeda, M., Taya, Y. and 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
  • 29
    • 0027244853 scopus 로고
    • The p53-mdm-2 autoregulatory feedback loop
    • Wu, X., Bayle, J.H., Olson, D. and Levine, A.J. (1993) The p53-mdm-2 autoregulatory feedback loop. Genes Dev., 7, 1126-1132.
    • (1993) Genes Dev. , vol.7 , pp. 1126-1132
    • Wu, X.1    Bayle, J.H.2    Olson, D.3    Levine, A.J.4
  • 30
    • 0026646635 scopus 로고
    • Drosophila ultraspiracle modulates ecdysone receptor function via heterodimer formation
    • Yao, T.P., Segraves, W.A., Oro, A.E., McKeown, M. and Evans, R.M. (1992) Drosophila ultraspiracle modulates ecdysone receptor function via heterodimer formation. Cell, 71, 63-72.
    • (1992) Cell , vol.71 , pp. 63-72
    • Yao, T.P.1    Segraves, W.A.2    Oro, A.E.3    McKeown, M.4    Evans, R.M.5
  • 31
    • 0034915032 scopus 로고    scopus 로고
    • Control of p53 ubiquitination and nuclear export by MDM2 and ARF
    • Zhang, Y. and Xiong, Y. (2001) Control of p53 ubiquitination and nuclear export by MDM2 and ARF. Cell Growth Differ., 12, 175-186.
    • (2001) Cell Growth Differ. , vol.12 , pp. 175-186
    • Zhang, Y.1    Xiong, Y.2
  • 32
    • 0032538293 scopus 로고    scopus 로고
    • The dermatomyositis-specific autoantigen Mi2 is a component of a complex containing histone deacetylase and nucleosome remodeling activities
    • Zhang, Y., LeRoy, G., Seelig, H.P., Lane, W.S. and Reinberg, D. (1998a) The dermatomyositis-specific autoantigen Mi2 is a component of a complex containing histone deacetylase and nucleosome remodeling activities. Cell, 95, 279-289.
    • (1998) Cell , vol.95 , pp. 279-289
    • Zhang, Y.1    LeRoy, G.2    Seelig, H.P.3    Lane, W.S.4    Reinberg, D.5
  • 33
    • 0032549711 scopus 로고    scopus 로고
    • ARF promotes MDM2 degradation and stabilizes p53: ARF-INK4a locus deletion impairs both the Rb and p53 tumor suppression pathways
    • Zhang, Y., Xiong, Y. and Yarbrough, W.G. (1998b) ARF promotes MDM2 degradation and stabilizes p53: ARF-INK4a locus deletion impairs both the Rb and p53 tumor suppression pathways. Cell, 92, 725-734.
    • (1998) Cell , vol.92 , pp. 725-734
    • Zhang, Y.1    Xiong, Y.2    Yarbrough, W.G.3


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