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Volumn 199, Issue 1-2, 2003, Pages 61-72

Sequences required for the transition from monomeric to homodimeric forms of thyroid hormone receptor α and v-erbA

Author keywords

Direct repeat; Everted repeat; Oncoprotein; Repressor; Thyroid hormone receptor; v erbA

Indexed keywords

ISOLEUCINE; METHYL GROUP; ONCOPROTEIN; RETINOID X RECEPTOR; THYROID HORMONE RECEPTOR; THYROID HORMONE RECEPTOR ALPHA; UNCLASSIFIED DRUG;

EID: 0037474127     PISSN: 03037207     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0303-7207(02)00299-X     Document Type: Article
Times cited : (5)

References (33)
  • 1
    • 0029097233 scopus 로고
    • A transcriptional co-repressor that interacts with nuclear hormone receptors
    • Chen D.J., Evans R.M. A transcriptional co-repressor that interacts with nuclear hormone receptors. Nature. 377:1995;454-457.
    • (1995) Nature , vol.377 , pp. 454-457
    • Chen, D.J.1    Evans, R.M.2
  • 2
    • 0027253629 scopus 로고
    • Different dimerization activities of alpha and beta thyroid hormone receptor isoforms
    • Darling D.S., Carter R.L., Yen P.M., Welborn J.Y., Chin W.W., Umeda P.K. Different dimerization activities of alpha and beta thyroid hormone receptor isoforms. J. Biol. Chem. 268:1993;10221-10227.
    • (1993) J. Biol. Chem. , vol.268 , pp. 10221-10227
    • Darling, D.S.1    Carter, R.L.2    Yen, P.M.3    Welborn, J.Y.4    Chin, W.W.5    Umeda, P.K.6
  • 3
    • 0029995572 scopus 로고    scopus 로고
    • Recessive resistance to thyroid hormone in mice lacking thyroid hormone receptor beta: Evidence for tissue-specific modulation of receptor function
    • Forrest D., Hanebuth E., Smeyne R.J., Everds N., Stewart C.L., Wehner J.M., Curran T. Recessive resistance to thyroid hormone in mice lacking thyroid hormone receptor beta: evidence for tissue-specific modulation of receptor function. EMBO J. 15:1996;3006-3015.
    • (1996) EMBO J. , vol.15 , pp. 3006-3015
    • Forrest, D.1    Hanebuth, E.2    Smeyne, R.J.3    Everds, N.4    Stewart, C.L.5    Wehner, J.M.6    Curran, T.7
  • 4
    • 0029947835 scopus 로고    scopus 로고
    • Thyroid hormone receptor beta is essential for development of auditory function
    • Forrest D., Erway L.C., Ng L., Altschuler R., Curran T. Thyroid hormone receptor beta is essential for development of auditory function. Nat. Genet. 13:1996;354-357.
    • (1996) Nat. Genet. , vol.13 , pp. 354-357
    • Forrest, D.1    Erway, L.C.2    Ng, L.3    Altschuler, R.4    Curran, T.5
  • 6
    • 0028332036 scopus 로고
    • Differential recognition of target genes by nuclear receptor monomers, dimers, and heterodimers
    • Glass C.K. Differential recognition of target genes by nuclear receptor monomers, dimers, and heterodimers. Endocr. Rev. 15:1994;391-407.
    • (1994) Endocr. Rev. , vol.15 , pp. 391-407
    • Glass, C.K.1
  • 7
    • 0032562589 scopus 로고    scopus 로고
    • A novel multifunctional motif in the amino-terminal A/B domain of TRα modulates DNA binding and receptor dimerization
    • Hadzic E., Habeos I., Raaka B.M., Samuels H.H. A novel multifunctional motif in the amino-terminal A/B domain of TRα modulates DNA binding and receptor dimerization. J. Biol. Chem. 273:1998;10270-10278.
    • (1998) J. Biol. Chem. , vol.273 , pp. 10270-10278
    • Hadzic, E.1    Habeos, I.2    Raaka, B.M.3    Samuels, H.H.4
  • 8
    • 0029060144 scopus 로고
    • Ligand-independent and -dependent functions of thyroid hormone receptor isoforms depend upon their distinct amino termini
    • Hollenberg A.N., Monden T., Wondisford F.E. Ligand-independent and -dependent functions of thyroid hormone receptor isoforms depend upon their distinct amino termini. J. Biol. Chem. 270:1995;14274-14280.
    • (1995) J. Biol. Chem. , vol.270 , pp. 14274-14280
    • Hollenberg, A.N.1    Monden, T.2    Wondisford, F.E.3
  • 10
    • 0025326334 scopus 로고
    • Gene splicing by overlap extension: Tailor-made genes using the polymerase chain reaction
    • Horton R.M., Cai Z.L., Ho S.N., Pease L.R. Gene splicing by overlap extension: tailor-made genes using the polymerase chain reaction. Biotechniques. 8:1990;528-535.
    • (1990) Biotechniques , vol.8 , pp. 528-535
    • Horton, R.M.1    Cai, Z.L.2    Ho, S.N.3    Pease, L.R.4
  • 11
    • 0027198384 scopus 로고
    • Nonbiased identification of DNA sequences that bind thyroid hormone receptor alpha 1 with high affinity
    • Katz R.W., Koenig R.J. Nonbiased identification of DNA sequences that bind thyroid hormone receptor alpha 1 with high affinity. J. Biol. Chem. 268:1993;19392-19397.
    • (1993) J. Biol. Chem. , vol.268 , pp. 19392-19397
    • Katz, R.W.1    Koenig, R.J.2
  • 14
    • 0027381438 scopus 로고
    • The patterns of binding of RAR, RXR, and TR homo- and heterodimers to direct repeats are dictated by the binding specificities of the DNA binding domains
    • Mader S., Chen J., Chen Z., Whit J., Chambon P., Gronemeyer H. The patterns of binding of RAR, RXR, and TR homo- and heterodimers to direct repeats are dictated by the binding specificities of the DNA binding domains. EMBO J. 13:1993;5029-5041.
    • (1993) EMBO J. , vol.13 , pp. 5029-5041
    • Mader, S.1    Chen, J.2    Chen, Z.3    Whit, J.4    Chambon, P.5    Gronemeyer, H.6
  • 15
    • 0029562554 scopus 로고
    • The RXR heterodimers and orphan receptors
    • Mangelsdorf D.J., Evans R.M. The RXR heterodimers and orphan receptors. Cell. 83:1995;841-850.
    • (1995) Cell , vol.83 , pp. 841-850
    • Mangelsdorf, D.J.1    Evans, R.M.2
  • 16
    • 0027324301 scopus 로고
    • Thyroid hormone receptor dimerization is required for dominant negative inhibition by mutations that cause thyroid hormone resistance
    • Nagaya T., Jameson J.L. Thyroid hormone receptor dimerization is required for dominant negative inhibition by mutations that cause thyroid hormone resistance. J. Biol. Chem. 268:1993;15766-15771.
    • (1993) J. Biol. Chem. , vol.268 , pp. 15766-15771
    • Nagaya, T.1    Jameson, J.L.2
  • 17
    • 0025081502 scopus 로고
    • Mutational analysis identifies a new functional domain of the thyroid hormone receptor
    • O'Donnell A.L., Koenig R.J. Mutational analysis identifies a new functional domain of the thyroid hormone receptor. Mol. Endocrinol. 4:1990;715-720.
    • (1990) Mol. Endocrinol. , vol.4 , pp. 715-720
    • O'Donnell, A.L.1    Koenig, R.J.2
  • 18
    • 0029736983 scopus 로고    scopus 로고
    • Two distinct dimerization interfaces differentially modulate target gene specificity of nuclear hormone receptors
    • Perlmann T., Umesono K., Rangarajan P., Forman B.M., Evans R.M. Two distinct dimerization interfaces differentially modulate target gene specificity of nuclear hormone receptors. Mol. Endocrinol. 10:1996;958-966.
    • (1996) Mol. Endocrinol. , vol.10 , pp. 958-966
    • Perlmann, T.1    Umesono, K.2    Rangarajan, P.3    Forman, B.M.4    Evans, R.M.5
  • 19
    • 0023948013 scopus 로고
    • Multiple sequences encoding potential thyroid hormone receptors isolated from mouse skeletal muscle cDNA libraries
    • Prost E., Koenig R.J., Moore D.D., Larsen P.R., Whalen R.G. Multiple sequences encoding potential thyroid hormone receptors isolated from mouse skeletal muscle cDNA libraries. Nucleic Acids Res. 16:1988;6248.
    • (1988) Nucleic Acids Res. , vol.16 , pp. 6248
    • Prost, E.1    Koenig, R.J.2    Moore, D.D.3    Larsen, P.R.4    Whalen, R.G.5
  • 20
    • 0022979576 scopus 로고
    • CAT vectors for analysis of eukaryotic promoters and enhancers
    • Prost E., Moore D.D. CAT vectors for analysis of eukaryotic promoters and enhancers. Gene. 45:1986;107-111.
    • (1986) Gene , vol.45 , pp. 107-111
    • Prost, E.1    Moore, D.D.2
  • 21
    • 0035805580 scopus 로고    scopus 로고
    • Definition of the surface in the thyroid hormone receptor ligand binding domain for association as homodimers and heterodimers with retinoid X receptor
    • Ribeiro R.C., Feng W., Wagner R.L., Costa C., Pereira A.C., Apriletti J.W., Fletterick R.J., Baxter J.D. Definition of the surface in the thyroid hormone receptor ligand binding domain for association as homodimers and heterodimers with retinoid X receptor. J. Biol. Chem. 276:2001;14987-14995.
    • (2001) J. Biol. Chem. , vol.276 , pp. 14987-14995
    • Ribeiro, R.C.1    Feng, W.2    Wagner, R.L.3    Costa, C.4    Pereira, A.C.5    Apriletti, J.W.6    Fletterick, R.J.7    Baxter, J.D.8
  • 22
    • 0035962667 scopus 로고    scopus 로고
    • Avian erythroleukemia: A model for corepressor function in cancer
    • Rietveld L.E., Caldenhoven E., Stunnenberg H.G. Avian erythroleukemia: a model for corepressor function in cancer. Oncogene. 20:2001;3100-3109.
    • (2001) Oncogene , vol.20 , pp. 3100-3109
    • Rietveld, L.E.1    Caldenhoven, E.2    Stunnenberg, H.G.3
  • 23
    • 0034454583 scopus 로고    scopus 로고
    • Nuclear hormone receptor coregulators in action: Diversity for shared tasks
    • Robyr D., Wolffe A.P., Wahli W. Nuclear hormone receptor coregulators in action: diversity for shared tasks. Mol. Endocrinol. 14:2000;329-347.
    • (2000) Mol. Endocrinol. , vol.14 , pp. 329-347
    • Robyr, D.1    Wolffe, A.P.2    Wahli, W.3
  • 24
    • 0034731442 scopus 로고    scopus 로고
    • Dimerization interfaces of v-erbA homodimers and heterodimers with retinoid X receptor α
    • Shen Q., Subauste J.S. Dimerization interfaces of v-erbA homodimers and heterodimers with retinoid X receptor α J. Biol. Chem. 275:2000;41018-41027.
    • (2000) J. Biol. Chem. , vol.275 , pp. 41018-41027
    • Shen, Q.1    Subauste, J.S.2
  • 25
    • 0032158788 scopus 로고    scopus 로고
    • Characterization of the DNA-binding and dominant negative activity of v-erbA homodimers
    • Subauste J.S., Koenig R.J. Characterization of the DNA-binding and dominant negative activity of v-erbA homodimers. Mol. Endocrinol. 12:1998;1380-1392.
    • (1998) Mol. Endocrinol. , vol.12 , pp. 1380-1392
    • Subauste, J.S.1    Koenig, R.J.2
  • 26
    • 0028907541 scopus 로고
    • Comparison of the DNA binding specificity and function of v-erbA and thyroid hormone receptor α1
    • Subauste J.S., Koenig R.J. Comparison of the DNA binding specificity and function of v-erbA and thyroid hormone receptor α1. J. Biol. Chem. 270:1995;7957-7962.
    • (1995) J. Biol. Chem. , vol.270 , pp. 7957-7962
    • Subauste, J.S.1    Koenig, R.J.2
  • 27
    • 0028032246 scopus 로고
    • DNA binding specificity and function of retinoid X receptor alpha
    • Subauste J.S., Katz R.W., Koenig R.J. DNA binding specificity and function of retinoid X receptor alpha. J. Biol. Chem. 269:1994;30232-30237.
    • (1994) J. Biol. Chem. , vol.269 , pp. 30232-30237
    • Subauste, J.S.1    Katz, R.W.2    Koenig, R.J.3
  • 28
    • 0004655257 scopus 로고
    • Trans-activation by thyroid hormone receptors: Functional parallels with steroid hormone receptors
    • Thompson C.C., Evans R.M. Trans-activation by thyroid hormone receptors: functional parallels with steroid hormone receptors. Proc. Natl. Acad. Sci. USA. 86:1989;3494-3498.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 3494-3498
    • Thompson, C.C.1    Evans, R.M.2
  • 30
    • 0029019747 scopus 로고
    • Role of the N terminus in DNA recognition by the v-erbA protein, an oncogenic derivate of a thyroid hormone receptor
    • Wong C.-W., Privalsky M.L. Role of the N terminus in DNA recognition by the v-erbA protein, an oncogenic derivate of a thyroid hormone receptor. Mol. Endocrinol. 9:1995;551-562.
    • (1995) Mol. Endocrinol. , vol.9 , pp. 551-562
    • Wong, C.-W.1    Privalsky, M.L.2
  • 31
  • 33
    • 0028313996 scopus 로고
    • The dimerization interfaces formed between the DNA binding domains of RXR, RAR, and TR determine the binding specificity and polarity of the full length receptors to direct repeats
    • Zechel C., Shen X., Chambon P., Gronemeyer H. The dimerization interfaces formed between the DNA binding domains of RXR, RAR, and TR determine the binding specificity and polarity of the full length receptors to direct repeats. EMBO J. 13:1994;1425-1433.
    • (1994) EMBO J. , vol.13 , pp. 1425-1433
    • Zechel, C.1    Shen, X.2    Chambon, P.3    Gronemeyer, H.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.