메뉴 건너뛰기




Volumn 18, Issue 3, 1998, Pages 1517-1524

The physical association of multiple molecular chaperone proteins with mutant p53 is altered by geldanamycin, an hsp90-binding agent

Author keywords

[No Author keywords available]

Indexed keywords

BINDING PROTEIN; CHAPERONE; GELDANAMYCIN; PROTEASOME; UBIQUITIN;

EID: 0031909866     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.18.3.1517     Document Type: Article
Times cited : (196)

References (40)
  • 1
    • 0029124132 scopus 로고
    • Microinjection of monoclonal antibody PAb421 into human SW480 colorectal carcinoma cells restores the transcriptional activation function to mutant p53
    • Abarzua, P., J. E. LoSardo, M. L. Gubler, and A. Neri. 1995. Microinjection of monoclonal antibody PAb421 into human SW480 colorectal carcinoma cells restores the transcriptional activation function to mutant p53. Cancer Res. 55:3490-3494.
    • (1995) Cancer Res. , vol.55 , pp. 3490-3494
    • Abarzua, P.1    LoSardo, J.E.2    Gubler, M.L.3    Neri, A.4
  • 2
    • 0027459198 scopus 로고
    • MDM2 expression is induced by wild type p53 activity
    • Barak, Y., T. Juven, R. Hafner, and M. Oren. 1993. MDM2 expression is induced by wild type p53 activity. EMDO J. 12:461-468.
    • (1993) EMDO J. , vol.12 , pp. 461-468
    • Barak, Y.1    Juven, T.2    Hafner, R.3    Oren, M.4
  • 3
    • 0029145215 scopus 로고
    • Geldanamycin selectively destabilizes and conformationally alters mutated p53
    • Blagosklonny, M. V., J. Toretsky, and L. Neckers. 1995. Geldanamycin selectively destabilizes and conformationally alters mutated p53. Oncogene 11:933-939.
    • (1995) Oncogene , vol.11 , pp. 933-939
    • Blagosklonny, M.V.1    Toretsky, J.2    Neckers, L.3
  • 4
    • 0029885423 scopus 로고    scopus 로고
    • Interactions of p60, a mediator of progesterone receptor assembly, with heat shock proteins hsp90 and hsp70
    • Chen, S., V. Prapapanich, R. A. Rimerman, B. Honore, and D. F. Smith. 1996. Interactions of p60, a mediator of progesterone receptor assembly, with heat shock proteins hsp90 and hsp70. Mol. Endocrinol. 10:682-693.
    • (1996) Mol. Endocrinol. , vol.10 , pp. 682-693
    • Chen, S.1    Prapapanich, V.2    Rimerman, R.A.3    Honore, B.4    Smith, D.F.5
  • 5
    • 0030988817 scopus 로고    scopus 로고
    • The p53 activation and apoptosis induced by DNA damage are reversibly inhibited by salicylate
    • Chernov, M. V., and G. Stark. 1997. The p53 activation and apoptosis induced by DNA damage are reversibly inhibited by salicylate. Oncogene 14:2503-2510.
    • (1997) Oncogene , vol.14 , pp. 2503-2510
    • Chernov, M.V.1    Stark, G.2
  • 6
    • 0002237472 scopus 로고
    • Cytosolic hsp70s of Saccharomyces cerevisiae: Roles in protein synthesis, protein translocation, proteolysis and regulation
    • R. I. Morimoto, A. Tissieres, and C. Georgopoulos (ed.). Cold Spring Harbor Laboratory Press, Plainview, N.Y.
    • Craig, E. A., B. K. Baxter, J. Becker, J. Halladay, and T. Ziegelhoffer. 1994. Cytosolic hsp70s of Saccharomyces cerevisiae: roles in protein synthesis, protein translocation, proteolysis and regulation, p. 31-52. In R. I. Morimoto, A. Tissieres, and C. Georgopoulos (ed.), The biology of heat shock proteins and molecular chaperones, vol. 26. Cold Spring Harbor Laboratory Press, Plainview, N.Y.
    • (1994) The Biology of Heat Shock Proteins and Molecular Chaperones , vol.26 , pp. 31-52
    • Craig, E.A.1    Baxter, B.K.2    Becker, J.3    Halladay, J.4    Ziegelhoffer, T.5
  • 7
    • 0026529909 scopus 로고
    • Immune response to p53 is dependent upon p53/HSP70 complexes in breast cancers
    • Davidoff, A. M., J. D. Iglehart, and J. R. Marks. 1992. Immune response to p53 is dependent upon p53/HSP70 complexes in breast cancers. Proc. Natl. Acad. Sci. USA 89:3439-3442.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 3439-3442
    • Davidoff, A.M.1    Iglehart, J.D.2    Marks, J.R.3
  • 8
    • 17544384391 scopus 로고    scopus 로고
    • Reconstitution of the steroid receptor-hsp90 heterocomplex assembly system of rabbit reticulocyte lysate
    • Dittmar, K. D., K. A. Hutchison, J. K. Owens-Grillo, and W. B. Pratt. 1996. Reconstitution of the steroid receptor-hsp90 heterocomplex assembly system of rabbit reticulocyte lysate. J. Biol. Chem. 271:12833-12839.
    • (1996) J. Biol. Chem. , vol.271 , pp. 12833-12839
    • Dittmar, K.D.1    Hutchison, K.A.2    Owens-Grillo, J.K.3    Pratt, W.B.4
  • 9
    • 0023959795 scopus 로고
    • Activating mutations lor transformation by p53 produce a gene prod-uct that forms an hsc70-p53 complex with an altered half-life
    • Finlay, C. A., P. W. Hinds, T.-H. Tan, D. Eliyahu, M. Oren, and A. J. Levine. 1988. Activating mutations lor transformation by p53 produce a gene prod-uct that forms an hsc70-p53 complex with an altered half-life. Mol. Cell. Biol. 8:531-539.
    • (1988) Mol. Cell. Biol. , vol.8 , pp. 531-539
    • Finlay, C.A.1    Hinds, P.W.2    Tan, T.-H.3    Eliyahu, D.4    Oren, M.5    Levine, A.J.6
  • 10
    • 0029852712 scopus 로고    scopus 로고
    • Molecular chaperone machines: Chaperone activities of the cyclophilin Cyp-40 and the steroid aporeceptor-associated protein p23
    • Freeman, B. C., D. O. Toft, and R. I. Morimoto. 1996. Molecular chaperone machines: chaperone activities of the cyclophilin Cyp-40 and the steroid aporeceptor-associated protein p23. Science 274:1718-1720.
    • (1996) Science , vol.274 , pp. 1718-1720
    • Freeman, B.C.1    Toft, D.O.2    Morimoto, R.I.3
  • 12
    • 0026779422 scopus 로고
    • Interaction of heat-shock protein 70 with p53 translated in vitro: Evidence for interaction with dimeric p53 and for a role in the regulation of p53 conformation
    • Hainaut, P., and J. Milner. 1992. Interaction of heat-shock protein 70 with p53 translated in vitro: evidence for interaction with dimeric p53 and for a role in the regulation of p53 conformation. EMBO J. 11:3513-3520.
    • (1992) EMBO J. , vol.11 , pp. 3513-3520
    • Hainaut, P.1    Milner, J.2
  • 13
    • 0025085667 scopus 로고
    • Different tumor-derived p53 mutants exhibit distinct biological activities
    • Halevy, O., D. Michalovitz, and M. Oren. 1990. Different tumor-derived p53 mutants exhibit distinct biological activities. Science 262:113-116.
    • (1990) Science , vol.262 , pp. 113-116
    • Halevy, O.1    Michalovitz, D.2    Oren, M.3
  • 14
    • 0028568315 scopus 로고
    • Cell cycle control and cancer
    • Hartwell, L. H., and M. B. Kastan. 1994. Cell cycle control and cancer. Science 266:1821-1828.
    • (1994) Science , vol.266 , pp. 1821-1828
    • Hartwell, L.H.1    Kastan, M.B.2
  • 15
    • 0030905284 scopus 로고    scopus 로고
    • Mdm-2 promotes the rapid degradation of p53
    • Haupt, Y., R. Maya, A. Kazaz, and M. Oren. 1997. Mdm-2 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
  • 16
    • 0025618980 scopus 로고
    • Mutant p53 DNA clones from human colon carcinomas cooperate with ras in transforming primary rat cells: A comparison of the "hot spot" mutant phenotypes
    • Hinds, P. W., C. A. Finlay, R. S. Quartin, S. J. Baker, E. R. Fearon, B. Vogelstein, and A. J. Levine. 1990. Mutant p53 DNA clones from human colon carcinomas cooperate with ras in transforming primary rat cells: a comparison of the "hot spot" mutant phenotypes. Cell Growth Differ. 1:571-580.
    • (1990) Cell Growth Differ. , vol.1 , pp. 571-580
    • Hinds, P.W.1    Finlay, C.A.2    Quartin, R.S.3    Baker, S.J.4    Fearon, E.R.5    Vogelstein, B.6    Levine, A.J.7
  • 17
    • 0027250493 scopus 로고
    • Activation of the cryptic DNA binding function of mutant forms of p53
    • Hupp, T. R., D. W. Meek, C. A. Midgley, and D. P. Lane. 1993. Activation of the cryptic DNA binding function of mutant forms of p53. Nucleic Acids Res. 21:3167-3174.
    • (1993) Nucleic Acids Res. , vol.21 , pp. 3167-3174
    • Hupp, T.R.1    Meek, D.W.2    Midgley, C.A.3    Lane, D.P.4
  • 18
    • 0029075280 scopus 로고
    • Binding of p23 and hsp90 during assembly with the progesterone receptor
    • Johnson, J. L., and D. O. Toft. 1995. Binding of p23 and hsp90 during assembly with the progesterone receptor. Mol. Endocrinol. 9:670-678.
    • (1995) Mol. Endocrinol. , vol.9 , pp. 670-678
    • Johnson, J.L.1    Toft, D.O.2
  • 19
    • 0030965946 scopus 로고    scopus 로고
    • Regulation of p53 stability by Mdm2
    • Kubbutat, M. H. G., S. N. Jones, and K. H. Vousden. 1997. Regulation of p53 stability by Mdm2. Science 387:299-303.
    • (1997) Science , vol.387 , pp. 299-303
    • Kubbutat, M.H.G.1    Jones, S.N.2    Vousden, K.H.3
  • 20
    • 0029964158 scopus 로고    scopus 로고
    • A reversible, p53-dependent G0/G1 cell cycle arrest induced by ribonucleotide depletion in the absence of detectable DNA damage
    • Linke, S. P., K. C. Clarkin, A. Di Leonardo, A. Tsou, and G. M. Wahl. 1996. A reversible, p53-dependent G0/G1 cell cycle arrest induced by ribonucleotide depletion in the absence of detectable DNA damage. Genes Dev. 10:934-947.
    • (1996) Genes Dev. , vol.10 , pp. 934-947
    • Linke, S.P.1    Clarkin, K.C.2    Di Leonardo, A.3    Tsou, A.4    Wahl, G.M.5
  • 21
    • 0030477012 scopus 로고    scopus 로고
    • Differential effects of phosphorylation of rat p53 on transactivation of promoters derived from different p53 responsive genes
    • Lohrum, M., and K. H. Scheidtmann. 1996. Differential effects of phosphorylation of rat p53 on transactivation of promoters derived from different p53 responsive genes. Oncogene 13:2527-2539.
    • (1996) Oncogene , vol.13 , pp. 2527-2539
    • Lohrum, M.1    Scheidtmann, K.H.2
  • 22
    • 0029952441 scopus 로고    scopus 로고
    • In vivo ubiquitination and proteasome-mediated degradation of p53
    • Maki, C. G., J. M. Huibregtse, and P. M. Howley. 1996. In vivo ubiquitination and proteasome-mediated degradation of p53. Cancer Res. 56:2649-2654.
    • (1996) Cancer Res. , vol.56 , pp. 2649-2654
    • Maki, C.G.1    Huibregtse, J.M.2    Howley, P.M.3
  • 23
    • 0026093164 scopus 로고
    • Cellular localization and cell cycle regulation by a temperature-sensitive p53 protein
    • Martinez, J., I. Georgoff, J. Martinez, and A. J. Levine. 1991. Cellular localization and cell cycle regulation by a temperature-sensitive p53 protein. Genes Dev. 5:151-159.
    • (1991) Genes Dev. , vol.5 , pp. 151-159
    • Martinez, J.1    Georgoff, I.2    Martinez, J.3    Levine, A.J.4
  • 24
    • 0030942625 scopus 로고    scopus 로고
    • Regulation of DNA binding and transactivation in p53 by nuclear localization and phosphorylation
    • Martinez, J. D., M. T. Craven, E. Joseloff, G. Milczarek, and G. T. Bowden. 1997. Regulation of DNA binding and transactivation in p53 by nuclear localization and phosphorylation. Oncogene 14:2511-2520.
    • (1997) Oncogene , vol.14 , pp. 2511-2520
    • Martinez, J.D.1    Craven, M.T.2    Joseloff, E.3    Milczarek, G.4    Bowden, G.T.5
  • 25
    • 0028455516 scopus 로고
    • Post-translational modification of p53
    • Meek, D. W. 1994. Post-translational modification of p53. Semin. Cancer Biol. 5:203-210.
    • (1994) Semin. Cancer Biol. , vol.5 , pp. 203-210
    • Meek, D.W.1
  • 26
    • 0025111068 scopus 로고
    • Conditional inhibition of transformation and of cell proliferation by a temperature-sensitive mutant of p53
    • Miehalovitz, D., O. Halevy, and M. Oren. 1990. Conditional inhibition of transformation and of cell proliferation by a temperature-sensitive mutant of p53. Cell 62:671-680.
    • (1990) Cell , vol.62 , pp. 671-680
    • Miehalovitz, D.1    Halevy, O.2    Oren, M.3
  • 28
    • 0026649648 scopus 로고
    • The mdm-2 oncogene product forms a complex with the p53 protein and inhibits p53-mediated transactivation
    • Momand, J., G. P. Zambetti, D. C. Olson, D. George, and A. J. Levine. 1992. The mdm-2 oncogene product forms a complex with the p53 protein and inhibits p53-mediated transactivation. Cell 69:1237-1245.
    • (1992) Cell , vol.69 , pp. 1237-1245
    • Momand, J.1    Zambetti, G.P.2    Olson, D.C.3    George, D.4    Levine, A.J.5
  • 29
    • 0030324952 scopus 로고    scopus 로고
    • A pathway of multi-chapcrone interactions common to diverse regulatory proteins: Estrogen receptor. Fes tyrosine kinase, heat shock transcription factor Hsf1 and the aryl hydrocarbon receptor
    • Nair, S. C., E. J. Toran, R. A. Rimerman, S. Hjermstad, T. E. Smithgall, and D. F. Smith. 1996. A pathway of multi-chapcrone interactions common to diverse regulatory proteins: estrogen receptor. Fes tyrosine kinase, heat shock transcription factor Hsf1 and the aryl hydrocarbon receptor. Cell Stress Chap. 1:237-250.
    • (1996) Cell Stress Chap. , vol.1 , pp. 237-250
    • Nair, S.C.1    Toran, E.J.2    Rimerman, R.A.3    Hjermstad, S.4    Smithgall, T.E.5    Smith, D.F.6
  • 30
    • 0027451956 scopus 로고
    • The role of heat shock proteins in regulating the function, folding and trafficking of the glucocorticoid receptor
    • Pratt, W. B. 1993. The role of heat shock proteins in regulating the function, folding and trafficking of the glucocorticoid receptor. J. Biol. Chem. 268:21455-21458.
    • (1993) J. Biol. Chem. , vol.268 , pp. 21455-21458
    • Pratt, W.B.1
  • 31
    • 0031444238 scopus 로고    scopus 로고
    • Identification and structural characterization of the ATP/ADP-hinding site in the hsp90 molecular chaperone
    • Prodromou, C., S. M. Roe, R. O'Brien, J. E. Ladbury, P. W. Piper, and L. H. Pearl. 1997. Identification and structural characterization of the ATP/ADP-hinding site in the hsp90 molecular chaperone. Cell 90:65-75.
    • (1997) Cell , vol.90 , pp. 65-75
    • Prodromou, C.1    Roe, S.M.2    O'Brien, R.3    Ladbury, J.E.4    Piper, P.W.5    Pearl, L.H.6
  • 33
    • 0028697474 scopus 로고
    • Multiple p53 protein isoforms and formation of oligomeric complexes with heat shock proteins hsp70 and hsp90 in the human mammary tumor, T47D, cell line
    • Selkirk, J. K., B. A. Merrick, B. L. Stackhouse, and C. He. 1994. Multiple p53 protein isoforms and formation of oligomeric complexes with heat shock proteins hsp70 and hsp90 in the human mammary tumor, T47D, cell line. Appl. Theor. Electrophoresis 4:11-18.
    • (1994) Appl. Theor. Electrophoresis , vol.4 , pp. 11-18
    • Selkirk, J.K.1    Merrick, B.A.2    Stackhouse, B.L.3    He, C.4
  • 34
    • 15844363948 scopus 로고    scopus 로고
    • Heat shock protein 84 forms a complex with mutant p53 protein predominantly within a cytoplasmic compartment of the cell
    • Sepehrnia, B., I. B. Paz, G. Dasgupta, and J. Momand. 1996. Heat shock protein 84 forms a complex with mutant p53 protein predominantly within a cytoplasmic compartment of the cell. J. Biol. Chem. 271:15084-15090.
    • (1996) J. Biol. Chem. , vol.271 , pp. 15084-15090
    • Sepehrnia, B.1    Paz, I.B.2    Dasgupta, G.3    Momand, J.4
  • 35
    • 0027484097 scopus 로고
    • Dynamics of heat shock protein 90-progesterone receptor binding and the disactivation loop model for steroid receptor complexes
    • Smith, D. F. 1993. Dynamics of heat shock protein 90-progesterone receptor binding and the disactivation loop model for steroid receptor complexes. Mol. Endocrinol. 7:1418-1429.
    • (1993) Mol. Endocrinol. , vol.7 , pp. 1418-1429
    • Smith, D.F.1
  • 36
    • 0028828273 scopus 로고
    • Progesterone receptor structure and function altered by geldanamycin, an Hsp90-binding agent
    • Smith, D. F., L. Whitesell, S. C. Nair, S. Chen, V. Prapapanich, and R. A. Rimerman. 1995. Progesterone receptor structure and function altered by geldanamycin, an Hsp90-binding agent. Mol. Cell. Biol. 15:6804-6812.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 6804-6812
    • Smith, D.F.1    Whitesell, L.2    Nair, S.C.3    Chen, S.4    Prapapanich, V.5    Rimerman, R.A.6
  • 37
    • 0031005361 scopus 로고    scopus 로고
    • Crystal structure of an hsp90-geldanamycin complex: Targeting of a protein chaperone by an anti-tumor agent
    • Stebbins, C. E., A. A. Russo, C. Schneider, N. Rosen, F. U. Hartl, and N. P. Pavletich. 1997. Crystal structure of an hsp90-geldanamycin complex: targeting of a protein chaperone by an anti-tumor agent. Cell 89:239-250.
    • (1997) Cell , vol.89 , pp. 239-250
    • Stebbins, C.E.1    Russo, A.A.2    Schneider, C.3    Rosen, N.4    Hartl, F.U.5    Pavletich, N.P.6
  • 38
    • 0029973294 scopus 로고    scopus 로고
    • Stable and specific binding of heat shock protein 90 by geldanamycin disrupts glucocorticoid receptor function in intact cells
    • Whitesell, L., and P. Cook. 1996. Stable and specific binding of heat shock protein 90 by geldanamycin disrupts glucocorticoid receptor function in intact cells. Mol. Endocrinol. 10:705-712.
    • (1996) Mol. Endocrinol. , vol.10 , pp. 705-712
    • Whitesell, L.1    Cook, P.2
  • 39
    • 0028064940 scopus 로고
    • Inhibition of heat shock protein HSP90-pp60v-src heteroprotein complex formation by benzoquinone ansamycins: Essential role for stress proteins in oncogenic transformation
    • Whitesell, L., E. G. Mimnaugh, B. De Costa, C. E. Myers, and L. M. Neckers. 1994. Inhibition of heat shock protein HSP90-pp60v-src heteroprotein complex formation by benzoquinone ansamycins: essential role for stress proteins in oncogenic transformation. Proc. Natl. Acad. Sci. USA 91:8324-8328.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 8324-8328
    • Whitesell, L.1    Mimnaugh, E.G.2    De Costa, B.3    Myers, C.E.4    Neckers, L.M.5
  • 40
    • 0030878952 scopus 로고    scopus 로고
    • Geldanamycin-stimulated destabilization of mutated p53 is mediated by the proteasome in vivo
    • Whitesell, L., P. Sutphin, W. G. An, T. Schulte, M. V. Blagosklonny, and L. Neckers. 1997. Geldanamycin-stimulated destabilization of mutated p53 is mediated by the proteasome in vivo. Oncogene 14:2809-2816.
    • (1997) Oncogene , vol.14 , pp. 2809-2816
    • Whitesell, L.1    Sutphin, P.2    An, W.G.3    Schulte, T.4    Blagosklonny, M.V.5    Neckers, L.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.