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Volumn 4, Issue 6, 1998, Pages 250-256

Keeping an old friend under control: Regulation of p53 stability

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN P53;

EID: 0031802921     PISSN: 13574310     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1357-4310(98)01260-X     Document Type: Review
Times cited : (98)

References (50)
  • 1
    • 0029670589 scopus 로고    scopus 로고
    • P53 in signaling checkpoint arrest or apoptosis
    • Bates S., Vosuden K.H. p53 in signaling checkpoint arrest or apoptosis. Curr. Opin. Genet. Dev. 6:1996;12-19.
    • (1996) Curr. Opin. Genet. Dev. , vol.6 , pp. 12-19
    • Bates, S.1    Vosuden, K.H.2
  • 2
    • 0021616838 scopus 로고
    • UV irradiation stimulates levels of p53 cellular tumor antigen in nontransformed mouse cells
    • Maltzman W., Czyzyk L. UV irradiation stimulates levels of p53 cellular tumor antigen in nontransformed mouse cells. Mol. Cell. Biol. 4:1984;1689-1694.
    • (1984) Mol. Cell. Biol. , vol.4 , pp. 1689-1694
    • Maltzman, W.1    Czyzyk, L.2
  • 3
    • 0030267239 scopus 로고    scopus 로고
    • Role of E6 and E7 oncoproteins in HPV-induced anogenital malignancies
    • Kubbutat M.H.G., Vousden K.H. Role of E6 and E7 oncoproteins in HPV-induced anogenital malignancies. Semin. Virol. 7:1996;295-304.
    • (1996) Semin. Virol. , vol.7 , pp. 295-304
    • Kubbutat, M.H.G.1    Vousden, K.H.2
  • 4
    • 0031058283 scopus 로고    scopus 로고
    • Antisense targeting of E6AP elevates p53 in HPV-infected cells but not in normal cells
    • Beer-Romero P., Glass S., Rolfe M. Antisense targeting of E6AP elevates p53 in HPV-infected cells but not in normal cells. Oncogene. 14:1997;595-602.
    • (1997) Oncogene , vol.14 , pp. 595-602
    • Beer-Romero, P.1    Glass, S.2    Rolfe, M.3
  • 5
    • 0031014946 scopus 로고    scopus 로고
    • Proteolytic cleavage of human p53 by calpain: A potential regulator of protein stability
    • Kubbutat M.H.G., Vousden K.H. Proteolytic cleavage of human p53 by calpain: a potential regulator of protein stability. Mol. Cell. Biol. 17:1997;460-468.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 460-468
    • Kubbutat, M.H.G.1    Vousden, K.H.2
  • 6
    • 0030987086 scopus 로고    scopus 로고
    • Proteolysis by calpains: A possible contribution to degradation of p53
    • Pariat M.et al. Proteolysis by calpains: a possible contribution to degradation of p53. Mol. Cell. Biol. 17:1997;2806-2815.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 2806-2815
    • Pariat, M.1
  • 7
    • 0030992491 scopus 로고    scopus 로고
    • On the involvement of calpains in the degradation of the tumor suppressor protein p53
    • Gonen H.et al. On the involvement of calpains in the degradation of the tumor suppressor protein p53. FEBS Lett. 406:1997;17-22.
    • (1997) FEBS Lett. , vol.406 , pp. 17-22
    • Gonen, H.1
  • 8
    • 0031452173 scopus 로고    scopus 로고
    • Structure and physiological function of calpains
    • Sorimachi H., Ishiura S., Suzuki K. Structure and physiological function of calpains. Biochem. J. 328:1997;721-732.
    • (1997) Biochem. J. , vol.328 , pp. 721-732
    • Sorimachi, H.1    Ishiura, S.2    Suzuki, K.3
  • 9
    • 0031027683 scopus 로고    scopus 로고
    • Inhibition of the growth of WI-38 fibroblasts by benzyloxycarbonyl-Leu-Leu-Tyr diazomethyl ketone: Evidence that cleavage of p53 by a calpain-like protease is necessary for G1 to S-phase transition
    • Zhang W., Lu Q., Xie Z.J., Mellgren R.L. Inhibition of the growth of WI-38 fibroblasts by benzyloxycarbonyl-Leu-Leu-Tyr diazomethyl ketone: evidence that cleavage of p53 by a calpain-like protease is necessary for G1 to S-phase transition. Oncogene. 14:1997;255-263.
    • (1997) Oncogene , vol.14 , pp. 255-263
    • Zhang, W.1    Lu, Q.2    Xie, Z.J.3    Mellgren, R.L.4
  • 10
    • 0029802282 scopus 로고    scopus 로고
    • Interaction with damaged DNA induces selective proteolytic cleavage of p53 to yield 40 kDa and 35 kDa fragments competent for sequence-specific DNA binding
    • Molinari M., Okorokov A.L., Milner J. Interaction with damaged DNA induces selective proteolytic cleavage of p53 to yield 40 kDa and 35 kDa fragments competent for sequence-specific DNA binding. Oncogene. 13:1996;2077-2086.
    • (1996) Oncogene , vol.13 , pp. 2077-2086
    • Molinari, M.1    Okorokov, A.L.2    Milner, J.3
  • 11
    • 0030826733 scopus 로고    scopus 로고
    • Induced N- And C-terminal cleavage of p53: A core fragment of p53, generated by interaction with damaged DNA, promotes cleavage of the N-terminus of full-length p53, whereas ssDNA induces C-terminal cleavage of p53
    • Okorokov A.L., Ponchel F., Milner J. Induced N- and C-terminal cleavage of p53: a core fragment of p53, generated by interaction with damaged DNA, promotes cleavage of the N-terminus of full-length p53, whereas ssDNA induces C-terminal cleavage of p53. EMBO J. 16:1997;6008-6017.
    • (1997) EMBO J. , vol.16 , pp. 6008-6017
    • Okorokov, A.L.1    Ponchel, F.2    Milner, J.3
  • 12
    • 0027459198 scopus 로고
    • Mdm2 expression is induced by wild type p53 activity
    • Barak Y., Juven T., Haffner R., Oren M. mdm2 expression is induced by wild type p53 activity. EMBO J. 12:1993;461-468.
    • (1993) EMBO J. , vol.12 , pp. 461-468
    • Barak, Y.1    Juven, T.2    Haffner, R.3    Oren, M.4
  • 13
    • 0026649648 scopus 로고
    • The mdm-2 oncogene product forms a complex with the p53 protein and inhibits p53-mediated transactivation
    • Momand J., Zambetti G.P., George D.L., Levine A.J. The mdm-2 oncogene product forms a complex with the p53 protein and inhibits p53-mediated transactivation. Cell. 69:1992;1237-1245.
    • (1992) Cell , vol.69 , pp. 1237-1245
    • Momand, J.1    Zambetti, G.P.2    George, D.L.3    Levine, A.J.4
  • 14
    • 0028823020 scopus 로고
    • Rescue of early embryonic lethality in mdm2-deficient mice by deletion of p53
    • Montes de Oca Luna R., Wagner D.S., Lozano G. Rescue of early embryonic lethality in mdm2-deficient mice by deletion of p53. Nature. 378:1995;203-206.
    • (1995) Nature , vol.378 , pp. 203-206
    • Montes De Oca Luna, R.1    Wagner, D.S.2    Lozano, G.3
  • 15
    • 0028834902 scopus 로고
    • Rescue of embryonic lethality in Mdm2-deficient mice by absence of p53
    • Jones S.N., Roe A.E., Donehower L.A., Bradley A. Rescue of embryonic lethality in Mdm2-deficient mice by absence of p53. Nature. 378:1995;206-208.
    • (1995) Nature , vol.378 , pp. 206-208
    • Jones, S.N.1    Roe, A.E.2    Donehower, L.A.3    Bradley, A.4
  • 16
  • 17
    • 0030905284 scopus 로고    scopus 로고
    • Mdm2 promotes the rapid degradation of p53
    • Haupt Y., Maya R., Kazaz A., Oren M. Mdm2 promotes the rapid degradation of p53. Nature. 387:1997;296-299.
    • (1997) Nature , vol.387 , pp. 296-299
    • Haupt, Y.1    Maya, R.2    Kazaz, A.3    Oren, M.4
  • 18
    • 0031282325 scopus 로고    scopus 로고
    • Design of a synthetic Mdm2-binding mini protein that activates the p53 response in vivo
    • Bottger A.et al. Design of a synthetic Mdm2-binding mini protein that activates the p53 response in vivo. Curr. Biol. 7:1997;860-869.
    • (1997) Curr. Biol. , vol.7 , pp. 860-869
    • Bottger, A.1
  • 19
    • 0027246716 scopus 로고
    • Regulation of p53 protein expression in human breast cancer cell lines
    • Vojtesek B., Lane D.P. Regulation of p53 protein expression in human breast cancer cell lines. J. Cell Sci. 105:1993;607-612.
    • (1993) J. Cell Sci. , vol.105 , pp. 607-612
    • Vojtesek, B.1    Lane, D.P.2
  • 20
    • 0030825813 scopus 로고    scopus 로고
    • P53 protein stability in tumour cells is not determined by mutation but is dependent on Mdm2 binding
    • Midgley C.A., Lane D.P. p53 protein stability in tumour cells is not determined by mutation but is dependent on Mdm2 binding. Oncogene. 15:1997;1179-1189.
    • (1997) Oncogene , vol.15 , pp. 1179-1189
    • Midgley, C.A.1    Lane, D.P.2
  • 21
    • 0030865801 scopus 로고    scopus 로고
    • MDM2 is a target of simian virus 40 in cellular transformation and during lytic infection
    • Henning W.et al. MDM2 is a target of simian virus 40 in cellular transformation and during lytic infection. J. Virol. 71:1997;7609-7618.
    • (1997) J. Virol. , vol.71 , pp. 7609-7618
    • Henning, W.1
  • 22
    • 0031435944 scopus 로고    scopus 로고
    • DNA damage induces phosphorylation of the amino terminus of p53
    • Siliciano J.D.et al. DNA damage induces phosphorylation of the amino terminus of p53. Genes Dev. 11:1997;3471-3481.
    • (1997) Genes Dev. , vol.11 , pp. 3471-3481
    • Siliciano, J.D.1
  • 23
    • 0030667702 scopus 로고    scopus 로고
    • DNA damage-induced phosphorylation of p53 alleviates inhibition by MDM2
    • Shieh S.Y., Ikeda M., Taya Y., Prives C. DNA damage-induced phosphorylation of p53 alleviates inhibition by MDM2. Cell. 91:1997;325-334.
    • (1997) Cell , vol.91 , pp. 325-334
    • Shieh, S.Y.1    Ikeda, M.2    Taya, Y.3    Prives, C.4
  • 24
    • 0030665146 scopus 로고    scopus 로고
    • Mdm-2 phosphorylation by DNA-dependent protein kinase prevents interaction with p53
    • Mayo L.D., Turchi J.J., Berberich S.J. Mdm-2 phosphorylation by DNA-dependent protein kinase prevents interaction with p53. Cancer Res. 57:1997;5013-5016.
    • (1997) Cancer Res. , vol.57 , pp. 5013-5016
    • Mayo, L.D.1    Turchi, J.J.2    Berberich, S.J.3
  • 25
    • 0029941651 scopus 로고    scopus 로고
    • P53-dependent cell cycle arrests are preserved in DNA-activated protein kinase-deficient mouse fibroblasts
    • Huang L., Clarkin K.C., Wahl G.M. p53-dependent cell cycle arrests are preserved in DNA-activated protein kinase-deficient mouse fibroblasts. Cancer Res. 56:1996;2940-2944.
    • (1996) Cancer Res. , vol.56 , pp. 2940-2944
    • Huang, L.1    Clarkin, K.C.2    Wahl, G.M.3
  • 26
    • 0031025079 scopus 로고    scopus 로고
    • DNA-dependent protein kinase is not required for accumulation of p53 of cell cycle arrest after DNA damage
    • Rathmell W.K.et al. DNA-dependent protein kinase is not required for accumulation of p53 of cell cycle arrest after DNA damage. Cancer Res. 57:1997;68-74.
    • (1997) Cancer Res. , vol.57 , pp. 68-74
    • Rathmell, W.K.1
  • 27
    • 0026496885 scopus 로고
    • A mammalian cell cycle checkpoint pathway utilizing p53 and GADD45 is defective in ataxia-telangiectasia
    • Kastan M.B.et al. A mammalian cell cycle checkpoint pathway utilizing p53 and GADD45 is defective in ataxia-telangiectasia. Cell. 71:1992;587-597.
    • (1992) Cell , vol.71 , pp. 587-597
    • Kastan, M.B.1
  • 28
    • 0029821651 scopus 로고    scopus 로고
    • Dual roles of ATM in the cellular response to radiation and in cell growth control
    • Xu Y., Baltimore D. Dual roles of ATM in the cellular response to radiation and in cell growth control. Genes Dev. 10:1996;2401-2410.
    • (1996) Genes Dev. , vol.10 , pp. 2401-2410
    • Xu, Y.1    Baltimore, D.2
  • 29
    • 0031583962 scopus 로고    scopus 로고
    • Oncoprotein MDM2 is a ubiquitin ligase E3 for tumor suppressor p53
    • Honda R., Tanaka H., Yasuda H. Oncoprotein MDM2 is a ubiquitin ligase E3 for tumor suppressor p53. FEBS Lett. 420:1997;25-27.
    • (1997) FEBS Lett. , vol.420 , pp. 25-27
    • Honda, R.1    Tanaka, H.2    Yasuda, H.3
  • 30
    • 0032549704 scopus 로고    scopus 로고
    • Arf, interacts with MDM2 and neutralizes MDM2's inhibition of p53
    • Arf, interacts with MDM2 and neutralizes MDM2's inhibition of p53. Cell. 92:1998;713-723.
    • (1998) Cell , vol.92 , pp. 713-723
    • Pomerantz, J.1
  • 31
    • 0032549711 scopus 로고    scopus 로고
    • ARF promotes MDM2 degradation and stabilizes p53: ARF-INK4a locus deletion impairs both the Rb and p53 tumor suppressor pathways
    • Zhang Y., Xiong Y., Yarbrough W.G. ARF promotes MDM2 degradation and stabilizes p53: ARF-INK4a locus deletion impairs both the Rb and p53 tumor suppressor pathways. Cell. 92:1998;725-734.
    • (1998) Cell , vol.92 , pp. 725-734
    • Zhang, Y.1    Xiong, Y.2    Yarbrough, W.G.3
  • 32
    • 0028845158 scopus 로고
    • Small peptides activate the latent sequence-specific DNA binding function of p53
    • Hupp T.R., Sparks A., Lane D.P. Small peptides activate the latent sequence-specific DNA binding function of p53. Cell. 83:1995;237-245.
    • (1995) Cell , vol.83 , pp. 237-245
    • Hupp, T.R.1    Sparks, A.2    Lane, D.P.3
  • 33
    • 0029055808 scopus 로고
    • Activation of p53 sequence-specific DNA binding by short single strands of DNA requires the p53 C-terminus
    • Jayaraman J., Prives C. Activation of p53 sequence-specific DNA binding by short single strands of DNA requires the p53 C-terminus. Cell. 81:1995;1021-1029.
    • (1995) Cell , vol.81 , pp. 1021-1029
    • Jayaraman, J.1    Prives, C.2
  • 34
    • 0029013273 scopus 로고
    • P53 and its 14 kDa C-terminal domain recognize primary DNA damage in the form of insertion/deletion mismatches
    • Lee S., Elenbaas B., Levine A., Griffith J. p53 and its 14 kDa C-terminal domain recognize primary DNA damage in the form of insertion/deletion mismatches. Cell. 81:1995;1013-1020.
    • (1995) Cell , vol.81 , pp. 1013-1020
    • Lee, S.1    Elenbaas, B.2    Levine, A.3    Griffith, J.4
  • 35
    • 0030900605 scopus 로고    scopus 로고
    • Identification of redox/repair protein Ref-1 as a potent activator of p53
    • Jayaraman L.et al. Identification of redox/repair protein Ref-1 as a potent activator of p53. Genes Dev. 11:1997;558-570.
    • (1997) Genes Dev. , vol.11 , pp. 558-570
    • Jayaraman, L.1
  • 36
    • 0029944241 scopus 로고    scopus 로고
    • A functionally inactive p53 protein in teratocarcinoma cells is activated by either DNA damage or cellular differentiation
    • Lutzker S.G., Levine A.J. A functionally inactive p53 protein in teratocarcinoma cells is activated by either DNA damage or cellular differentiation. Nat. Med. 2:1996;804-810.
    • (1996) Nat. Med. , vol.2 , pp. 804-810
    • Lutzker, S.G.1    Levine, A.J.2
  • 38
    • 0030935858 scopus 로고    scopus 로고
    • The tumor suppressor p53 is subject to both nuclear import and export, and both are fast, energy-dependent and lectin-inhibited
    • Middeler G.et al. The tumor suppressor p53 is subject to both nuclear import and export, and both are fast, energy-dependent and lectin-inhibited. Oncogene. 14:1997;1407-1417.
    • (1997) Oncogene , vol.14 , pp. 1407-1417
    • Middeler, G.1
  • 39
    • 0030048389 scopus 로고    scopus 로고
    • Cytoplasmic sequestration of wild-type p53 protein impairs the G1 checkpoint after DNA damage
    • Moll U.M.et al. Cytoplasmic sequestration of wild-type p53 protein impairs the G1 checkpoint after DNA damage. Mol. Cell. Biol. 16:1996;1126-1137.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 1126-1137
    • Moll, U.M.1
  • 40
    • 0032518917 scopus 로고    scopus 로고
    • Nucleo-cytoplasmic shuttling of the hdm2 oncoprotein regulates the levels of the p53 protein via a pathway used by the human immunodeficiency virus rev protein
    • Roth J.et al. Nucleo-cytoplasmic shuttling of the hdm2 oncoprotein regulates the levels of the p53 protein via a pathway used by the human immunodeficiency virus rev protein. EMBO J. 17:1998;554-564.
    • (1998) EMBO J. , vol.17 , pp. 554-564
    • Roth, J.1
  • 41
    • 0029766553 scopus 로고    scopus 로고
    • Translational regulation of human p53 gene expression
    • Fu L., Minden M.D., Benchimol S. Translational regulation of human p53 gene expression. EMBO J. 15:1996;4392-4401.
    • (1996) EMBO J. , vol.15 , pp. 4392-4401
    • Fu, L.1    Minden, M.D.2    Benchimol, S.3
  • 42
    • 0030983331 scopus 로고    scopus 로고
    • Participation of the human p53 3′UTR in translational repression and activation following gamma-irradiation
    • Fu L., Benchimol S. Participation of the human p53 3′UTR in translational repression and activation following gamma-irradiation. EMBO J. 16:1997;4117-4125.
    • (1997) EMBO J. , vol.16 , pp. 4117-4125
    • Fu, L.1    Benchimol, S.2
  • 43
    • 0029115918 scopus 로고
    • Negative feedback regulation of wild-type p53 biosynthesis
    • Mosner J.et al. Negative feedback regulation of wild-type p53 biosynthesis. EMBO J. 14:1995;4442-4449.
    • (1995) EMBO J. , vol.14 , pp. 4442-4449
    • Mosner, J.1
  • 44
    • 0025648762 scopus 로고
    • Germ-line transmission of a mutated p53 gene in a cancer-prone family with Li-Fraumeni syndrome
    • Srivistava S.et al. Germ-line transmission of a mutated p53 gene in a cancer-prone family with Li-Fraumeni syndrome. Nature. 348:1990;747-749.
    • (1990) Nature , vol.348 , pp. 747-749
    • Srivistava, S.1
  • 45
    • 0025633582 scopus 로고
    • Germ line p53 mutations in a familial syndrome of breast cancer, sarcomas, and other neoplasias
    • Malkin D.et al. Germ line p53 mutations in a familial syndrome of breast cancer, sarcomas, and other neoplasias. Science. 250:1990;1233-1238.
    • (1990) Science , vol.250 , pp. 1233-1238
    • Malkin, D.1
  • 46
    • 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.et al. Restoration of the growth suppression function of mutant p53 by a synthetic peptide derived from the p53 C-terminal domain. Nat. Med. 3:1997;632-638.
    • (1997) Nat. Med. , vol.3 , pp. 632-638
    • Selivanova, G.1
  • 47
    • 0027980357 scopus 로고
    • Interaction of p53 with MDM2 is independent of E6 and does not mediate wild type transformation suppressor function
    • Marston N.J., Crook T., Vousden K.H. Interaction of p53 with MDM2 is independent of E6 and does not mediate wild type transformation suppressor function. Oncogene. 9:1994;2707-2716.
    • (1994) Oncogene , vol.9 , pp. 2707-2716
    • Marston, N.J.1    Crook, T.2    Vousden, K.H.3
  • 48
    • 0026694826 scopus 로고
    • Two distinct mechanisms alter p53 in breast cancer: Mutation and nuclear exclusion
    • Moll U.M., Riou G., Levine A.J. Two distinct mechanisms alter p53 in breast cancer: mutation and nuclear exclusion. Proc. Natl. Acad. Sci. U. S. A. 89:1992;7262-7266.
    • (1992) Proc. Natl. Acad. Sci. U. S. A. , vol.89 , pp. 7262-7266
    • Moll, U.M.1    Riou, G.2    Levine, A.J.3
  • 49
    • 0026740449 scopus 로고
    • Amplification of a gene encoding a p53-associated protein in human sarcomas
    • Oliner J.D.et al. Amplification of a gene encoding a p53-associated protein in human sarcomas. Nature. 358:1992;80-83.
    • (1992) Nature , vol.358 , pp. 80-83
    • Oliner, J.D.1
  • 50
    • 0026530432 scopus 로고
    • Clonal p53 mutation in primary cervical cancer: Association with human-papillomavirus-negative tumours
    • Crook T.et al. Clonal p53 mutation in primary cervical cancer: association with human-papillomavirus-negative tumours. Lancet. 339:1992;1070-1073.
    • (1992) Lancet , vol.339 , pp. 1070-1073
    • Crook, T.1


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