The phantom ligand effect: Allosteric control of transcription by the retinoid X receptor

Genes and Development

Volumn 11, Issue 3, 1997, Pages 299-308

  Schulman, Ira G ^a,c   Li, Chuan ^a,b   Schwabe, John W R ^a   Evans, Ronald M ^a,b  

^a SALK INSTITUTE FOR BIOLOGICAL STUDIES   (United States)

^b HOWARD HUGHES MEDICAL INSTITUTE   (United States)

^c LIGAND PHARMACEUTICALS INC   (United States)

Author keywords

phantom ligand effect; RAR; RXR; Transcription

Indexed keywords

DNA; LIGAND; RETINOID X RECEPTOR; STEROID RECEPTOR; THYROID HORMONE RECEPTOR; TRANSCRIPTION FACTOR;

ALLOSTERISM; ANIMAL CELL; ARTICLE; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; DNA BINDING; LIGAND BINDING; NONHUMAN; PHANTOM; PRIORITY JOURNAL; TRANSACTIVATION;

EID: 0031043055     PISSN: 08909369     EISSN: None     Source Type: Journal    
DOI: 10.1101/gad.11.3.299     Document Type: Article

References (41)

1. Allegretto, E.A., M.R. McClurg, S.B. Lazarchik, D.L. Clemm, S.A. Kerner, M.G. Elgort, M.F. Boehm, S.K. White, J.W. Pike, and R.A. Heyman. 1993. Transactivation properties of retinoic acid and retinoid X receptors in mammalian cells and yeast. Correlation with hormone binding and effects of metabolism. J. biol. Chem. 268: 26625-26633.
2. Allenby, G., M.-T. Bocquel, M. Saunders, S. Kazmer, J. Speck, M. Rosenberger, A. Lovey, P. Kastner, J.F. Grippo, P. Chambon, and A.A. Levin. 1993. Retinoic acid receptors and retinoid X receptors: Interactions with endogenous retinoic acids. Proc. Natl. Acad. Sci. 90: 30-34.
3. Baniahmad, A., A.C. Kohne, and R. Renkawitz. 1992. A transferable silencing domain is present in the thyroid hormone receptor, in the v-erbA oncogene product and the retinoic acid receptor. EMBO J. 11: 1015-1023.
4. Bourguet, W., M. Ruff, P. Chambon, H. Gronemeyer, and D. Moras. 1995. Crystal structure of the ligand-binding domain of the human nuclear receptor RXR-alpha. Nature 375: 377-382
5. Canan Koch, S.S., L.J. Dardashti, J.J. Hebert, G.E. Croston, K.S. Flatten, R.A. Heyman, and A.M. Nadzan. 1996. Identification of the first retinoid X receptor homodimer antagonist. J. Med. Chem. 39: 3229-3234.
6. Cavailles, V., S. Dauvois, P.S. Danielum, and M.G. Parker. 1994. Interaction of proteins with transcriptionally active estrogen receptors. Proc. Natl. Acad. Sci. 91: 10009-10013.
7. Chakravarti, D., V.J. LaMorte, M.C. Nelson, T. Nakajima, I.G. Schulman, H. Juguilon, M. Montminy, and R.M. Evans. 1996. Role of CBP/P300 in nuclear receptor signaling. Nature 383: 99-103.
8. Chen, J.D. and R.M. Evans. 1995. A transcriptional co-repressor that interacts with nuclear hormone receptors. Nature 377: 454-457.
9. Chen, J.D., K. Umesono, and R.M. Evans. 1996. SMRT isoforms mediate repression and anti-repression of nuclear receptor heterodimers. Proc. Natl. Acad. Sci. 93: 7567-7571.
10. Claret, F.-X., T. Antakly, M. Karin, and F. Saatcioglu. 1996. A shift in the ligand responsiveness of thyroid hormone receptor a induced by heterodimerization with retinoid X receptor a. Mol. Cell. Biol. 16: 219-227.
11. Damm, K., R.A. Heyman, K. Umesono, and R.A. Evans. 1993. Functional inhibition of retinoic acid response by dominant negative retinoic receptor mutants. Proc. Natl. Acad. Sci. 90: 2989-2993.
12. Forman, B.M., K. Umesono, J. Chen, and and R.M. Evans. 1995. Unique response pathways are established by allosteric interactions among nuclear hormone receptors. Cell 81: 541-550.
13. Halachmi, S., E. Marden, G. Martin, H. MacKay, C. Abbondanza, and M. Brown. 1994. Estrogen receptor-associated proteins: Possible mediators of hormone induced transcription. Science 264: 1455-1458.
14. Hörlein, A.J., A.M. Naar, T. Heinzel, J. Torchia, B. Gloss, R. Kurokawa, A. Ryan, Y. Kamai, M. Soderstrom, C.K. Glass, and M.G. Rosenfeld. 1995. Hormone-independent repression by the thyroid hormone receptor is mediated by a nuclear receptor co-repressor N-COR. Nature 377: 397-404.
15. Jacob, F. and J. Monod. 1961. Genetic regulatory mechanisms in the synthesis of proteins. J. Mol. Biol. 3: 318-356.
16. Kamei, Y., L. Xu, T. Heinzel, J. Torchia, R. Kurokawa, B. Gloss, S.-C. Lin, R.A. Heyman, D.W. Rose, C.K. Glass, and M.G. Rosenfeld. 1996. A CBP integrator complex mediates transcriptional activation and AP-1 inhibition by nuclear receptors. Cell 85: 403-414.
17. Kastner, P., M. Mark, and P. Chambon. 1995. Nonsteroid nuclear receptors: What are genetic studies telling us about their role in real life? Cell 83: 859-869.
18. Kurokawa, R., J. DiRenzo, M. Boehm, J. Sugarman, B. Gloss, M.G. Rosenfeld, R.A. Heyman, and C.K. Glass. 1994. Regulation of retinoid signalling by receptor polarity and allosteric control of ligand binding. Nature 371: 528-531.
19. Kurokawa, R., M. Soderstrom, A. Horlein, S. Halachmi, M. Brown, M.G. Rosenfeld, and C.K. Glass. 1995. A co-repressor specifies polarity-specific activities of retinoic acid receptors. Nature 377: 451-457.
20. Lala, D.S., R. Mukherjee, I.G. Schulman, S.S. Canan-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.
21. Leblanc, B.P. and H.G. Stunnenberg. 1995. 9-cis retinoic acid signaling: Changing partners causes some excitement. Genes & Dev. 9: 1811-1816.
22. 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.
23. Lefstin, J.A., J.R. Thomas, and K.R. Yamamoto. 1994. Influence of a steroid receptor-DNA-binding domain on transcriptional regulatory functions. Genes & Dev. 8: 2842-2856.
24. Leng, X., J. Blanco, S.Y. Tsai, K. Ozato, B.W. O'Malley, and M.-J. Tsai. 1995. Mouse retinoid X receptor contains a separable ligand-binding and transactivation domain in its E region. Mol. Cell. Biol. 15: 255-263.
25. Li, C., J.W.R. Schwabe, and R.M. Evans. 1997. Co-expression of nuclear receptor partners increases their solubility and biological activities. Proc. Natl. Acad. Sci. (in press).
26. Mangelsdorf, D.J. and R.M. Evans. 1995. The RXR heterodimers and orphan receptors. Cell 83: 841-850.
27. Mangelsdorf, D.J., C. Thummel, M. Beato, P. Herrlich, G. Schutz, K. Umesono, P. Kastner, M. Mark, P. Chambon, and R.M. Evans. 1995. The nuclear receptor superfamily: The second decade. Cell 83: 835-839.
28. Oñate, 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: 1354-1347.
29. Renaud, J.-P., N. Rochel, M. Ruff, V. Vivat, P. Chambon, H. Gronemeyer, and D. Moras. 1995. Crystal structure of the RAR-γ ligand-binding domain bound to all-trans retinoic acid. Nature 378: 681-689.
30. Rose, M.D., F. Winston, and P. Hieter. 1990. Methods in yeast genetics. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
31. Schulman, I.G., D. Chakravarti, H. Juguilon, A. Romo, and R.M. Evans. 1995. Interactions between the retinoid X receptor and a conserved region of the TATA-binding protein mediate hormone-dependent transactivation. Proc. Natl. Acad. Sci. 92: 8288-8292.
32. Schulman, I.G., H. Juguilon, and R.M. Evans. 1996. Activation and repression by nuclear hormone receptors: Hormone modulates an equilibrium between active and repressive states. Mol. Cell. Biol. 16: 3807-3818.
33. Schwabe, J.W.R. 1996. Transcriptional control: How nuclear receptors get turned on. Curr. Biol. 6: 372-374.
34. Starr, D.B., W. Matsui, J.R. Thomas, and K.R. Yamamoto. 1996. Intracellular receptors use a common mechanism to interpret signaling information at response elements. Genes & Dev. 10: 1271-1283.
35. Tate, B.F. and J.F. Grippo. 1995. Mutagenesis of the ligand binding domain of the human retinoic acid receptor a identifies critical residues for 9-cis-retinoic acid binding. J. Biol. Chem. 270: 20258-20263.
36. Tate, B.F., G. Allenby, R. Janocha, S. Kazmer, J. Speck, L.J. Sturzenbecker, P. Abarzua, A.A. Levin, and J.F. Grippo. 1994. Distinct binding determinants for 9-cis retinoic acid are located within AF-2 of retinoic acid receptorα. Mol. Cell. Biol. 14: 2323-2330.
37. 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 D, receptors. Cell 65: 1255-1266.
38. vom Baur, E., C. Zechel, D. Heery, M.J.S. Heine, J.M. Garnier, V. Vivat, B. Le Douarin, H. Gronemeyer, P. Chambon, and R. Losson. 1996. Differential ligand-dependent interactions between the AF-2 activating domain of nuclear receptors and putative transcriptional intermediary factors mSUG1 and TIF1. EMBO J. 15: 110-124.
39. Wagner, R.L., J.W. Apriletti, M.E. McGrath, B.L. West, J.D. Baxter, and R.J. Fletterick. 1995. A structural role for hormone in the thyroid hormone receptor. Nature 378: 690-697.
40. 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. Nature Struct. Biol. 3: 87-94.
41. Yao, T.P., B.M. Forman, Z. Jiang, L. Cherbas, J.D. Chen, M. McKeown, P. Cherbas, and R.M. Evans. 1993. Functional ecdysone receptor is the product of EcR and Ultraspiracle genes. Nature 366: 476-479.