Auto-silencing by the retinoid X receptor

Journal of Molecular Biology

Volumn 284, Issue 1, 1998, Pages 21-32

  Kersten, Sander ^a   Dong, Diane ^a   Lee, Wen yi ^a   Reczek, Peter R ^b   Noy, Noa ^a  

^a Department of Obstetrics Gynecology   (United States)

^b BRISTOL MYERS SQUIBB   (United States)

Author keywords

Hormone; Oligomers; Receptor; Retinoid; RXR

Indexed keywords

CELL NUCLEUS RECEPTOR; RETINOID X RECEPTOR; TETRAMER;

ARTICLE; DIMERIZATION; GENETIC TRANSCRIPTION; LIGAND BINDING; OLIGOMERIZATION; POINT MUTATION; PRIORITY JOURNAL;

EID: 0032553558     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1998.2168     Document Type: Article

References (36)

1. Beato M., Chavez S., Truss M. Transcriptional regulation by steroid hormones. Steroids. 61:1996;240-251.
2. Bourguet W., Ruff M., Chambon P., Gronemeyer H., Moras D. Crystal structure of the ligand-binding domain of the human nuclear receptor RXR-alpha. Nature. 375:1995;377-382.
3. Chambon P. A decade of molecular biology of retinoic acid receptors. FASEB J. 10:1996;940-954.
4. Chen J. D., Evans R. M. A transcriptional co-repressor that interacts with nuclear hormone receptors. Nature. 377:1995;454-457.
5. Chen Z.-P., Shemshedini L., Durand B., Noy N., Chambon P., Gronemeyer H. Pure and functionally homogeneous recombinant retinoid X receptor. J. Biol. Chem. 269:1994;25770-25776.
6. Gronemeyer H. Ligand and DNA-induced dissociation of RXR tetramers. J. Mol. Biol. 275:1998;55-65.
7. Cheskis B., Freedman L. P. Modulation of nuclear receptor interactions by ligands: kinetic analysis using surface plasmon resonance. Biochemistry. 35:1996;3309-3318.
8. Cogan U., Kopelman M., Mokady S., Shinitzky M. Binding affinities of retinol and related compounds to retinol binding proteins. Eur. J. Biochem. 65:1976;71-78.
9. Dong D., Noy N. Heterodimerization of the retinoid X receptor with the retinoic acid-and the vitamin D-receptors is regulated by ligands and by the self-association properties of RXR. Biochemistry. 37:1998;10691-10700.
10. Durand B., Saunders M., Leroy P., Leid M., Chambon P. All- trans and 9- cis retinoic acid induction of CRABPII transcription is mediated by RAR-RXR heterodimers bound to DR1 and DR2 repeated motifs. Cell. 71:1992;73-85.
11. Glass C. K., Rose D. W., Rosenfeld M. G. Nuclear receptor coactivators. Curr. Opin. Cell Biol. 9:1997;222-232.
12. Gronemeyer H., Laudet V. Transcription factors 3: nuclear receptors. Protein Profile. 2:1995;1173-1308.
13. Hallenbeck P. L., Marks M. S., Lippoldt R. E., Ozato K., Nikodem V. M. Heterodimerization of the thyroid hormone receptor with H-IIBP retinoid X receptorβ enhances DNA binding and TH-dependent transcriptional regulation. Proc. Natl Acad. Sci. USA. 89:1992;5572-5576.
14. Hörlein A. J., Naar A. M., Heinzel T., Torchia J., Gloss B., Kurokawa R., Ryan A., Kamei Y., Soderstrom M., Glass C. K., Rosenfeld M. G. Ligand-independent repression by the thyroid hormone receptor mediated by a nuclear receptor co-repressor. Nature. 377:1995;397-404.
15. Horwitz K. B., Jackson T. A., Bain D. L., Richer J. K., Takimoto G. S., Tung L. Nuclear receptor coactivators and corepressors. Mol. Endocrinol. 10:1996;1.
16. Kersten S., Kelleher D., Chambon P., Gronemeyer H., Noy N. Retinoid X receptor alpha forms tetramers in solution. Proc. Natl Acad. Sci. USA. 92:1995a;8645-8649.
17. Kersten D., Pan L., Chambon P., Gronemeyer H., Noy N. Role of ligand in retinoid signaling. 9-cis-retinoic modulates the oligomeric state of the retinoid X receptor. Biochemistry. 34:1995b;13717-13721.
18. Kersten S., Pan L., Noy N. On the role of ligand in retinoid signaling: positive cooperativity in the interactions of 9- cis -retinoic acid with tetramers of the retinoid X receptor. Biochemistry. 34:1995c;14263-14269.
19. Kersten S., Dawson M. I., Lewis B. A., Noy N. Individual subunits of heterodimers comprised of retinoic acid and retinoid X receptors interact with their ligands independently. Biochemistry. 35:1996;3816-3824.
20. Kersten S., Reczek P., Noy N. The tetramerization domain of RXR is important for transcriptional activation by the receptor. J. Biol. Chem. 272:1997a;29759-29768.
21. Kersten S., Gronemeyer H., Noy N. The DNA binding pattern of the retinoid X receptor is regulated by ligand-dependent modulation of its oligomeric state. J. Biol. Chem. 272:1997b;12771-12777.
22. Lakowicz J. A. Principles of Fluorescence Spectroscopy. 1983;Plenum Press, New York.
23. Leid M., Kastner P., Chambon P. Multiplicity generates diversity in the retinoic acid signalling pathways. Trends Biochem. Sci. 17:1992;427-433.
24. Mangelsdorf D. J., Thummel C., Beato M., Herrlich P., Schuetz G., Umesono K., Blumnberg B., Kastner P., Mark M., Chambon P., Evans R. M. The nuclear receptor superfamily: the second decade. Cell. 83:1995;835-839.
25. Peet D. J., Doyle D. F., Corey D. R., Mangelsdorf D. J. Chem. Biol. 5:1998;13-21.
26. Renaud J. P., Rochel N., Ruff M., Vivat V., Chambon P., Gronemeyer H., Moras D. Crystal structure of the RAR-gamma ligand-binding domain bound to all- trans retinoic acid. Nature. 378:1995;681-689.
27. Royer C. A., Smith W. R., Beeches J. M. Analysis of binding in macromolecular complexes: a generalized numerical approach. Anal. Biochem. 191:1990;287-294.
28. Sande S., Privalsky M. L. Identification of TRACs (T3 receptor-associating cofactors), a family of cofactors that associate with, and modulate the activity of, nuclear hormone receptors. Mol. Endocrinol. 10:1996;813-825.
29. Seol W., Mahon M. J., Lee Y. K., Moore D. D. Two receptor interacting domains in the nuclear hormone receptor corepressor RIP13/N-CoR. Mol. Endocrinol. 10:1996;1646-1655.
30. Torchia J., Rose D. W., Inostroza J., Kamei Y., Westin S., Glass C. K., Rosenfeld M. G. The transcriptional co-activator p-CIP binds CBP and mediates nuclear-receptor function. Nature. 387:1997;677-684.
31. Vivat V., Zechel C., Wurtz J.-M., Bourguet W., Kagechika H., Unemiya H., Shudo K., Moras D., Gronemeyer H., Chambon P. A mutation mimicking the ligand-induced transconformation yields a constitutive RXR that senses allosteric effects in heterodimers. EMBO J. 16:1997;5697-5709.
32. Wilson T. J., Mardoudas P., Howlett G. J., Davidson B. E. Ligand-induced self association of the Escherichia coli regulatory protein TyrR. J. Mol. Biol. 238:1994;309-318.
33. Wolffe A. P. Transcriptional control: sinful repression. Nature. 387:1997;16-17.
34. Wurtz J. M., Bourguet W., Renaud J. P., Vivat V., Chambon P., Moras D., Gronemeyer H. A canonical structure for the ligand-binding domain of nuclear receptors. Nature Struct. Biol. 3:1996;87-94.
35. Yu V., Delsert C., Andersen B., Holloway J., Devary O. V., Naeaer A. M., Kim S. Y., Boutin J. M., Glass C. K., Rosenfeld M. G. RXRβ, a coregulator that enhances binding of retinoic acid, thyroid hormone, and vitamin D receptors to their cognate response elements. Cell. 67:1991;1251-1266.
36. Zhang X. K., Hoffman B., Transcriptional elongation P. B.-V., Graupner G., Pfahl M. Retinoid X receptor is an auxiliary protein for thyroid hormone and retinoic acid receptor. Nature. 355:1992;441-446.