메뉴 건너뛰기




Volumn 137, Issue 2, 1996, Pages 712-721

Understanding the Molecular Mechanism of Dominant Negative Action of Mutant Thyroid Hormone β1-Receptors: The Important Role of the Wild-Type/Mutant Receptor Heterodimer

Author keywords

[No Author keywords available]

Indexed keywords

DIMER; LIOTHYRONINE; RECEPTOR SUBTYPE; THYROID HORMONE RECEPTOR;

EID: 0030023159     PISSN: 00137227     EISSN: None     Source Type: Journal    
DOI: 10.1210/endo.137.2.8593822     Document Type: Article
Times cited : (25)

References (38)
  • 1
    • 0028911237 scopus 로고
    • New insights into the structure and function of the thyroid hormone receptor
    • Cheng S-y 1995 New insights into the structure and function of the thyroid hormone receptor. J Biomed Sci 2:77-89
    • (1995) J Biomed Sci , vol.2 , pp. 77-89
    • S-y, C.1
  • 4
    • 0025729027 scopus 로고
    • 3,5,3′-Triiodothyronine receptor auxiliary protein (TRAP) enhances receptor binding by interactions within the thyroid hormone response element
    • Beebe JS, Darling DS, Chin WW 1991 3,5,3′-Triiodothyronine receptor auxiliary protein (TRAP) enhances receptor binding by interactions within the thyroid hormone response element. Mol Endocrinol 5:85-93
    • (1991) Mol Endocrinol , vol.5 , pp. 85-93
    • Beebe, J.S.1    Darling, D.S.2    Chin, W.W.3
  • 6
    • 0026592518 scopus 로고
    • Retinoid X receptor interacts with nuclear receptors in retinoic acid, thyroid hormone and vitamin D3 signalling
    • Kliewer SA, Umesono K, Mangelsdorf DJ, Evans RM 1992 Retinoid X receptor interacts with nuclear receptors in retinoic acid, thyroid hormone and vitamin D3 signalling. Nature 355:446-449
    • (1992) Nature , vol.355 , pp. 446-449
    • Kliewer, S.A.1    Umesono, K.2    Mangelsdorf, D.J.3    Evans, R.M.4
  • 7
    • 0026608464 scopus 로고
    • H-2RIIBP (RXR beta) heterodimerization provides a mechanism for combinatorial diversity in the regulation of retinoic acid and thyroid hormone responsive genes
    • Marks MS, Hallenbeck PL, Nagata T, Segars JH, Appella E, Nikodem VM, Ozato K 1992 H-2RIIBP (RXR beta) heterodimerization provides a mechanism for combinatorial diversity in the regulation of retinoic acid and thyroid hormone responsive genes. EMBOJ 11:1419-1435
    • (1992) EMBOJ , vol.11 , pp. 1419-1435
    • Marks, M.S.1    Hallenbeck, P.L.2    Nagata, T.3    Segars, J.H.4    Appella, E.5    Nikodem, V.M.6    Ozato, K.7
  • 8
    • 0026570217 scopus 로고
    • Purification, cloning, and RXR identity of the HeLa cell factor with which RAR or TR heterodimerizes to bind target sequences efficiently
    • Leid M, Kastner P, Lyons R, Nakshatri H, Saunders M, Zacharewski T, Chen JY, Staub A, Gamier JM, Mader S, et al 1992 Purification, cloning, and RXR identity of the HeLa cell factor with which RAR or TR heterodimerizes to bind target sequences efficiently. Cell 68:377-395
    • (1992) Cell , vol.68 , pp. 377-395
    • Leid, M.1    Kastner, P.2    Lyons, R.3    Nakshatri, H.4    Saunders, M.5    Zacharewski, T.6    Chen, J.Y.7    Staub, A.8    Gamier, J.M.9    Mader, S.10
  • 9
    • 0026613089 scopus 로고
    • 3-recep-tor/retinoid x receptor heterodimer binding to DNA
    • 3-recep-tor/retinoid x receptor heterodimer binding to DNA. J Biol Chem 267:23248-28252
    • (1992) J Biol Chem , vol.267 , pp. 23248-28252
    • Yen, P.M.1    Sugawara, A.2    Chin, W.W.3
  • 11
    • 0027225769 scopus 로고
    • Regulation of retinoid and thyroid hormone action through homodimeric and heterodimeric receptors
    • Zhang XK, Pfahl M 1993 Regulation of retinoid and thyroid hormone action through homodimeric and heterodimeric receptors. Trends Endocrinol Metab 4:10-16
    • (1993) Trends Endocrinol Metab , vol.4 , pp. 10-16
    • Zhang, X.K.1    Pfahl, M.2
  • 12
    • 0025754448 scopus 로고
    • Ligand-binding domain of thyroid hormone receptors modulates DNA binding and determines their bifunctional roles
    • Zhang XK, Wills KN, Graupner G, Tzukerman M, Hermann T, Pfahl M 1991 Ligand-binding domain of thyroid hormone receptors modulates DNA binding and determines their bifunctional roles. New Biol 3:169-181
    • (1991) New Biol , vol.3 , pp. 169-181
    • Zhang, X.K.1    Wills, K.N.2    Graupner, G.3    Tzukerman, M.4    Hermann, T.5    Pfahl, M.6
  • 14
    • 0027241002 scopus 로고
    • The syndromes of resistance to thyroid hormone
    • Refetoff S, Weiss RE, Usala SJ 1993 The syndromes of resistance to thyroid hormone. Endocr Rev 14:348-399
    • (1993) Endocr Rev , vol.14 , pp. 348-399
    • Refetoff, S.1    Weiss, R.E.2    Usala, S.J.3
  • 15
    • 0028873268 scopus 로고
    • New developments in clinical and genetic aspects of thyroid hormone resistance syndromes
    • Usala SJ 1995 New developments in clinical and genetic aspects of thyroid hormone resistance syndromes. Endocrinologist 5:68-76
    • (1995) Endocrinologist , vol.5 , pp. 68-76
    • Usala, S.J.1
  • 16
    • 0026539146 scopus 로고
    • Variable transcriptional activity and ligand binding of mutant β1 3,5,3′-triiodothyronine receptors from four families with generalized resistance to thyroid hormone
    • Meier CA, Dickstein BM, Ashizawa K, McClaskey JH, Muchmore P, Ransom SC, Menke JB, Hao EH, Usala SJ, Bereu BB, et al 1992 Variable transcriptional activity and ligand binding of mutant β1 3,5,3′-triiodothyronine receptors from four families with generalized resistance to thyroid hormone. Mol Endocrinol 6:248-258
    • (1992) Mol Endocrinol , vol.6 , pp. 248-258
    • Meier, C.A.1    Dickstein, B.M.2    Ashizawa, K.3    McClaskey, J.H.4    Muchmore, P.5    Ransom, S.C.6    Menke, J.B.7    Hao, E.H.8    Usala, S.J.9    Bereu, B.B.10
  • 17
    • 0026715866 scopus 로고
    • Thyroid hormone receptor mutants that cause resistance to thyroid hormone
    • Nagaya T, Madison LD, Jameson JL 1992 Thyroid hormone receptor mutants that cause resistance to thyroid hormone. J Biol Chem 267:13014-13019
    • (1992) J Biol Chem , vol.267 , pp. 13014-13019
    • Nagaya, T.1    Madison, L.D.2    Jameson, J.L.3
  • 18
    • 0027998335 scopus 로고
    • 3)-binding domain of the thyroid hormone receptor (TR) β gene that appears to be devoid of natural mutations may not be detected because they are unlikely to produce the clinical phenotype of resistance to thyroid hormone
    • 3)-binding domain of the thyroid hormone receptor (TR) β gene that appears to be devoid of natural mutations may not be detected because they are unlikely to produce the clinical phenotype of resistance to thyroid hormone. J Clin Invest 94:607-615
    • (1994) J Clin Invest , vol.94 , pp. 607-615
    • Hayashi, Y.1    Sunthornthepvarakul, T.2    Refetoff, S.3
  • 20
    • 0027324301 scopus 로고
    • Thyroid hormone receptor dimerization is required for dominant negative inhibition by mutations that cause thyroid hormone resistance
    • Nagaya T Jameson JL 1993 Thyroid hormone receptor dimerization is required for dominant negative inhibition by mutations that cause thyroid hormone resistance. J Biol Chem 268:15766-15771
    • (1993) J Biol Chem , vol.268 , pp. 15766-15771
    • Nagaya, T.1    Jameson, J.L.2
  • 21
    • 0027370375 scopus 로고
    • Dominant negative inhibition by mutant thyroid hormone receptors is thyroid hormone response element and receptor isoform specific
    • Zavacki AM, Harney JW, Brent GA, Larsen PR 1993 Dominant negative inhibition by mutant thyroid hormone receptors is thyroid hormone response element and receptor isoform specific. Mol Endocrinol 7:1319-1330
    • (1993) Mol Endocrinol , vol.7 , pp. 1319-1330
    • Zavacki, A.M.1    Harney, J.W.2    Brent, G.A.3    Larsen, P.R.4
  • 22
    • 0029258452 scopus 로고
    • Cell type-dependent modulation of the dominant negative action of human mutant thyroid hormone β1 receptors
    • Wong R, Zhu XG, Pineda MA, Cheng SY, Weintraub BD 1995 Cell type-dependent modulation of the dominant negative action of human mutant thyroid hormone β1 receptors. Mol Med 1:306-319
    • (1995) Mol Med , vol.1 , pp. 306-319
    • Wong, R.1    Zhu, X.G.2    Pineda, M.A.3    Cheng, S.Y.4    Weintraub, B.D.5
  • 23
    • 0024457916 scopus 로고
    • A domain containing leucine-zipper-like motifs mediate novel in vivo interactions between the thyroid hormone and retinoic acid receptors
    • Forman BM, Yang CR, Au M, Casanova J, Ghysdael J, Samuels HH 1989 A domain containing leucine-zipper-like motifs mediate novel in vivo interactions between the thyroid hormone and retinoic acid receptors. Mol Endocrinol 3:1610-1626
    • (1989) Mol Endocrinol , vol.3 , pp. 1610-1626
    • Forman, B.M.1    Yang, C.R.2    Au, M.3    Casanova, J.4    Ghysdael, J.5    Samuels, H.H.6
  • 24
    • 0028037369 scopus 로고
    • Molecular mechanisms of dominant negative activity by nuclear hormone receptors
    • Yen P, Chin WW 1994 Molecular mechanisms of dominant negative activity by nuclear hormone receptors. Mol Endocrinol 8:1450-1454
    • (1994) Mol Endocrinol , vol.8 , pp. 1450-1454
    • Yen, P.1    Chin, W.W.2
  • 25
    • 0028896912 scopus 로고
    • Modulation of thyroid hormone action by mutant thyroid hormone receptors, c-erbAa2 and peroxisome proliferation-activated receptor: Evidence for different mechanisms of inhibition
    • Meier-Heusler SC, Zhu XG, Juge-Aubry C, Pernin A, Burger AG, Cheng SY, Meier CA 1995 Modulation of thyroid hormone action by mutant thyroid hormone receptors, c-erbAa2 and peroxisome proliferation-activated receptor: evidence for different mechanisms of inhibition. Mol Cell Endocrinol 107:55-66
    • (1995) Mol Cell Endocrinol , vol.107 , pp. 55-66
    • Meier-Heusler, S.C.1    Zhu, X.G.2    Juge-Aubry, C.3    Pernin, A.4    Burger, A.G.5    Cheng, S.Y.6    Meier, C.A.7
  • 26
    • 0025854410 scopus 로고
    • An essential role of domain D in the hormone-binding activity of human β1 thyroid hormone nuclear receptor
    • Lin KH, Parkison C, McPhie P, Cheng SY 1991 An essential role of domain D in the hormone-binding activity of human β1 thyroid hormone nuclear receptor. Mol Endocrinol 5:485-492
    • (1991) Mol Endocrinol , vol.5 , pp. 485-492
    • Lin, K.H.1    Parkison, C.2    McPhie, P.3    Cheng, S.Y.4
  • 27
    • 0025903633 scopus 로고
    • Effects of varying the position of thyroid hormone response elements within the rat growth hormone promoter: Implications for positive and negative regulations by 3,5,3′-triiodothyronine
    • Brent GA, Williams GR, Harney JW, Forman BM, Samuels HH, Moore DD, Larsen PR 1991 Effects of varying the position of thyroid hormone response elements within the rat growth hormone promoter: implications for positive and negative regulations by 3,5,3′-triiodothyronine. Mol Endocrinol 5:542-548
    • (1991) Mol Endocrinol , vol.5 , pp. 542-548
    • Brent, G.A.1    Williams, G.R.2    Harney, J.W.3    Forman, B.M.4    Samuels, H.H.5    Moore, D.D.6    Larsen, P.R.7
  • 28
    • 0026732714 scopus 로고
    • Phosphorylation stimulates the transcriptional activity of the human β1 thyroid hormone nuclear receptor
    • Lin KH, Ashizawa K, Cheng SY 1992 Phosphorylation stimulates the transcriptional activity of the human β1 thyroid hormone nuclear receptor. Proc Natl Acad Sci USA 89:7737-7741
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 7737-7741
    • Lin, K.H.1    Ashizawa, K.2    Cheng, S.Y.3
  • 29
    • 0028122418 scopus 로고
    • Phosphorylation enhances the target gene sequence-dependent dimerization of thyroid hormone receptor with the retinoid X receptor
    • Bhat MK, Ashizawa K, Cheng SY 1994 Phosphorylation enhances the target gene sequence-dependent dimerization of thyroid hormone receptor with the retinoid X receptor. Proc Natl Acad Sci USA 91:7927-7931
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 7927-7931
    • Bhat, M.K.1    Ashizawa, K.2    Cheng, S.Y.3
  • 30
    • 0026495763 scopus 로고
    • New insights on the mechanism(s) of the dominant negative effect of mutant thyroid hormone receptor in generalized resistance to thyroid hormone
    • Yen PM, Sugawara A, Refetoff S, Chin WW 1992 New insights on the mechanism(s) of the dominant negative effect of mutant thyroid hormone receptor in generalized resistance to thyroid hormone. J Clin Invest 90:1825-1831
    • (1992) J Clin Invest , vol.90 , pp. 1825-1831
    • Yen, P.M.1    Sugawara, A.2    Refetoff, S.3    Chin, W.W.4
  • 31
    • 0026320853 scopus 로고
    • Characterization of seven novel mutations of the c-erbA beta gene in unrelated kindreds with generalized thyroid hormone resistance. Evidence for two hot spot regions of the ligand binding domain
    • Parrilla R, Mixson AJ, McPherson JA, McClaskey JH, Weintraub BD 1991 Characterization of seven novel mutations of the c-erbA beta gene in unrelated kindreds with generalized thyroid hormone resistance. Evidence for two hot spot regions of the ligand binding domain. J Clin Invest 88:2123-2130
    • (1991) J Clin Invest , vol.88 , pp. 2123-2130
    • Parrilla, R.1    Mixson, A.J.2    McPherson, J.A.3    McClaskey, J.H.4    Weintraub, B.D.5
  • 32
    • 0027469410 scopus 로고
    • The relative expression of mutant and normal thyroid hormone receptor genes in patients with generalized resistance to thyroid hormone determined by estimation of their specific messenger ribonucleic acid products
    • Hayashi Y, Janssen OE, Weiss RE, Murata Y, Seo H, Refetoff S 1993 The relative expression of mutant and normal thyroid hormone receptor genes in patients with generalized resistance to thyroid hormone determined by estimation of their specific messenger ribonucleic acid products. J Clin Endocrinol Metab 76:64-69
    • (1993) J Clin Endocrinol Metab , vol.76 , pp. 64-69
    • Hayashi, Y.1    Janssen, O.E.2    Weiss, R.E.3    Murata, Y.4    Seo, H.5    Refetoff, S.6
  • 34
    • 0029092227 scopus 로고
    • The structure of the carboxyl-terminal region of thyroid hormone nuclear receptor and its role in hormone dependent intermolecular interactions
    • Bhat MK, McPhie P, Ting YT, Zhu XG, Cheng SY 1995 The structure of the carboxyl-terminal region of thyroid hormone nuclear receptor and its role in hormone dependent intermolecular interactions. Biochemistry 34:10591-10599
    • (1995) Biochemistry , vol.34 , pp. 10591-10599
    • Bhat, M.K.1    McPhie, P.2    Ting, Y.T.3    Zhu, X.G.4    Cheng, S.Y.5
  • 35
    • 0029043756 scopus 로고
    • Studies on the repression of basal transcription (silencing) by artificial and natural human thyroid hormone receptor-β mutants
    • Yen PM, Wilcox EC, Hayashi Y, Refetoff S, Chin WW 1995 Studies on the repression of basal transcription (silencing) by artificial and natural human thyroid hormone receptor-β mutants. Endocrinology 136:2845-2851
    • (1995) Endocrinology , vol.136 , pp. 2845-2851
    • Yen, P.M.1    Wilcox, E.C.2    Hayashi, Y.3    Refetoff, S.4    Chin, W.W.5
  • 36
    • 0015965095 scopus 로고
    • Asymmetrical hemoglobin hybrids. An approach to the study of subunit interactions
    • Bunn HF, McDonough M 1974 Asymmetrical hemoglobin hybrids. An approach to the study of subunit interactions. Biochemistry 13:988-993
    • (1974) Biochemistry , vol.13 , pp. 988-993
    • Bunn, H.F.1    McDonough, M.2
  • 37
    • 0025337579 scopus 로고
    • Relationship of c-erbA mRNA content to tissue triiodothyronine nuclear binding capacity and function in developing and adult rats
    • Strait KA, Schwartz HL, Perez-Castillo A, Oppenheimer JH 1990 Relationship of c-erbA mRNA content to tissue triiodothyronine nuclear binding capacity and function in developing and adult rats. J Biol Chem 265:10514-10521
    • (1990) J Biol Chem , vol.265 , pp. 10514-10521
    • Strait, K.A.1    Schwartz, H.L.2    Perez-Castillo, A.3    Oppenheimer, J.H.4
  • 38
    • 0026651722 scopus 로고
    • Quantitation of rat tissue thyroid hormone binding receptor isoforms by immunoprecipitation of nuclear triiodothyronine binding capacity
    • Schwartz HL, Strait KA, Ling NC, Oppenheimer JH 1992 Quantitation of rat tissue thyroid hormone binding receptor isoforms by immunoprecipitation of nuclear triiodothyronine binding capacity. J Biol Chem 267:11794-11799
    • (1992) J Biol Chem , vol.267 , pp. 11794-11799
    • Schwartz, H.L.1    Strait, K.A.2    Ling, N.C.3    Oppenheimer, J.H.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.