메뉴 건너뛰기




Volumn 17, Issue 10, 1997, Pages 6131-6138

A conformational switch in nuclear hormone receptors is involved in coupling hormone binding to corepressor release

Author keywords

[No Author keywords available]

Indexed keywords

GLUTATHIONE TRANSFERASE; HORMONE RECEPTOR; LIOTHYRONINE RECEPTOR; RETINOIC ACID; RETINOID X RECEPTOR; THYROID HORMONE; TRANSCRIPTION FACTOR;

EID: 0030771328     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.17.10.6131     Document Type: Article
Times cited : (79)

References (54)
  • 2
    • 0026557594 scopus 로고
    • A transferable silencing domain is present in the thyroid hormone receptor, in the v-Erb A oncogene product, and in the retinoic acid receptor
    • Baniahmad, A., A. C. Kohne, and R. Renkawitz. 1992. A transferable silencing domain is present in the thyroid hormone receptor, in the v-Erb A oncogene product, and in the retinoic acid receptor. EMBO J. 11:1015-1023.
    • (1992) EMBO J. , vol.11 , pp. 1015-1023
    • Baniahmad, A.1    Kohne, A.C.2    Renkawitz, R.3
  • 3
    • 0028988482 scopus 로고
    • The τ4 activation domain of the thyroid hormone receptor is required for release of a putative corepressor(s) necessary for transcriptional silencing
    • Baniahmad, A., X. Leng, T. P. Burris, S. Y. Tsai, M. J. Tsai, and B. W. O'Malley. 1995. The τ4 activation domain of the thyroid hormone receptor is required for release of a putative corepressor(s) necessary for transcriptional silencing. Mol. Cell. Biol. 15:76-86.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 76-86
    • Baniahmad, A.1    Leng, X.2    Burris, T.P.3    Tsai, S.Y.4    Tsai, M.J.5    O'Malley, B.W.6
  • 4
    • 0029618368 scopus 로고
    • Steroid hormone receptors: Many actors in search of a plot
    • Beato, M., P. Herrlich, and G. Schutz. 1995. Steroid hormone receptors: many actors in search of a plot. Cell 83:851-858.
    • (1995) Cell , vol.83 , pp. 851-858
    • Beato, M.1    Herrlich, P.2    Schutz, G.3
  • 5
    • 0028287579 scopus 로고
    • The variable clinical phenotype in thyroid hormone resistance syndrome
    • Beck-Peccoz, P., and V. K. K. Chatterjee. 1994. The variable clinical phenotype in thyroid hormone resistance syndrome. Thyroid 4:225-232.
    • (1994) Thyroid , vol.4 , pp. 225-232
    • Beck-Peccoz, P.1    Chatterjee, V.K.K.2
  • 6
    • 0023791461 scopus 로고
    • c-erbA encodes multiple proteins in chicken erythroid cells
    • Bigler, J., and R. N. Eisenman. 1988. c-erbA encodes multiple proteins in chicken erythroid cells. Mol. Cell. Biol. 8:4155-4161.
    • (1988) Mol. Cell. Biol. , vol.8 , pp. 4155-4161
    • Bigler, J.1    Eisenman, R.N.2
  • 7
    • 0029012163 scopus 로고
    • Crystal structure of the ligand-binding domain of the human nuclear hormone receptor RXR alpha
    • Bourguet, W., M. Ruff, P. Chambon, H. Gronemeyer, and D. Moras. 1995. Crystal structure of the ligand-binding domain of the human nuclear hormone receptor RXR alpha. Nature 375:377-382.
    • (1995) Nature , vol.375 , pp. 377-382
    • Bourguet, W.1    Ruff, M.2    Chambon, P.3    Gronemeyer, H.4    Moras, D.5
  • 9
    • 0028419153 scopus 로고
    • The retinoid signaling pathway
    • Chambon, P. 1994. The retinoid signaling pathway. Semin. Cell Biol. 5:115-125.
    • (1994) Semin. Cell Biol. , vol.5 , pp. 115-125
    • Chambon, P.1
  • 10
    • 0027385416 scopus 로고
    • The erbA oncogene represses the actions of both retinoid X and retinoid A receptors, but does so by distinct mechanisms
    • Chen, H.-W., and M. L. Privalsky. 1993. The erbA oncogene represses the actions of both retinoid X and retinoid A receptors, but does so by distinct mechanisms. Mol. Cell. Biol. 13:5970-5980.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 5970-5980
    • Chen, H.-W.1    Privalsky, M.L.2
  • 11
    • 0029097233 scopus 로고
    • A transcriptional co-repressor that interacts with nuclear hormone receptors
    • Chen, J. D., and R. M. Evans. 1995. A transcriptional co-repressor that interacts with nuclear hormone receptors. Nature 377:454-457.
    • (1995) Nature , vol.377 , pp. 454-457
    • Chen, J.D.1    Evans, R.M.2
  • 12
    • 0029794881 scopus 로고    scopus 로고
    • SMRT isoforms mediate repression and anti-repression of nuclear receptor heterodimers
    • 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. USA 93:7567-7571.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 7567-7571
    • Chen, J.D.1    Umesono, K.2    Evans, R.M.3
  • 13
    • 0027978768 scopus 로고
    • Spectrum of transcriptional, dimerization, and dominant negative properties of twenty different mutant thyroid hormone β receptors in thyroid hormone resistance syndrome
    • Collingwood, T. N., M. Adams, Y. Tone, and V. K. K. Chatterjee. 1994. Spectrum of transcriptional, dimerization, and dominant negative properties of twenty different mutant thyroid hormone β receptors in thyroid hormone resistance syndrome. Mol. Endocrinol. 8:1262-1277.
    • (1994) Mol. Endocrinol. , vol.8 , pp. 1262-1277
    • Collingwood, T.N.1    Adams, M.2    Tone, Y.3    Chatterjee, V.K.K.4
  • 14
    • 0024336324 scopus 로고
    • Protein encoded by v-Erb a functions as a thyroid hormone receptor antagonist
    • Damm, K., C. C. Thompson, and R. M. Evans. 1989. Protein encoded by v-Erb A functions as a thyroid hormone receptor antagonist. Nature 339: 593-597.
    • (1989) Nature , vol.339 , pp. 593-597
    • Damm, K.1    Thompson, C.C.2    Evans, R.M.3
  • 15
    • 0025875679 scopus 로고
    • The PML-RARα fusion mRNA encodes a functionally altered RAR
    • de The, H., C. Lavau, A. Marchio, C. Chomienne, L. Degos, and A. Dejean. 1991. The PML-RARα fusion mRNA encodes a functionally altered RAR. Cell 66:675-684.
    • (1991) Cell , vol.66 , pp. 675-684
    • De The, H.1    Lavau, C.2    Marchio, A.3    Chomienne, C.4    Degos, L.5    Dejean, A.6
  • 16
    • 0029002298 scopus 로고
    • Unique response pathways are established by allosteric interactions among nuclear hormone receptors
    • Forman, B. M., K. Umesono, J. Chen, and R. M. Evans. 1995. Unique response pathways are established by allosteric interactions among nuclear hormone receptors. Cell 81:541-550.
    • (1995) Cell , vol.81 , pp. 541-550
    • Forman, B.M.1    Umesono, K.2    Chen, J.3    Evans, R.M.4
  • 17
    • 0027327942 scopus 로고
    • Reconstitution of retinoid X receptor function and combinatorial regulation of other nuclear hormone receptors in the yeast, Saccharomyces cerevisiae
    • Hall, B. L., Z. Smit-McBride, and M. L. Privalsky. 1993. Reconstitution of retinoid X receptor function and combinatorial regulation of other nuclear hormone receptors in the yeast, Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. USA 90:6929-6933.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 6929-6933
    • Hall, B.L.1    Smit-McBride, Z.2    Privalsky, M.L.3
  • 18
    • 0017690245 scopus 로고
    • Carboxypeptidase Y in sequence determination of peptides
    • Hayashi, R. 1977. Carboxypeptidase Y in sequence determination of peptides. Methods Enzymol. 47:84-93.
    • (1977) Methods Enzymol. , vol.47 , pp. 84-93
    • Hayashi, R.1
  • 23
    • 0029790067 scopus 로고    scopus 로고
    • Different DNA elements can modulate the conformation of thyroid hormone receptor heterodimer and its transcriptional activity
    • Ikeda, M., E. C. Wilcox, and W. W. Chin. 1996. Different DNA elements can modulate the conformation of thyroid hormone receptor heterodimer and its transcriptional activity. J. Biol. Chem. 271:23096-23104.
    • (1996) J. Biol. Chem. , vol.271 , pp. 23096-23104
    • Ikeda, M.1    Wilcox, E.C.2    Chin, W.W.3
  • 24
    • 0025780876 scopus 로고
    • Chromosomal translocation t(15:17) in human acute promyelocytic leukemia fuses RARα with a novel putative transcription factor
    • Kakizuka, A., W. H. Miller, K. Umesono, R. P. Warrell, S. R. Frankel, V. V. S. Murty, E. Dmitrovsky, and R. M. Evans. 1991. Chromosomal translocation t(15:17) in human acute promyelocytic leukemia fuses RARα with a novel putative transcription factor. Cell 66:663-674.
    • (1991) Cell , vol.66 , pp. 663-674
    • Kakizuka, A.1    Miller, W.H.2    Umesono, K.3    Warrell, R.P.4    Frankel, S.R.5    Murty, V.V.S.6    Dmitrovsky, E.7    Evans, R.M.8
  • 25
    • 0029584593 scopus 로고
    • Nonsteroidal nuclear receptors: What are genetic studies telling us about their role in real life?
    • Kastner, P., M. Mark, and P. Chambon. 1995. Nonsteroidal nuclear receptors: what are genetic studies telling us about their role in real life? Cell 83:859-870.
    • (1995) Cell , vol.83 , pp. 859-870
    • Kastner, P.1    Mark, M.2    Chambon, P.3
  • 26
    • 0028012039 scopus 로고
    • Different agonist- and antagonist-induced conformational changes in retinoic acid receptors analyzed by protease mapping
    • Keidel, S., P. LeMotte, and C. Apfel. 1994. Different agonist- and antagonist-induced conformational changes in retinoic acid receptors analyzed by protease mapping. Mol. Cell. Biol. 14:287-298.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 287-298
    • Keidel, S.1    LeMotte, P.2    Apfel, C.3
  • 27
    • 0030060417 scopus 로고    scopus 로고
    • Syndrome of resistance to thyroid hormone: Insights into thyroid hormone action
    • Kopp, P., K. Kitajima, and J. L. Jameson. 1996. Syndrome of resistance to thyroid hormone: insights into thyroid hormone action. Proc. Soc. Exp. Biol. Med. 211:49-61.
    • (1996) Proc. Soc. Exp. Biol. Med. , vol.211 , pp. 49-61
    • Kopp, P.1    Kitajima, K.2    Jameson, J.L.3
  • 30
    • 0027416347 scopus 로고
    • Thyroid hormone receptors: Multiple forms, multiple possibilities
    • Lazar, M. A. 1993. Thyroid hormone receptors: multiple forms, multiple possibilities. Endocrinol. Rev. 14:184-193.
    • (1993) Endocrinol. Rev. , vol.14 , pp. 184-193
    • Lazar, M.A.1
  • 31
    • 0027754125 scopus 로고
    • Ligand-dependent conformational changes in thyroid hormone and retinoic acid receptors are potentially enhanced by heterodimerization with retinoic X receptor
    • Leng, X., S. Y. Tsai, B. W. O'Malley, and M. J. Tsai. 1993. Ligand-dependent conformational changes in thyroid hormone and retinoic acid receptors are potentially enhanced by heterodimerization with retinoic X receptor. J. Steroid Biochem. Mol. Biol. 46:643-661.
    • (1993) J. Steroid Biochem. Mol. Biol. , vol.46 , pp. 643-661
    • Leng, X.1    Tsai, S.Y.2    O'Malley, B.W.3    Tsai, M.J.4
  • 32
    • 0029562554 scopus 로고
    • The RXR heterodimers and orphan receptors
    • Mangelsdorf, D. J., and R. M. Evans. 1995. The RXR heterodimers and orphan receptors. Cell 83:841-850.
    • (1995) Cell , vol.83 , pp. 841-850
    • Mangelsdorf, D.J.1    Evans, R.M.2
  • 34
    • 0027402346 scopus 로고
    • Genetic basis of endocrine disease 4: The spectrum of mutations in the androgen receptor gene that cause androgen resistance
    • McPhaul, M. J., M. Marcelli, S. Zoppi, J. E. Griffin, and J. D. Wilson. 1993. Genetic basis of endocrine disease 4: the spectrum of mutations in the androgen receptor gene that cause androgen resistance. J. Clin. Endocrinol. Metab. 76:17-23.
    • (1993) J. Clin. Endocrinol. Metab. , vol.76 , pp. 17-23
    • McPhaul, M.J.1    Marcelli, M.2    Zoppi, S.3    Griffin, J.E.4    Wilson, J.D.5
  • 35
    • 0026236698 scopus 로고
    • Transcriptional factor interactions: Selectors of positive or negative regulation from a single DNA element
    • Miner, J. N., M. I. Diamond, and K. R. Yamamoto. 1991. Transcriptional factor interactions: selectors of positive or negative regulation from a single DNA element. Cell Growth Differ. 2:525-530.
    • (1991) Cell Growth Differ. , vol.2 , pp. 525-530
    • Miner, J.N.1    Diamond, M.I.2    Yamamoto, K.R.3
  • 37
    • 0030916336 scopus 로고    scopus 로고
    • What's up and down with histone deacetylation and transcription?
    • Pazin, M. J., and J. T. Kadonaga. 1997. What's up and down with histone deacetylation and transcription? Cell 89:325-328.
    • (1997) Cell , vol.89 , pp. 325-328
    • Pazin, M.J.1    Kadonaga, J.T.2
  • 38
    • 0027241002 scopus 로고
    • The syndromes of resistance to thyroid hormone
    • Refetoff, S., R. E. Weiss, and S. Usala. 1993. The syndromes of resistance to thyroid hormone. Endocrine Rev. 14:348-399.
    • (1993) Endocrine Rev. , vol.14 , pp. 348-399
    • Refetoff, S.1    Weiss, R.E.2    Usala, S.3
  • 39
    • 0029643780 scopus 로고
    • Crystal structure of the RAR-γ ligand-binding domain bound to all-trans retinoic acid
    • 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.
    • (1995) Nature , vol.378 , pp. 681-689
    • Renaud, J.-P.1    Rochel, N.2    Ruff, M.3    Vivat, V.4    Chambon, P.5    Gronemeyer, H.6    Moras, D.7
  • 41
    • 0027175503 scopus 로고
    • A conserved C-terminal sequence that is deleted in v-ErbA is essential for the biological activities of c-ErbA (the thyroid hormone receptor)
    • Saatcioglu, F., P. Bartunek, T. Deng, M. Zenke, and M. Karin. 1993. A conserved C-terminal sequence that is deleted in v-ErbA is essential for the biological activities of c-ErbA (the thyroid hormone receptor). Mol. Cell. Biol. 13:3675-3685.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 3675-3685
    • Saatcioglu, F.1    Bartunek, P.2    Deng, T.3    Zenke, M.4    Karin, M.5
  • 42
    • 0029657787 scopus 로고    scopus 로고
    • Identification of TRACs (T3 receptor-associating cofactors), a family of cofactors that associate with, and modulate the activity of, nuclear hormone receptors
    • Sande, S., and M. L. Privalsky. 1996. Identification of TRACs (T3 receptor-associating cofactors), a family of cofactors that associate with, and modulate the activity of, nuclear hormone receptors. Mol. Endocrinol. 10:813-825.
    • (1996) Mol. Endocrinol. , vol.10 , pp. 813-825
    • Sande, S.1    Privalsky, M.L.2
  • 43
    • 0024400724 scopus 로고
    • Repression of transcription mediated by a thyroid hormone response element by the v-Erb A oncogene product
    • Sap, J., A. Munoz, H. Schmitt, H. Stunnenberg, and B. Vennstrom. 1989. Repression of transcription mediated by a thyroid hormone response element by the v-Erb A oncogene product. Nature 340:242-244.
    • (1989) Nature , vol.340 , pp. 242-244
    • Sap, J.1    Munoz, A.2    Schmitt, H.3    Stunnenberg, H.4    Vennstrom, B.5
  • 44
    • 0029938795 scopus 로고    scopus 로고
    • Activation and repression by nuclear hormone receptors: Hormone modulates an equilibrium between active and repressive states
    • 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. 16:3807-3813.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 3807-3813
    • Schulman, I.G.1    Juguilon, H.2    Evans, R.M.3
  • 45
    • 0031043055 scopus 로고    scopus 로고
    • The phantom ligand effect: Allosteric control of transcription by the retinoid X receptor
    • Schulman, I. G., C. Li, J. W. R. Schwabe, and R. M. Evans. 1997. The phantom ligand effect: allosteric control of transcription by the retinoid X receptor. Genes Dev. 11:299-308.
    • (1997) Genes Dev. , vol.11 , pp. 299-308
    • Schulman, I.G.1    Li, C.2    Schwabe, J.W.R.3    Evans, R.M.4
  • 46
    • 0028836714 scopus 로고
    • Isolation of proteins that interact specifically with the retinoid X receptor: Two novel orphan receptors
    • 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.
    • (1995) Mol. Endocrinol. , vol.9 , pp. 72-85
    • Seol, W.1    Choi, H.S.2    Moore, D.D.3
  • 47
    • 0029856508 scopus 로고    scopus 로고
    • Two receptor interacting domains in the nuclear hormone receptor corepressor RIP13/N-CoR
    • Seol, W., M. J. Mahon, Y. K. Lee, and D. D. Moore. 1996. Two receptor interacting domains in the nuclear hormone receptor corepressor RIP13/N-CoR. Mol. Endocrinol. 10:1646-1655.
    • (1996) Mol. Endocrinol. , vol.10 , pp. 1646-1655
    • Seol, W.1    Mahon, M.J.2    Lee, Y.K.3    Moore, D.D.4
  • 48
    • 0028283503 scopus 로고
    • Molecular mechanisms of action of steroid/thyroid hormone receptor superfamily members
    • Tsai, M. J., and B. W. O'Malley. 1994. Molecular mechanisms of action of steroid/thyroid hormone receptor superfamily members. Annu. Rev. Biochem. 63:451-483.
    • (1994) Annu. Rev. Biochem. , vol.63 , pp. 451-483
    • Tsai, M.J.1    O'Malley, B.W.2
  • 50
    • 0031042762 scopus 로고    scopus 로고
    • Unique requirements for retinoid dependent transcriptional activation by the orphan receptor LXR
    • Willy, P. J., and D. J. Mangelsdorf. 1997. Unique requirements for retinoid dependent transcriptional activation by the orphan receptor LXR. Genes Dev. 11:289-298.
    • (1997) Genes Dev. , vol.11 , pp. 289-298
    • Willy, P.J.1    Mangelsdorf, D.J.2
  • 51
    • 0030922545 scopus 로고    scopus 로고
    • Transcriptional control - Sinful repression
    • Wolffe, A. P. 1997. Transcriptional control - sinful repression. Nature 387: 16-17.
    • (1997) Nature , vol.387 , pp. 16-17
    • Wolffe, A.P.1
  • 52
    • 0030988565 scopus 로고    scopus 로고
    • Thyroid hormone resistance syndrome manifests as an aberrant interaction between mutant T3 receptors and transcriptional corepressors
    • Yoh, S. M., V. K. K. Chatterjee, and M. L. Privalsky. 1997. Thyroid hormone resistance syndrome manifests as an aberrant interaction between mutant T3 receptors and transcriptional corepressors. Mol. Endocrinol. 11:470-480.
    • (1997) Mol. Endocrinol. , vol.11 , pp. 470-480
    • Yoh, S.M.1    Chatterjee, V.K.K.2    Privalsky, M.L.3
  • 53
    • 0029837730 scopus 로고    scopus 로고
    • A nuclear hormone receptor corepressor mediates transcriptional silencing by receptors with distinct repression domains
    • Zamir, I., H. P. Harding, G. B. Atkins, A. Horlein, C. K. Glass, M. Rosenfeld, and M. A. Lazar. 1996. A nuclear hormone receptor corepressor mediates transcriptional silencing by receptors with distinct repression domains. Mol. Cell. Biol. 16:5458-5465.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 5458-5465
    • Zamir, I.1    Harding, H.P.2    Atkins, G.B.3    Horlein, A.4    Glass, C.K.5    Rosenfeld, M.6    Lazar, M.A.7
  • 54
    • 0030991152 scopus 로고    scopus 로고
    • Stoichiometric and steric principles governing repression by nuclear hormone receptors
    • Zamir, I., J. Zhang, and M. A. Lazar. 1997. Stoichiometric and steric principles governing repression by nuclear hormone receptors. Genes Dev. 11: 835-846.
    • (1997) Genes Dev. , vol.11 , pp. 835-846
    • Zamir, I.1    Zhang, J.2    Lazar, M.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.