A Cellular Factor Stimulates Ligand-Dependent Release of hsp90 from the Basic Helix-Loop-Helix Dioxin Receptor

REFERENCES

• Ayer, D. E., L. Kretzner, and R. N. Eisenman. 1993. Mad: a heterodimeric partner for Max that antagonizes Myc transcriptional activity. Cell 72:211–222.
   PubMed Web of Science ®Google Scholar
• Beato, M. 1989. Gene regulation by steroid hormones. Cell 56:335–344.
   PubMed Web of Science ®Google Scholar
• Berghard, A., K. Gradin, I. Pongratz, M. Whitelaw, and L. Poellinger. 1993. Cross-coupling of signal transduction pathways: the dioxin receptor mediates induction of cytochrome P-450IA1 expression via a protein kinase C-dependent mechanism. Mol. Cell. Biol. 13:677–689.
   PubMed Web of Science ®Google Scholar
• Bresnick, E. H., F. C. Dalman, E. R. Sanchez, and W. B. Pratt. 1989. Evidence that the 90-kDa heat shock protein is necessary for the steroid binding conformation of the L cell glucocorticoid receptor. J. Biol. Chem. 264:4992–4997.
   PubMed Web of Science ®Google Scholar
• Burbach, K. M., A. Poland, and C. A. Bradfield. 1992. Cloning of the Ah receptor cDNA reveals a distinctive ligand-activated transcription factor. Proc. Natl. Acad. Sci. USA 89:8185–8189.
   PubMed Web of Science ®Google Scholar
• Cuthill, S., A. Wilhelmsson, and L. Poellinger. 1991. Role of the ligand in intracellular receptor function: receptor affinity determines activation in vitro of the latent dioxin receptor to a DNA-binding form. Mol. Cell. Biol. 11:401–411.
   PubMedGoogle Scholar
• Dahmer, M. K., P. R. Housley, and W. B. Pratt. 1984. Effects of molybdate and endogenous inhibitors on steroid receptor inacti-vation, transformation, and translocation. Annu. Rev. Physiol. 46:67–81.
   PubMedGoogle Scholar
• Dalman, F. C., E. H. Bresnick, P. D. Patel, G. H. Perdew, S. J. Watson, and W. B. Pratt. 1989. Direct evidence that the glucocorticoid receptor binds to hsp90 at or near the termination of receptor translation in vitro. J. Biol. Chem. 264:19815–19821.
   PubMedGoogle Scholar
• Dalman, F. C., L. C. Scherrer, L. P. Taylor, H. Akil, and W. B. Pratt. 1991. Localization of the 90-kDa heat shock protein binding site within the hormone binding domain of the glucocorticoid receptor by peptide competition. J. Biol. Chem. 266:3482–3490.
   PubMedGoogle Scholar
• Denis, M., S. Cuthill, A.-C. Wikstrom, L. Poellinger, and J.-A. Gustafsson. 1988. Association of the dioxin receptor with the mr 90,000 heat shock protein: a structural kinship with the glucocorticoid receptor. Biochem. Biophys. Res. Commun. 155:801–807.
   PubMedGoogle Scholar
• Denis, M., and J.-A. Gustafsson. 1989. Translation of glucocorticoid receptor mRNA in vitro yields a non-activated protein. J. Biol. Chem. 264:6005–6008.
   PubMedGoogle Scholar
• Denis, M., L. Poellinger, A.-C. Wikstrom, and J.-A. Gustafsson. 1988. Requirement of hormone for thermal conversion of the glucocorticoid receptor to a DNA-binding state. Nature (London) 333:686–688.
   PubMedGoogle Scholar
• Denis, M., A.-C. Wikstrom, and J.-A. Gustafsson. 1987. The molybdate-stabilized non-activated glucocorticoid receptor contains a dimer of Mr 90,000 non-hormone binding protein. J. Biol. Chem. 262:11803–11806.
   PubMedGoogle Scholar
• Denison, M. S., J. M. Fisher, and J. J. Whitlock. 1988. Inducible, receptor-dependent protein-DNA interactions at a dioxin-respon-sive transcriptional enhancer. Proc. Natl. Acad. Sci. USA 85:2528–2532.
   PubMed Web of Science ®Google Scholar
• Denison, M. S., and E. F. Yao. 1991. Characterization of the interaction of transformed rat hepatic cytosolic Ah receptor with a dioxin responsive transcriptional enhancer. Arch. Biochem. Biophys. 284:158–166.
   PubMedGoogle Scholar
• Eilers, M., D. Picard, K. R. Yamamoto, and J. M. Bishop. 1989. Chimaeras of Myc oncoprotein and steroid receptors cause hormone-dependent transformation of cells. Nature (London) 340:66–68.
   PubMedGoogle Scholar
• Ema, M., K. Sogawa, Y. Watanabe, Y. Chujoh, N. Matsushita, O. Gotoh, Y. Funae, and Y. Fujii-Kuriyama. 1992. cDNA cloning and structure of mouse putative Ah receptor. Biochem. Biophys. Res. Commun. 184:246–253.
   PubMed Web of Science ®Google Scholar
• Ferré-D'Amaré, A. R., G. C. Prendergast, E. B. Ziff, and S. K. Burley. 1993. Recognition by Max of its cognate DNA through a dimeric b/HLH/Z domain. Nature (London) 363:38–45.
   PubMed Web of Science ®Google Scholar
• Fujisawa-Sehara, A., M. Yamane, and Y. Fujii-Kuriyama. 1988. A DNA-binding factor specific for xenobiotic responsive elements of P-450c gene exists as a cryptic form in cytoplasm: its possible translocation to nucleus. Proc. Natl. Acad. Sci. USA 85:5859–5863.
   PubMed Web of Science ®Google Scholar
• Gasiewicz, T. A., and R. A. Neal. 1982. The examination and quantification of tissue cytosolic receptors for 2,3,7,8-tetrachloro-dibenzo-p-dioxin using hydroxylapatite. Anal. Biochem. 124:1–11.
   PubMed Web of Science ®Google Scholar
• Gassmann, M., P. Thommes, T. Weiser, and U. Hubscher. 1990. Efficient production of chicken egg yolk antibodies against a conserved mammalian protein. FASEB J. 4:2528–2532.
   PubMed Web of Science ®Google Scholar
• Godowski, P. J., S. Rusconi, R. Miesfeld, and K. R. Yamomoto. 1987. Glucocorticoid receptor mutants that are constitutive activators of transcriptional enhancement. Nature (London) 325:365–368.
   PubMed Web of Science ®Google Scholar
• Hankinson, O. 1983. Evidence that benzo(a)pyrene-resistant, aryl hydrocarbon hydroxylase-deficient variants of mouse hepatoma line, Hepa-1, are mutational in origin. Somatic Cell Genet. 9:497–514.
   PubMedGoogle Scholar
• Hapgood, J., S. Cuthill, M. Denis, L. Poellinger, and J.-A. Gustafsson. 1989. Specific protein-DNA interactions at a xenobiotic-responsive element: copurification of dioxin receptor and DNA-binding activity. Proc. Natl. Acad. Sci. USA 86:60–64.
   PubMedGoogle Scholar
• Hoffman, E. C., H. Reyes, F. F. Chu, F. Sander, L. H. Conley, B. A. Brooks, and O. Hankinson. 1991. Cloning of a factor required for activity of the Ah (dioxin) receptor. Science 252:954–958.
   PubMed Web of Science ®Google Scholar
• Jackson, P., D. Baltimore, and D. Picard. 1993. Hormone-conditional transformation by fusion proteins of c-Abl and its transforming variants. EMBO J. 12:2809–2819.
   PubMedGoogle Scholar
• Kadesh, T. 1993. Consequences of heteromeric interactions among helix-loop-helix proteins. Cell Growth Differ. 4:49–55.
   PubMedGoogle Scholar
• Kozak, M. 1987. An analysis of 5′-noncoding sequences from 699 vertebrate messenger RNAs. Nucleic Acids Res. 15:8125–8148.
   PubMed Web of Science ®Google Scholar
• Nambu, J. R., J. O. Lewis, K. A. Wharton, Jr., and S. T. Crews. 1991. The drosophila single-minded gene encodes a helix-loop-helix protein that acts as a master regulator of CNS midline development. Cell 67:1157–1167.
   PubMed Web of Science ®Google Scholar
• Nemoto, T., G. G. F. Mason, A. Wilhelmsson, S. Cuthill, J. Hapgood, J.-A. Gustafsson, and L. Poellinger. 1990. Activation of the dioxin and glucocorticoid receptors to a DNA binding state under cell-free conditions. J. Biol. Chem. 265:2269–2277.
   PubMedGoogle Scholar
• Nemoto, T., Y. Ohara-Nemoto, M. Denis, and J.-A. Gustafsson. 1990. The transformed glucocorticoid receptor has a lower steroid binding affinity than the nontransformed receptor. Biochemistry 29:1880–1886.
   PubMedGoogle Scholar
• Neuhold, L. A., Y. Shirayoshi, K. Ozato, J. E. Jones, and D. W. Nebert. 1989. Regulation of mouse CYP1A1 gene expression by dioxin: requirement of two cis-acting elements during induction. Mol. Cell. Biol. 9:2378–2386.
   PubMed Web of Science ®Google Scholar
• Perdew, G. H. 1988. Association of the Ah receptor with the 90 kD heat shock protein. J. Biol. Chem. 263:13802–13805.
   PubMed Web of Science ®Google Scholar
• Perdew, G. H., and M. L. Whitelaw. 1991. Evidence that the 90-kDa heat shock protein (hsp90) exists in cytosol in heteromeric complexes containing hsp70 and three other proteins with Mr of 63,00, 56,000, and 50,000. J. Biol. Chem. 266:6708–6713.
   PubMed Web of Science ®Google Scholar
• Picard, D., B. Khursheed, M. J. Garabedian, M. G. Fortin, S. Lindquist, and K. R. Yamamoto. 1990. Reduced levels of hsp90 compromise steroid receptor action in vivo. Nature (London) 348:166–168.
   PubMed Web of Science ®Google Scholar
• Picard, D., S. J. Salser, and K. R. Yamamoto. 1988. A movable and regulable inactivation function within the steroid binding domain of the glucocorticoid receptor. Cell 54:1073–1080.
   PubMed Web of Science ®Google Scholar
• Poellinger, L., M. Gottlicher, and J.-A. Gustafsson. 1992. The dioxin and peroxisome proliferator-activated receptors: nuclear receptors in search of endogenous ligands. Trends Pharm. Sci. 13:241–245.
   PubMed Web of Science ®Google Scholar
• Poellinger, L., J. Lund, E. Dahlberg, and J.-A. Gustafsson. 1985. A hydroxylapatite microassay for receptor binding of 2,3,7,8-tetrachlorodibenzo-p-dioxin and 3-methylcholanthrene in various tissues. Anal Biochem. 144:371–384.
   PubMedGoogle Scholar
• Pongratz, I., G. G. F. Mason, and L. Poellinger. 1992. Dual roles of the 90 kDa heat shock protein in modulating functional activities of the dioxin receptor. J. Biol. Chem. 267:13728–13734.
   PubMed Web of Science ®Google Scholar
• Pratt, W. B., K. A. Hutchinson, and L. C. Scherrer. 1992. Steroid receptor folding by heat-shock proteins and composition of the receptor heterocomplex. Trends Endocrinol. Metab. 3:326–333.
   PubMedGoogle Scholar
• Reyes, H., S. Reiz-Porszasz, and O. Hankinson. 1992. Identification of the Ah receptor nuclear translocator protein (Arnt) as a component of the DNA binding form of the Ah receptor. Science 256:1193–1195.
   PubMed Web of Science ®Google Scholar
• Rusconi, S., and K. R. Yamamoto. 1987. Functional dissection of the hormone and DNA binding activities of the glucocorticoid receptor. EMBO J. 6:1309–1315.
   PubMed Web of Science ®Google Scholar
• Scherrer, L. C., F. C. Dalman, E. Massa, S. Meshinchi, and W. B. Pratt. 1990. Structural and functional reconstitution of the glucocorticoid receptor-hsp90 complex. J. Biol. Chem. 265:21397–21400.
   PubMedGoogle Scholar
• Scherrer, L. C., D. Picard, E. Massa, J. M. Harmon, S. S. Simons, K. R. Yamamoto, and W. B. Pratt. 1993. Evidence that the hormone binding domain of steroid receptors confers hormonal control on chimeric proteins by determining their hormone-regulated binding to heat shock protein 90. Biochemistry 32:5381–5386.
   PubMedGoogle Scholar
• Shaknovich, R., G. Shue, and D. S. Kohtz. 1992. Conformational activation of a basic helix-loop-helix protein (MyoD) by the C-terminal region of murine HSP90 (HSP84). Mol. Cell. Biol. 12:5059–5068.
   PubMedGoogle Scholar
• Sjöblom, K., and L. Poellinger. Unpublished results.
   Google Scholar
• Smith, D. F., and D. O. Toft. 1993. Steroid receptors and their associated proteins. Mol. Endocrinol. 7:4–11.
   PubMed Web of Science ®Google Scholar
• Takahashi, J. S. 1992. Circadian clock genes are ticking. Science 258:238–240.
   PubMed Web of Science ®Google Scholar
• Thayer, M. T., and H. Weintraub. 1993. A cellular factor stimulates the DNA binding activity of MyoD and E47. Proc. Natl. Acad. Sci. USA 90:6483–6487.
   PubMedGoogle Scholar
• Whitelaw, M. L., M. Gottlicher, J. A. Gustafsson, and L. Poellinger. 1993. Definition of a novel ligand binding domain of a nuclear bHLH receptor: colocalization of ligand and hsp90 binding activities within the regulable inactivation domain of the dioxin receptor. EMBO J. 12:4169–4179.
   PubMed Web of Science ®Google Scholar
• Whitelaw, M. L., I. Pongratz, A. Wilhelmsson, J. A. Gustafsson, and L. Poellinger. 1993. Ligand-dependent recruitment of the Arnt coregulator determines DNA recognition by the dioxin receptor. Mol. Cell. Biol. 13:2504–2514.
   PubMed Web of Science ®Google Scholar
• Wilhelmsson, A., S. Cuthill, M. Denis, A. C. Wikstrom, J.-A. Gustafsson, and L. Poellinger. 1990. The specific DNA binding activity of the dioxin receptor is modulated by the 90 kd heat shock protein. EMBO J. 9:69–76.
   PubMed Web of Science ®Google Scholar