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Volumn 57, Issue 1, 2000, Pages 82-92

Role of heat shock protein 90 dissociation in mediating agonist-induced activation of the aryl hydrocarbon receptor

Author keywords

[No Author keywords available]

Indexed keywords

AROMATIC HYDROCARBON RECEPTOR; HEAT SHOCK PROTEIN 90; MOLYBDATE SODIUM;

EID: 0033970688     PISSN: 0026895X     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (99)

References (40)
  • 1
    • 0028858813 scopus 로고
    • Distinct roles of the molecular chaperone HSp90 in modulating dioxin receptor function via the basic helix-loop-helix and PAS domains
    • Antonsson C, Whitelaw ML, McGuire J, Gustafsson J-A and Poellinger L (1995) Distinct roles of the molecular chaperone HSP90 in modulating dioxin receptor function via the basic helix-loop-helix and PAS domains. Mol Cell Biol 15:756-765.
    • (1995) Mol Cell Biol , vol.15 , pp. 756-765
    • Antonsson, C.1    Whitelaw, M.L.2    McGuire, J.3    Gustafsson, J.-A.4    Poellinger, L.5
  • 2
    • 0030897705 scopus 로고    scopus 로고
    • Ligand-dependent interaction of the aryl hydrocarbon receptor with a novel immunophilin homolog in vivo
    • Carver L and Bradfield C (1997) Ligand-dependent interaction of the aryl hydrocarbon receptor with a novel immunophilin homolog in vivo. J Biol Chem 272:11452-11456.
    • (1997) J Biol Chem , vol.272 , pp. 11452-11456
    • Carver, L.1    Bradfield, C.2
  • 3
    • 0028077887 scopus 로고
    • The 90-kDa heat shock protein in essential for AH receptor signaling in a yeast expression system
    • Carver L, Jackiw V and Bradfield C (1994) The 90-kDa heat shock protein in essential for AH receptor signaling in a yeast expression system. J Biol Chem 269:30109-30112.
    • (1994) J Biol Chem , vol.269 , pp. 30109-30112
    • Carver, L.1    Jackiw, V.2    Bradfield, C.3
  • 4
    • 0027970550 scopus 로고
    • Subunit composition of the heteromeric cytosolic aryl hydrocarbon receptor complex
    • Chen H-S and Perdew G (1994) Subunit composition of the heteromeric cytosolic aryl hydrocarbon receptor complex. J Biol Chem 269:27554-27558.
    • (1994) J Biol Chem , vol.269 , pp. 27554-27558
    • Chen, H.-S.1    Perdew, G.2
  • 5
    • 0031543526 scopus 로고    scopus 로고
    • The AH receptor is a sensitive target of geldanamycin-induced protein turnover
    • Chen H-S, Singh S and Perdew G (1997) The AH receptor is a sensitive target of geldanamycin-induced protein turnover. Arch Biochem Biophys 348:190-198.
    • (1997) Arch Biochem Biophys , vol.348 , pp. 190-198
    • Chen, H.-S.1    Singh, S.2    Perdew, G.3
  • 6
    • 0023654310 scopus 로고
    • The receptor for 2,3,7,8-tetrachloro-dibenzo-p-dioxin in the mouse hepatoma cell line Hepa 1c1c7
    • Cuthill S, Poellinger L and Gustafsson J-A (1987) The receptor for 2,3,7,8-tetrachloro-dibenzo-p-dioxin in the mouse hepatoma cell line Hepa 1c1c7. J Biol Chem 262:3477-3481.
    • (1987) J Biol Chem , vol.262 , pp. 3477-3481
    • Cuthill, S.1    Poellinger, L.2    Gustafsson, J.-A.3
  • 7
    • 0025021719 scopus 로고
    • The binding of transformed aromatic hydrocarbon receptor (AH) receptor to its DNA recognition site is not affected by metal depletion
    • Denison M and Deal R (1990) The binding of transformed aromatic hydrocarbon receptor (AH) receptor to its DNA recognition site is not affected by metal depletion. Mol Cell Endocrinol 69:51-57.
    • (1990) Mol Cell Endocrinol , vol.69 , pp. 51-57
    • Denison, M.1    Deal, R.2
  • 8
    • 0022847049 scopus 로고
    • Hepatic AH receptor for 2,3,7,8-tetrachloro-dibenzo-p-dioxin
    • Denison M, Vella L and Okey A (1986) Hepatic AH receptor for 2,3,7,8-tetrachloro-dibenzo-p-dioxin. J Biol Chem 261:10189-10195.
    • (1986) J Biol Chem , vol.261 , pp. 10189-10195
    • Denison, M.1    Vella, L.2    Okey, A.3
  • 10
    • 0027169125 scopus 로고
    • In vitro analysis of AH receptor domains involved in ligand-activated DNA recognition
    • Dolwick K, Swanson H and Bradfield C (1993b) In vitro analysis of AH receptor domains involved in ligand-activated DNA recognition. Proc Natl Acad Sci USA 90:8566-8570.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 8566-8570
    • Dolwick, K.1    Swanson, H.2    Bradfield, C.3
  • 11
  • 12
    • 0028858097 scopus 로고
    • Identification of functional domains of the aryl hydrocarbon receptor
    • Fukunaga B, Probst M, Reisz-Porzasz S and Hankinson O (1995) Identification of functional domains of the aryl hydrocarbon receptor. J Biol Chem 270:29270-29278.
    • (1995) J Biol Chem , vol.270 , pp. 29270-29278
    • Fukunaga, B.1    Probst, M.2    Reisz-Porzasz, S.3    Hankinson, O.4
  • 13
    • 0032519879 scopus 로고    scopus 로고
    • Prolonged depletion of AH receptor without alteration of receptor mRNA levels after treatment of cells in culture with 2,3,7,8-tetrachloro-dibenzo-p-dioxin
    • Giannone J, Li W, Probst M and Okey A (1998) Prolonged depletion of AH receptor without alteration of receptor mRNA levels after treatment of cells in culture with 2,3,7,8-tetrachloro-dibenzo-p-dioxin. Biochem Pharmacol 55:489-497.
    • (1998) Biochem Pharmacol , vol.55 , pp. 489-497
    • Giannone, J.1    Li, W.2    Probst, M.3    Okey, A.4
  • 14
    • 0029789568 scopus 로고    scopus 로고
    • Functional interference between hypoxia and dioxin signal transduction pathways: Competition for recruitment of the Arnt transcription factor
    • Gradin K, McGuire J, Wenger R, Kvietikova I, Whitelaw M, Toftgard R, Tora L, Gassmann M and Poellinger L (1996) Functional interference between hypoxia and dioxin signal transduction pathways: Competition for recruitment of the Arnt transcription factor Mol Cell Biol 16:5221-5331
    • (1996) Mol Cell Biol , vol.16 , pp. 5221-5331
    • Gradin, K.1    McGuire, J.2    Wenger, R.3    Kvietikova, I.4    Whitelaw, M.5    Toftgard, R.6    Tora, L.7    Gassmann, M.8    Poellinger, L.9
  • 15
    • 0033555947 scopus 로고    scopus 로고
    • Nucleocytoplasmic trafficking of steroid-free glucocorticoid receptor
    • Hache R, Tse R, Reich T, Savory J and Lefebvre Y (1999) Nucleocytoplasmic trafficking of steroid-free glucocorticoid receptor. J Biol Chem 274:1432-1439.
    • (1999) J Biol Chem , vol.274 , pp. 1432-1439
    • Hache, R.1    Tse, R.2    Reich, T.3    Savory, J.4    Lefebvre, Y.5
  • 16
    • 0028987872 scopus 로고
    • The aryl hydrocarbon receptor complex
    • Hankinson O (1995) The aryl hydrocarbon receptor complex. Annu Rev Pharmicol Toxicol 35:307-340.
    • (1995) Annu Rev Pharmicol Toxicol , vol.35 , pp. 307-340
    • Hankinson, O.1
  • 17
    • 0027304728 scopus 로고
    • Transformation of the aryl hydrocarbon receptor to a DNA-binding form is accompanied by release of the 90 kDa heat-shock protein and increased affinity for 2,3,7,8-tetrachloro-dibenzo-p-dioxin
    • Henry EC and Gasiewicz TA (1993) Transformation of the aryl hydrocarbon receptor to a DNA-binding form is accompanied by release of the 90 kDa heat-shock protein and increased affinity for 2,3,7,8-tetrachloro-dibenzo-p-dioxin. Biochem J 294:95-101.
    • (1993) Biochem J , vol.294 , pp. 95-101
    • Henry, E.C.1    Gasiewicz, T.A.2
  • 18
    • 0032579265 scopus 로고    scopus 로고
    • Nuclear localization and export signals of the human aryl hydrocarbon receptor
    • Ikuta T, Eguchi H, Tachibana T, Yoneda Y and Kawajiri K (1998) Nuclear localization and export signals of the human aryl hydrocarbon receptor. J Biol Chem 273:2895-2904.
    • (1998) J Biol Chem , vol.273 , pp. 2895-2904
    • Ikuta, T.1    Eguchi, H.2    Tachibana, T.3    Yoneda, Y.4    Kawajiri, K.5
  • 19
    • 0028156864 scopus 로고
    • In vivo functional protein-protein interaction: Nuclear-targeted hsp90 shifts cytoplasmic steroid receptor from cytoplasm to nucleus
    • Kang K, Devin J, Cadepond F, Jibard N, Guichon-Mantel A, Baulieu E and Catelli M (1994) In vivo functional protein-protein interaction: Nuclear-targeted hsp90 shifts cytoplasmic steroid receptor from cytoplasm to nucleus. Proc Natl Acad Sci USA 91:340-344.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 340-344
    • Kang, K.1    Devin, J.2    Cadepond, F.3    Jibard, N.4    Guichon-Mantel, A.5    Baulieu, E.6    Catelli, M.7
  • 20
    • 0031002895 scopus 로고    scopus 로고
    • A novel cytoplasmic protein that interacts with the AH receptor, contains tetratricopeptide repeat motifs, and augments the transcriptional response to 2,3,7,8-tetrachloro-dibenzo-p-dioxin
    • Ma Q and Whitlock J (1997) A novel cytoplasmic protein that interacts with the AH receptor, contains tetratricopeptide repeat motifs, and augments the transcriptional response to 2,3,7,8-tetrachloro-dibenzo-p-dioxin. J Biol Chem 272:8878-8884.
    • (1997) J Biol Chem , vol.272 , pp. 8878-8884
    • Ma, Q.1    Whitlock, J.2
  • 21
    • 0023617544 scopus 로고
    • AH receptor in human placenta: Stabilization by molybdate and characterization of binding of 2,3,7,8-tetrachbro-dibenzo-p-dioxin
    • Manchester D, Gordon S, Golas C, Roberts E and Okey A (1987) AH receptor in human placenta: Stabilization by molybdate and characterization of binding of 2,3,7,8-tetrachbro-dibenzo-p-dioxin. Cancer Res 47:4861-4868.
    • (1987) Cancer Res , vol.47 , pp. 4861-4868
    • Manchester, D.1    Gordon, S.2    Golas, C.3    Roberts, E.4    Okey, A.5
  • 22
    • 0029611034 scopus 로고
    • The basic helix-loop-helix/PAS factor sim is associated with hsp90, implications for regulation by interaction with partner factors
    • McGuire J, Coumailleau P, Whitelaw M, Gustafsson J and Poellinger L (1995) The basic helix-loop-helix/PAS factor Sim is associated with hsp90, Implications for regulation by interaction with partner factors. J Biol Chem 270:31353-31357.
    • (1995) J Biol Chem , vol.270 , pp. 31353-31357
    • McGuire, J.1    Coumailleau, P.2    Whitelaw, M.3    Gustafsson, J.4    Poellinger, L.5
  • 23
    • 0027213375 scopus 로고
    • Single-minded regulation of genes in the embryonic midline of the Drosophila central nervous system
    • Muralidhar M, Callahan C and Thomas J (1993) Single-minded regulation of genes in the embryonic midline of the Drosophila central nervous system. Mech Dev 41:129-138.
    • (1993) Mech Dev , vol.41 , pp. 129-138
    • Muralidhar, M.1    Callahan, C.2    Thomas, J.3
  • 24
    • 0028846193 scopus 로고
    • Sequence and characterization of a coactivator for the steroid hormone receptor superfamily
    • Onate S, Tsai S, Tsai M-J and O'Malley B (1995) Sequence and characterization of a coactivator for the steroid hormone receptor superfamily. Science (Wash DC) 270:1354-1357.
    • (1995) Science (Wash DC) , vol.270 , pp. 1354-1357
    • Onate, S.1    Tsai, S.2    Tsai, M.-J.3    O'Malley, B.4
  • 25
    • 0026332694 scopus 로고
    • Comparison of the nuclear and cytosolic forms of the AH receptor from Hepa 1c1c7 cells: Charge heterogeneity and ATP binding properties
    • Perdew G (1991) Comparison of the nuclear and cytosolic forms of the AH receptor from Hepa 1c1c7 cells: Charge heterogeneity and ATP binding properties. Arch Biochem Biophys 291:284-290.
    • (1991) Arch Biochem Biophys , vol.291 , pp. 284-290
    • Perdew, G.1
  • 26
    • 0030015845 scopus 로고    scopus 로고
    • Mapping the 90 kDa heat shock protein binding region of the AH receptor
    • Perdew G and Bradfield C (1996) Mapping the 90 kDa heat shock protein binding region of the AH receptor. Biochem Mol Biol Int 39:589-593.
    • (1996) Biochem Mol Biol Int , vol.39 , pp. 589-593
    • Perdew, G.1    Bradfield, C.2
  • 27
    • 0030925683 scopus 로고    scopus 로고
    • Steroid receptor interactions with heat shock protein and immunophilin chaperones
    • Pratt W and Toft D (1997) Steroid receptor interactions with heat shock protein and immunophilin chaperones. Endocrine Rev 18:306-360.
    • (1997) Endocrine Rev , vol.18 , pp. 306-360
    • Pratt, W.1    Toft, D.2
  • 28
    • 0029986534 scopus 로고    scopus 로고
    • The aryl-hydrocarbon receptor, but not the aryl-hydrocarbon receptor nuclear translocator protein is rapidly depleted in hepatic and non-hepatic culture cells exposed to 2,3,7,8-tetrachlorodibenzo-p-dioxin
    • Pollenz R (1996) The aryl-hydrocarbon receptor, but not the aryl-hydrocarbon receptor nuclear translocator protein is rapidly depleted in hepatic and non-hepatic culture cells exposed to 2,3,7,8-tetrachlorodibenzo-p-dioxin. Mol Pharmacol 49: 391-398.
    • (1996) Mol Pharmacol , vol.49 , pp. 391-398
    • Pollenz, R.1
  • 29
    • 0028207310 scopus 로고
    • The aryl hydrocarbon receptor and aryl hydrocarbon receptor nuclear translocator protein show distinct subcellular localizations in Hepa 1c1c7 cells by immunofluorescence microscopy
    • Pollenz R, Sattler C and Poland A (1994) The aryl hydrocarbon receptor and aryl hydrocarbon receptor nuclear translocator protein show distinct subcellular localizations in Hepa 1c1c7 cells by immunofluorescence microscopy. Mol Pharmacol 45:428-438.
    • (1994) Mol Pharmacol , vol.45 , pp. 428-438
    • Pollenz, R.1    Sattler, C.2    Poland, A.3
  • 30
    • 0026631538 scopus 로고
    • Dual roles of the 90 kDa heat shock protein in modulating functional activities of the dioxin receptor
    • Pongratz I, Mason G and Poellinger L (1992) Dual roles of the 90 kDa heat shock protein in modulating functional activities of the dioxin receptor. J Biol Chem 267:13728-13734.
    • (1992) J Biol Chem , vol.267 , pp. 13728-13734
    • Pongratz, I.1    Mason, G.2    Poellinger, L.3
  • 31
    • 0025159425 scopus 로고
    • Characterization of the AH receptor mediating aryl hydrocarbon hydroxylase induction in the human liver cell line HepG2
    • Roberts E, Johnson K, Harper P and Okey A (1990) Characterization of the AH receptor mediating aryl hydrocarbon hydroxylase induction in the human liver cell line HepG2. Arch Biochem Biophys 276:442-450.
    • (1990) Arch Biochem Biophys , vol.276 , pp. 442-450
    • Roberts, E.1    Johnson, K.2    Harper, P.3    Okey, A.4
  • 32
    • 0010417886 scopus 로고    scopus 로고
    • Responsiveness of the adult male rat reproductive tract to 2,3,7,8-tetrachloro-dibenzo-p-dioxin exposure: Ah receptor and ARNT expression, CYP1A1 induction, and Ah receptor down-regulation
    • Roman B, Pollenz R and Peterson R (1998) Responsiveness of the adult male rat reproductive tract to 2,3,7,8-tetrachloro-dibenzo-p-dioxin exposure: Ah receptor and ARNT expression, CYP1A1 induction, and Ah receptor down-regulation. Toxicol Appl Pharmacol 150:228-239.
    • (1998) Toxicol Appl Pharmacol , vol.150 , pp. 228-239
    • Roman, B.1    Pollenz, R.2    Peterson, R.3
  • 33
    • 0027980828 scopus 로고
    • Structural and functional aspects of basic helix-loop-helix protein folding by heat-shock protein 90
    • Shue G and Kohtz D (1994) Structural and functional aspects of basic helix-loop-helix protein folding by heat-shock protein 90. J Biol Chem 269:2707-2711.
    • (1994) J Biol Chem , vol.269 , pp. 2707-2711
    • Shue, G.1    Kohtz, D.2
  • 34
    • 0032549524 scopus 로고    scopus 로고
    • Identification and characterization of specific DNA-binding complexes containing members of the Myc/Max/Mad network of transcriptional regulators
    • Sommer A, Bousset K, Kremmer E, Austen M and Luscher B (1998) Identification and characterization of specific DNA-binding complexes containing members of the Myc/Max/Mad network of transcriptional regulators. J Biol Chem 273:6632-6642.
    • (1998) J Biol Chem , vol.273 , pp. 6632-6642
    • Sommer, A.1    Bousset, K.2    Kremmer, E.3    Austen, M.4    Luscher, B.5
  • 35
    • 0028865103 scopus 로고
    • DNA binding specificities and pairing rules of the AH receptor, ARNT, and SIM proteins
    • Swanson H, Chan W and Bradfield C (1995) DNA binding specificities and pairing rules of the AH receptor, ARNT, and SIM proteins. J Biol Chem 270:26292-26302.
    • (1995) J Biol Chem , vol.270 , pp. 26292-26302
    • Swanson, H.1    Chan, W.2    Bradfield, C.3
  • 38
    • 0027403810 scopus 로고
    • Ligand-dependent recruitment of the ARNT coregulator determines DNA recognition by the dioxin receptor
    • Whitelaw M, Pongratz I, Wilhelmsson A, Gustafsson J-A and Poellinger L (1993) Ligand-dependent recruitment of the ARNT coregulator determines DNA recognition by the dioxin receptor. Mol Cell Biol 13:2504-2514.
    • (1993) Mol Cell Biol , vol.13 , pp. 2504-2514
    • Whitelaw, M.1    Pongratz, I.2    Wilhelmsson, A.3    Gustafsson, J.-A.4    Poellinger, L.5
  • 39
    • 0025157272 scopus 로고
    • The specific DNA binding activity of the dioxin receptor is modulated by the 90 kd heat shock protein
    • Wilhelmsson A, Cuthill S, Denis M, Wikstrom A, Gustafsson J-A and Poellinger L (1990) The specific DNA binding activity of the dioxin receptor is modulated by the 90 kd heat shock protein. EMBO J 9:69-76.
    • (1990) EMBO J , vol.9 , pp. 69-76
    • Wilhelmsson, A.1    Cuthill, S.2    Denis, M.3    Wikstrom, A.4    Gustafsson, J.-A.5    Poellinger, L.6
  • 40
    • 0030046766 scopus 로고    scopus 로고
    • Assessment of glucocorticoid receptor-heat shock protein 90 interactions in vivo during nucleocytoplasmic trafficking
    • Yang J and DeFranco DB (1996) Assessment of glucocorticoid receptor-heat shock protein 90 interactions in vivo during nucleocytoplasmic trafficking. Mol Endocrinol 10:3-13.
    • (1996) Mol Endocrinol , vol.10 , pp. 3-13
    • Yang, J.1    Defranco, D.B.2


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