A Structural Model of the Constitutive Androstane Receptor Defines Novel Interactions That Mediate Ligand-Independent Activity

REFERENCES

• Anzenbacher, P., and E. Anzenbacherova. 2001. Cytochromes P450 and metabolism of xenobiotics. Cell. Mol. Life Sci. 58: 737–747.
   PubMed Web of Science ®Google Scholar
• Anzick, S. L., J. Kononen, R. L. Walker, D. O. Azorsa, M. M. Tanner, X. Y. Guan, G. Sauter, O. P. Kallioniemi, J. M. Trent, and P. S. Meltzer. 1997. AIB1, a steroid receptor coactivator amplified in breast and ovarian cancer. Science 277: 965–968.
   PubMed Web of Science ®Google Scholar
• Brzozowski, A. M., A. C. Pike, Z. Dauter, R. E. Hubbard, T. Bonn, O. Engstrom, L. Ohman, G. L. Greene, J. A. Gustafsson, and M. Carlquist. 1997. Molecular basis of agonism and antagonism in the oestrogen receptor. Nature 389: 753–758.
   PubMed Web of Science ®Google Scholar
• Chen, H., R. J. Lin, R. L. Schiltz, D. Chakravarti, A. Nash, L. Nagy, M. L. Privalsky, Y. Nakatani, and R. M. Evans. 1997. Nuclear receptor coactivator ACTR is a novel histone acetyltransferase and forms a multimeric activation complex with P/CAF and CBP/p300. Cell 90: 569–580.
   PubMed Web of Science ®Google Scholar
• Chen, J. D., and R. M. Evans. 1995. A transcriptional corepressor that interacts with nuclear hormone receptors. Nature 377: 454–457.
   PubMed Web of Science ®Google Scholar
• Chen, S., B. A. Johnson, Y. Li, S. Aster, B. McKeever, R. Mosley, D. E. Moller, and G. Zhou. 2000. Both coactivator LXXLL motif-dependent and -independent interactions are required for peroxisome proliferator-activated receptor gamma (PPARγ) function. J. Biol. Chem. 275: 3733–3736.
   PubMed Web of Science ®Google Scholar
• Choi, H. S., M. Chung, I. Tzameli, D. Simha, Y. K. Lee, W. Seol, and D. D. Moore. 1997. Differential transactivation by two isoforms of the orphan nuclear hormone receptor CAR. J. Biol. Chem. 272: 23565–23571.
   PubMed Web of Science ®Google Scholar
• Darimont, B. D., R. L. Wagner, J. W. Apriletti, M. R. Stallcup, P. J. Kushner, J. D. Baxter, R. J. Fletterick, and K. R. Yamamoto. 1998. Structure and specificity of nuclear receptor-coactivator interactions. Genes Dev. 12: 3343–3356.
   PubMed Web of Science ®Google Scholar
• Dauber-Osguthorpe, P., V. A. Roberts, D. J. Osguthorpe, J. Wolff, M. Genest, and A. T. Hagler. 1988. Structure and energetics of ligand binding to proteins: Escherichia coli dihydrofolate reductase-trimethoprim, a drug-receptor system. Proteins 4: 31–47.
   PubMed Web of Science ®Google Scholar
• Ekins, S., and S. A. Wrighton. 1999. The role of CYP2B6 in human xenobiotic metabolism. Drug Metab. Rev. 31: 719–754.
   PubMed Web of Science ®Google Scholar
• Feng, W., R. C. Ribeiro, R. L. Wagner, H. Nguyen, J. W. Apriletti, R. J. Fletterick, J. D. Baxter, P. J. Kushner, and B. L. West. 1998. Hormone-dependent coactivator binding to a hydrophobic cleft on nuclear receptors. Science 280: 1747–1749.
   PubMed Web of Science ®Google Scholar
• Forman, B. M., E. Goode, J. Chen, A. E. Oro, D. J. Bradley, T. Perlmann, D. J. Noonan, L. T. Burka, T. McMorris, W. W. Lamph, et al. 1995. Identification of a nuclear receptor that is activated by farnesol metabolites. Cell 81: 687–693.
   PubMed Web of Science ®Google Scholar
• Forman, B. M., P. Tontonoz, J. Chen, R. P. Brun, B. M. Spiegelman, and R. M. Evans. 1995. 15-Deoxy-Δ12,14-prostaglandin J2 is a ligand for the adipocyte determination factor PPARγ. Cell E83: 803–812.
   Google Scholar
• Forman, B. M., I. Tzameli, H. S. Choi, J. Chen, D. Simha, W. Seol, R. M. Evans, and D. D. Moore. 1998. Androstane metabolites bind to and deactivate the nuclear receptor CAR-beta. Nature 395: 612–615.
   PubMed Web of Science ®Google Scholar
• Freedman, L. P. 1999. Increasing the complexity of coactivation in nuclear receptor signaling. Cell 97: 5–8.
   PubMed Web of Science ®Google Scholar
• Gampe, R. T., Jr., V. G. Montana, M. H. Lambert, A. B. Miller, R. K. Bledsoe, M. V. Milburn, S. A. Kliewer, T. M. Willson, and H. E. Xu. 2000. Asymmetry in the PPARγ/RXRα crystal structure reveals the molecular basis of heterodimerization among nuclear receptors. Mol. Cell 5: 545–555.
   PubMed Web of Science ®Google Scholar
• Glass, C. K., and M. G. Rosenfeld. 2000. The coregulator exchange in transcriptional functions of nuclear receptors. Genes Dev. 14: 121–141.
   PubMed Web of Science ®Google Scholar
• Heery, D. M., E. Kalkhoven, S. Hoare, and M. G. Parker. 1997. A signature motif in transcriptional coactivators mediates binding to nuclear receptors. Nature 387: 733–736.
   PubMed Web of Science ®Google Scholar
• Hong, H., K. Kohli, M. J. Garabedian, and M. R. Stallcup. 1997. GRIP1, a transcriptional coactivator for the AF-2 transactivation domain of steroid, thyroid, retinoid, and vitamin D receptors. Mol. Cell. Biol. 17: 2735–2744.
   PubMed Web of Science ®Google Scholar
• Honkakoski, P., I. Zelko, T. Sueyoshi, and M. Negishi. 1998. The nuclear orphan receptor CAR-retinoid X receptor heterodimer activates the phenobarbital-responsive enhancer module of the CYP2B gene. Mol. Cell. Biol. 18: 5652–5658.
   PubMed Web of Science ®Google Scholar
• Horlein, A. J., A. M. Naar, T. Heinzel, J. Torchia, B. Gloss, R. Kurokawa, A. Ryan, Y. Kamei, M. Soderstrom, C. K. Glass, et al. 1995. Ligand-independent repression by the thyroid hormone receptor mediated by a nuclear receptor corepressor. Nature 377: 397–404.
   PubMed Web of Science ®Google Scholar
• Hu, X., and M. A. Lazar. 1999. The CoRNR motif controls the recruitment of corepressors by nuclear hormone receptors. Nature 402: 93–96.
   PubMed Web of Science ®Google Scholar
• Hu, X., Y. Li, and M. A. Lazar. 2001. Determinants of CoRNR-dependent repression complex assembly on nuclear hormone receptors. Mol. Cell. Biol. 21: 1747–1758.
   PubMedGoogle Scholar
• Jackson, T. A., J. K. Richer, D. L. Bain, G. S. Takimoto, L. Tung, and K. B. Horwitz. 1997. The partial agonist activity of antagonist-occupied steroid receptors is controlled by a novel hinge domain-binding coactivator L7/SPA and the corepressors N-CoR or SMRT. Mol. Endocrinol. 11: 693–705.
   PubMed Web of Science ®Google Scholar
• Jeannin, E., D. Robyr, and B. Desvergne. 1998. Transcriptional regulatory patterns of the myelin basic protein and malic enzyme genes by the thyroid hormone receptors alpha1 and beta1. J. Biol. Chem. 273: 24239–24248.
   PubMedGoogle Scholar
• Klein, E. S., J. W. Wang, B. Khalifa, S. A. Gavigan, and R. A. Chandraratna. 2000. Recruitment of nuclear receptor corepressor and coactivator to the retinoic acid receptor by retinoid ligands. Influence of DNA-heterodimer interactions. J. Biol. Chem. 275: 19401–19408.
   PubMed Web of Science ®Google Scholar
• Lala, D. S., R. Mukherjee, I. G. Schulman, S. S. Koch, L. J. Dardashti, A. M. Nadzan, G. E. Croston, R. M. Evans, and R. A. Heyman. 1996. Activation of specific RXR heterodimers by an antagonist of RXR homodimers. Nature 383: 450–453.
   PubMed Web of Science ®Google Scholar
• Laskowski, R. A., D. S. Moss, and J. M. Thornton. 1993. Main-chain bond lengths and bond angles in protein structures. J. Mol. Biol. 231: 1049–1067.
   PubMed Web of Science ®Google Scholar
• Lavinsky, R. M., K. Jepsen, T. Heinzel, J. Torchia, T. M. Mullen, R. Schiff, A. L. Del-Rio, M. Ricote, S. Ngo, J. Gemsch, S. G. Hilsenbeck, C. K. Osborne, C. K. Glass, M. G. Rosenfeld, and D. W. Rose. 1998. Diverse signaling pathways modulate nuclear receptor recruitment of N-CoR and SMRT complexes. Proc. Natl. Acad. Sci. USA 95: 2920–2925.
   PubMed Web of Science ®Google Scholar
• Lee, J. W., F. Ryan, J. C. Swaffield, S. A. Johnston, and D. D. Moore. 1995. Interaction of thyroid-hormone receptor with a conserved transcriptional mediator. Nature 374: 91–94.
   PubMed Web of Science ®Google Scholar
• Leers, J., E. Treuter, and J. A. Gustafsson. 1998. Mechanistic principles in NR box-dependent interaction between nuclear hormone receptors and the coactivator TIF2. Mol. Cell. Biol. 18: 6001–6013.
   PubMedGoogle Scholar
• Li, H., P. J. Gomes, and J. D. Chen. 1997. RAC3, a steroid/nuclear receptor-associated coactivator that is related to SRC-1 and TIF2. Proc. Natl. Acad. Sci. USA 94: 8479–8484.
   PubMed Web of Science ®Google Scholar
• Mangelsdorf, D. J., C. Thummel, M. Beato, P. Herrlich, G. Schutz, K. Umesono, B. Blumberg, P. Kastner, M. Mark, P. Chambon, et al. 1995. The nuclear receptor superfamily: the second decade. Cell 83: 835–839.
   PubMed Web of Science ®Google Scholar
• McInerney, E. M., D. W. Rose, S. E. Flynn, S. Westin, T. M. Mullen, A. Krones, J. Inostroza, J. Torchia, R. T. Nolte, N. Assa-Munt, M. V. Milburn, C. K. Glass, and M. G. Rosenfeld. 1998. Determinants of coactivator LXXLL motif specificity in nuclear receptor transcriptional activation. Genes Dev. 12: 3357–3368.
   PubMed Web of Science ®Google Scholar
• Moore, L. B., D. J. Parks, S. A. Jones, R. K. Bledsoe, T. G. Consler, J. B. Stimmel, B. Goodwin, C. Liddle, S. G. Blanchard, T. M. Willson, J. L. Collins, and S. A. Kliewer. 2000. Orphan nuclear receptors constitutive androstane receptor and pregnane X receptor share xenobiotic and steroid ligands. J. Biol. Chem. 275: 15122–15127.
   PubMed Web of Science ®Google Scholar
• Muangmoonchai, R., D. Smirlis, S. C. Wong, M. Edwards, I. R. Phillips, and E. A. Shephard. 2001. Xenobiotic induction of cytochrome P450 2B1 (CYP2B1) is mediated by the orphan nuclear receptor constitutive androstane receptor (CAR) and requires steroid coactivator 1 (SRC-1) and the transcription factor Sp1. Biochem. J. 355: 71–78.
   PubMed Web of Science ®Google Scholar
• Nolte, R. T., G. B. Wisely, S. Westin, J. E. Cobb, M. H. Lambert, R. Kurokawa, M. G. Rosenfeld, T. M. Willson, C. K. Glass, and M. V. Milburn. 1998. Ligand binding and coactivator assembly of the peroxisome proliferator-activated receptor-gamma. Nature 395: 137–143.
   PubMed Web of Science ®Google Scholar
• Onate, S. A., S. Y. Tsai, M. J. Tsai, and B. W. O'Malley. 1995. Sequence and characterization of a coactivator for the steroid hormone receptor superfamily. Science 270: 1354–1357.
   PubMed Web of Science ®Google Scholar
• Perissi, V., L. M. Staszewski, E. M. McInerney, R. Kurokawa, A. Krones, D. W. Rose, M. H. Lambert, M. V. Milburn, C. K. Glass, and M. G. Rosenfeld. 1999. Molecular determinants of nuclear receptor-corepressor interaction. Genes Dev. 13: 3198–3208.
   PubMed Web of Science ®Google Scholar
• Renaud, J. P., N. Rochel, M. Ruff, V. Vivat, P. Chambon, H. Gronemeyer, and D. Moras. 1995. Crystal structure of the RAR-gamma ligand-binding domain bound to all-trans retinoic acid. Nature 378: 681–689.
   PubMed Web of Science ®Google Scholar
• Rochel, N., J. M. Wurtz, A. Mitschler, B. Klaholz, and D. Moras. 2000. The crystal structure of the nuclear receptor for vitamin D bound to its natural ligand. Mol. Cell 5: 173–179.
   PubMed Web of Science ®Google Scholar
• Seol, W., H. S. Choi, and D. D. Moore. 1995. Isolation of proteins that interact specifically with the retinoid X receptor: two novel orphan receptors. Mol. Endocrinol. 9: 72–85.
   PubMed Web of Science ®Google Scholar
• Shiau, A. K., D. Barstad, P. M. Loria, L. Cheng, P. J. Kushner, D. A. Agard, and G. L. Greene. 1998. The structural basis of estrogen receptor/coactivator recognition and the antagonism of this interaction by tamoxifen. Cell 95: 927–937.
   PubMed Web of Science ®Google Scholar
• Smith, C. L., Z. Nawaz, and B. W. O'Malley. 1997. Coactivator and corepressor regulation of the agonist/antagonist activity of the mixed antiestrogen, 4-hydroxytamoxifen. Mol. Endocrinol. 11: 657–666.
   PubMed Web of Science ®Google Scholar
• Sueyoshi, T., T. Kawamoto, I. Zelko, P. Honkakoski, and M. Negishi. 1999. The repressed nuclear receptor CAR responds to phenobarbital in activating the human CYP2B6 gene. J. Biol. Chem. 274: 6043–6046.
   PubMed Web of Science ®Google Scholar
• Tagami, T., W. X. Gu, P. T. Peairs, B. L. West, and J. L. Jameson. 1998. A novel natural mutation in the thyroid hormone receptor defines a dual functional domain that exchanges nuclear receptor corepressors and coactivators. Mol. Endocrinol. 12: 1888–1902.
   PubMedGoogle Scholar
• Torchia, J., D. W. Rose, J. Inostroza, Y. Kamei, S. Westin, C. K. Glass, and M. G. Rosenfeld. 1997. The transcriptional coactivator p/CIP binds CBP and mediates nuclear-receptor function. Nature 387: 677–684.
   PubMed Web of Science ®Google Scholar
• Tzameli, I., P. Pissios, E. G. Schuetz, and D. D. Moore. 2000. The xenobiotic compound 1,4-bis[2-(3,5-dichloropyridyloxy)]benzene is an agonist ligand for the nuclear receptor CAR. Mol. Cell. Biol. 20: 2951–2958.
   PubMed Web of Science ®Google Scholar
• Umesono, K., K. K. Murakami, C. C. Thompson, and R. M. Evans. 1991. Direct repeats as selective response elements for the thyroid hormone, retinoic acid, and vitamin D3 receptors. Cell 65: 1255–1266.
   PubMed Web of Science ®Google Scholar
• Uppenberg, J., C. Svensson, M. Jaki, G. Bertilsson, L. Jendeberg, and A. Berkenstam. 1998. Crystal structure of the ligand binding domain of the human nuclear receptor PPARγ. J. Biol. Chem. 273: 31108–31112.
   PubMedGoogle Scholar
• Watkins, R. E., G. B. Wisely, L. B. Moore, J. L. Collins, M. H. Lambert, S. P. Williams, T. M. Willson, S. A. Kliewer, and M. R. Redinbo. 2001. The human nuclear xenobiotic receptor PXR: structural determinants of directed promiscuity. Science 292: 2329–2333.
   PubMed Web of Science ®Google Scholar
• Wei, P., J. Zhang, M. Egan-Hafley, S. Liang, and D. D. Moore. 2000. The nuclear receptor CAR mediates specific xenobiotic induction of drug metabolism. Nature 407: 920–923.
   PubMed Web of Science ®Google Scholar
• Wurtz, J. M., W. Bourguet, J. P. Renaud, V. Vivat, P. Chambon, D. Moras, and H. Gronemeyer. 1996. A canonical structure for the ligand-binding domain of nuclear receptors. Nat. Struct. Biol. 3: 87–94.
   PubMedGoogle Scholar
• Xie, W., J. L. Barwick, C. M. Simon, A. M. Pierce, S. Safe, B. Blumberg, P. S. Guzelian, and R. M. Evans. 2000. Reciprocal activation of xenobiotic response genes by nuclear receptors SXR/PXR and CAR. Genes Dev. 14: 3014–3023.
   PubMed Web of Science ®Google Scholar
• Xu, L., C. K. Glass, and M. G. Rosenfeld. 1999. Coactivator and corepressor complexes in nuclear receptor function. Curr. Opin. Genet. Dev. 9: 140–147.
   PubMed Web of Science ®Google Scholar
• Yuan, C. X., M. Ito, J. D. Fondell, Z. Y. Fu, and R. G. Roeder. 1998. The TRAP220 component of a thyroid hormone receptor-associated protein (TRAP) coactivator complex interacts directly with nuclear receptors in a ligand-dependent fashion. Proc. Natl. Acad. Sci. USA 95: 7939–7944.
   PubMed Web of Science ®Google Scholar
• Zamir, I., J. Dawson, R. M. Lavinsky, C. K. Glass, M. G. Rosenfeld, and M. A. Lazar. 1997. Cloning and characterization of a corepressor and potential component of the nuclear hormone receptor repression complex. Proc. Natl. Acad. Sci. USA 94: 14400–14405.
   PubMedGoogle Scholar
• Zhang, J., X. Hu, and M. A. Lazar. 1999. A novel role for helix 12 of retinoid X receptor in regulating repression. Mol. Cell. Biol. 19: 6448–6457.
   PubMed Web of Science ®Google Scholar
• Zhu, Y., C. Qi, S. Jain, M. S. Rao, and J. K. Reddy. 1997. Isolation and characterization of PBP, a protein that interacts with peroxisome proliferator-activated receptor. J. Biol. Chem. 272: 25500–25506.
   PubMed Web of Science ®Google Scholar