메뉴 건너뛰기




Volumn 5, Issue 2, 1994, Pages 95-103

Vertebrate receptors: Molecular biology, dimerization and response elements

Author keywords

Heterodimers; Homodimers; Retinoic acid receptors; Steroid hormone receptors; Thyroid hormone receptors; Vitamin D3 receptors

Indexed keywords

CALCITRIOL RECEPTOR; CELL RECEPTOR; DNA; RETINOIC ACID RECEPTOR; STEROID RECEPTOR; THYROID HORMONE RECEPTOR; TRANSCRIPTION FACTOR;

EID: 0028415542     PISSN: 10849521     EISSN: None     Source Type: Journal    
DOI: 10.1006/scel.1994.1013     Document Type: Article
Times cited : (67)

References (56)
  • 1
    • 0023913120 scopus 로고
    • The steroid and thyroid hormone receptor family
    • Evans RM (1988) The steroid and thyroid hormone receptor family. Science 240:889-895
    • (1988) Science , vol.240 , pp. 889-895
    • Evans, R.M.1
  • 2
    • 0023797380 scopus 로고
    • Nuclear receptors enhance our understanding of transcription regulation
    • Green S, Chambon P (1988) Nuclear receptors enhance our understanding of transcription regulation. Trends Genet 4:309
    • (1988) Trends Genet , vol.4 , pp. 309
    • Green, S.1    Chambon, P.2
  • 3
    • 0024545638 scopus 로고
    • Gene regulation by steroid hormones
    • Beato M (1989) Gene regulation by steroid hormones. Cell 56:335-344
    • (1989) Cell , vol.56 , pp. 335-344
    • Beato, M.1
  • 5
    • 0027222793 scopus 로고
    • Structure of the retinoid X receptor a DNA binding domain: A helix required for homodimeric DNA binding
    • Lee M-S, Kliewer S, Provencal J, Wright P, Evans RM (1993) Structure of the retinoid X receptor a DNA binding domain: A helix required for homodimeric DNA binding. Science 260:1117-1121
    • (1993) Science , vol.260 , pp. 1117-1121
    • Lee, M.-S.1    Kliewer, S.2    Provencal, J.3    Wright, P.4    Evans, R.M.5
  • 6
    • 0024457916 scopus 로고
    • A domain containing leucine-zipper-like motifs between the thyroid hormone and retinoic acid receptors
    • Forman BM, Yang G-R, Au M, Casanova J, Ghysdael J, Samuels HH (1989) A domain containing leucine-zipper-like motifs 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, G.-R.2    Au, M.3    Casanova, J.4    Ghysdael, J.5    Samuels, H.H.6
  • 7
    • 0027017570 scopus 로고
    • A novel, highly conserved structural motif is present in all members of the steroid receptor superfamily
    • Maksymowych AB, Hsu T-C, Litwack G (1993) A novel, highly conserved structural motif is present in all members of the steroid receptor superfamily. Receptor 2:225-239
    • (1993) Receptor , vol.2 , pp. 225-239
    • Maksymowych, A.B.1    Hsu, T.-C.2    Litwack, G.3
  • 8
    • 0025812291 scopus 로고
    • Direct repeats as selective response elements for the thyroid hormone, retinoic acid and vitamin D3 receptors
    • Umesono K, Murakami KK, Thompson CC, Evans RM (1991) Direct repeats as selective response elements for the thyroid hormone, retinoic acid and vitamin D3 receptors. Cell 65:1255-1266
    • (1991) Cell , vol.65 , pp. 1255-1266
    • Umesono, K.1    Murakami, K.K.2    Thompson, C.C.3    Evans, R.M.4
  • 9
    • 0025860708 scopus 로고
    • The orientation and spacing of core DNA-binding motifs dictate selective transcriptional responses to three nuclear receptors
    • Naar AM, Boutin J-M, Lipkin SM, Yu VC, Holloway JM, Glass CK, Rosenfeld MG (1991) The orientation and spacing of core DNA-binding motifs dictate selective transcriptional responses to three nuclear receptors. Cell 65:1267-1279
    • (1991) Cell , vol.65 , pp. 1267-1279
    • Naar, A.M.1    Boutin, J.-M.2    Lipkin, S.M.3    Yu, V.C.4    Holloway, J.M.5    Glass, C.K.6    Rosenfeld, M.G.7
  • 11
    • 0026758142 scopus 로고
    • A retinoic acid response element from the rat CRBPI promoter is activated by an RAR/RXR heterodimer
    • Husmann M, Hoffmann B, Stump DG, Chytil F, Pfahl M (1992) A retinoic acid response element from the rat CRBPI promoter is activated by an RAR/RXR heterodimer. Biochem Biophys Res Comm 187:1558-1564
    • (1992) Biochem Biophys Res Comm , vol.187 , pp. 1558-1564
    • Husmann, M.1    Hoffmann, B.2    Stump, D.G.3    Chytil, F.4    Pfahl, M.5
  • 12
    • 0023695580 scopus 로고
    • The thyroid hormone receptor binds with opposite transcriptional effects to a common sequence motif in thyroid hormone and estrogen response elements
    • Glass CK, Holloway JM, Devary OV, Rosenfeld MG (1988) The thyroid hormone receptor binds with opposite transcriptional effects to a common sequence motif in thyroid hormone and estrogen response elements. Cell 54:313-323
    • (1988) Cell , vol.54 , pp. 313-323
    • Glass, C.K.1    Holloway, J.M.2    Devary, O.V.3    Rosenfeld, M.G.4
  • 13
    • 0025950381 scopus 로고
    • Cross-coupling of signal transduction pathways: Zinc finger meets leucine zipper
    • Schiile R, Evans RM (1991) Cross-coupling of signal transduction pathways: Zinc finger meets leucine zipper. Trends Genet 7:377-381
    • (1991) Trends Genet , vol.7 , pp. 377-381
    • Schiile, R.1    Evans, R.M.2
  • 14
    • 0027521592 scopus 로고
    • Nuclear receptor/AP-1 interaction
    • Pfahl M (1993) Nuclear receptor/AP-1 interaction. Endocrinol Rev 14:651-658
    • (1993) Endocrinol Rev , vol.14 , pp. 651-658
    • Pfahl, M.1
  • 15
    • 0024524385 scopus 로고
    • The contribution of the N- and C-terminal regions of steroid receptors to activation of transcription is both receptor and cell-specific
    • Bocquel MT, Kumar V, Strieker C, Chambon P, Gronemeyer H (1989) The contribution of the N- and C-terminal regions of steroid receptors to activation of transcription is both receptor and cell-specific. Nucl Acids Res 17:2581-2595
    • (1989) Nucl Acids Res , vol.17 , pp. 2581-2595
    • Bocquel, M.T.1    Kumar, V.2    Strieker, C.3    Chambon, P.4    Gronemeyer, H.5
  • 16
    • 0025062215 scopus 로고
    • Role of the two activating domains of the oestrogen receptor in the cell-type and promoter context dependent agonistic activity of the anti-oestrogen 4-hydroxytamoxifen
    • Berry M, Metzger D, Chambon P (1990) Role of the two activating domains of the oestrogen receptor in the cell-type and promoter context dependent agonistic activity of the anti-oestrogen 4-hydroxytamoxifen. EMBO J 9: 2811-2818
    • (1990) EMBO J , vol.9 , pp. 2811-2818
    • Berry, M.1    Metzger, D.2    Chambon, P.3
  • 17
    • 0023794190 scopus 로고
    • Multiple and cooperative trans-activation domains of the human glucocorticoid receptor
    • Hollenberg SM, Evans RM (1988) Multiple and cooperative trans-activation domains of the human glucocorticoid receptor. Cell 55:899-906
    • (1988) Cell , vol.55 , pp. 899-906
    • Hollenberg, S.M.1    Evans, R.M.2
  • 18
    • 0026343481 scopus 로고
    • Transcription activation by estrogen and progesterone receptors
    • Gronemeyer H (1991) Transcription activation by estrogen and progesterone receptors. Annu Rev Genet 25:89-123
    • (1991) Annu Rev Genet , vol.25 , pp. 89-123
    • Gronemeyer, H.1
  • 19
    • 0024317270 scopus 로고
    • The human estrogen receptor has two independent nonacidic transcriptional activation functions
    • Tora L, White J, Brou C, Tasset D, Webster N, Scheer E, Chambon P (1989) The human estrogen receptor has two independent nonacidic transcriptional activation functions. Cell 59:477-487
    • (1989) Cell , vol.59 , pp. 477-487
    • Tora, L.1    White, J.2    Brou, C.3    Tasset, D.4    Webster, N.5    Scheer, E.6    Chambon, P.7
  • 20
    • 0024337858 scopus 로고
    • Determinants of target gene specificity for steroid/thyroid hormone receptors
    • Umesono K, Evans RM (1989) Determinants of target gene specificity for steroid/thyroid hormone receptors. Cell 57:1139-1146
    • (1989) Cell , vol.57 , pp. 1139-1146
    • Umesono, K.1    Evans, R.M.2
  • 21
    • 0023034983 scopus 로고
    • An estrogen-responsive element derived from the 5’ flanking region of the Xenopus vitellogenin A2 gene functions in transfected human cells
    • Klein-Hitpass L, Schorpp M, Wagner U, Ryffel GU (1986) An estrogen-responsive element derived from the 5’ flanking region of the Xenopus vitellogenin A2 gene functions in transfected human cells. Cell 46:1053-1061
    • (1986) Cell , vol.46 , pp. 1053-1061
    • Klein-Hitpass, L.1    Schorpp, M.2    Wagner, U.3    Ryffel, G.U.4
  • 22
    • 0023462125 scopus 로고
    • The estrogen-responsive element as an inducible enhancer: DNA sequence requirements and conversion to a glucocorticoid-responsive element
    • Martinez E, Givel F, Wahli W (1987) The estrogen-responsive element as an inducible enhancer: DNA sequence requirements and conversion to a glucocorticoid-responsive element. EMBO J 6:3719-3727
    • (1987) EMBO J , vol.6 , pp. 3719-3727
    • Martinez, E.1    Givel, F.2    Wahli, W.3
  • 23
    • 0025155251 scopus 로고
    • The human estrogen receptor has transcriptional activator and repressor functions in the absence of ligand
    • Tzukerman M, Zhang X-K, Hermann T, Wills KN, Graupner G, Pfahl M (1990) The human estrogen receptor has transcriptional activator and repressor functions in the absence of ligand. New Biol 2:613-620
    • (1990) New Biol , vol.2 , pp. 613-620
    • Tzukerman, M.1    Zhang, X.-K.2    Hermann, T.3    Wills, K.N.4    Graupner, G.5    Pfahl, M.6
  • 24
    • 0025756174 scopus 로고
    • Protein-protein interactions involved erbA superfamily receptors, through the TRAPdoor
    • Rosen ED, O’Donnell AL, Koenig RJ (1991) Protein-protein interactions involved erbA superfamily receptors, through the TRAPdoor. Mol Cell Endocrinol 78: C83-C88
    • (1991) Mol Cell Endocrinol , vol.78 , pp. C83-C88
    • Rosen, E.D.1    O’donnell, A.L.2    Koenig, R.J.3
  • 28
    • 0026592518 scopus 로고
    • Retinoid X receptor interacts with nuclear receptors in retinoic acid, thyroid hormone and vitamin D3 signaling
    • Kliewer SA, Umesono K, Mangelsdorf DJ, Evans RM (1992) Retinoid X receptor interacts with nuclear receptors in retinoic acid, thyroid hormone and vitamin D3 signaling. 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
  • 29
    • 0026551704 scopus 로고
    • RXRa, a promiscuous partner of retinoic acid and thyroid hormone receptors
    • Bugge TH, Pohl J, Lonnoy O, Stunnenberg HG (1992) RXRa, a promiscuous partner of retinoic acid and thyroid hormone receptors. EMBO J 11:1409-1418
    • (1992) EMBO J , vol.11 , pp. 1409-1418
    • Bugge, T.H.1    Pohl, J.2    Lonnoy, O.3    Stunnenberg, H.G.4
  • 30
    • 0026608464 scopus 로고
    • H-2RIIBP (RXRβ) hetero-dimerization provides a mechanism for combinatorial diversity in the regulation of retinoic acid and thyroid hormone responsive gene
    • Marks MS, Hallenbeck PL, Nagata T, Segars JH, Apella E, Nikodem VM, Ozato K (1992) H-2RIIBP (RXRβ) hetero-dimerization provides a mechanism for combinatorial diversity in the regulation of retinoic acid and thyroid hormone responsive gene. EMBO J 11:1419-1435
    • (1992) EMBO J , vol.11 , pp. 1419-1435
    • Marks, M.S.1    Hallenbeck, P.L.2    Nagata, T.3    Segars, J.H.4    Apella, E.5    Nikodem, V.M.6    Ozato, K.7
  • 31
    • 0023695580 scopus 로고
    • The thyroid hormone receptor binds with opposite transcriptional effects to a common sequence motif in thyroid hormone and estrogen response elements
    • Glass CK, Holloway JM, Devary OV, Rosenfeld MG (1988) The thyroid hormone receptor binds with opposite transcriptional effects to a common sequence motif in thyroid hormone and estrogen response elements. Cell 54:313-323
    • (1988) Cell , vol.54 , pp. 313-323
    • Glass, C.K.1    Holloway, J.M.2    Devary, O.V.3    Rosenfeld, M.G.4
  • 32
    • 0024385540 scopus 로고
    • Dual regulatory role for thyroid-hormone receptors allows control of retinoic-acid receptor activity
    • Graupner G, Willis KN, Tzukerman M, Zhang X-K, Pfahl M (1989) Dual regulatory role for thyroid-hormone receptors allows control of retinoic-acid receptor activity. Nature 340:653-656
    • (1989) Nature , vol.340 , pp. 653-656
    • Graupner, G.1    Willis, K.N.2    Tzukerman, M.3    Zhang, X.-K.4    Pfahl, M.5
  • 33
    • 0026645597 scopus 로고
    • Heterodimeric receptor complexes determine 3, 5, 3’-triiodothyronine and reinoid signaling specificities
    • Hermann T, Hoffmann B, Zhang X-K, Tran P, Pfahl M (1992) Heterodimeric receptor complexes determine 3, 5, 3’-triiodothyronine and reinoid signaling specificities. Mol Endocrinol 6:1153-1162
    • (1992) Mol Endocrinol , vol.6 , pp. 1153-1162
    • Hermann, T.1    Hoffmann, B.2    Zhang, X.-K.3    Tran, P.4    Pfahl, M.5
  • 34
    • 0026705751 scopus 로고
    • Convergence of 9-cis retinoic acid and peroxisome proliferator signaling pathways through heterodimer formation of their receptors
    • Kliewer SA, Umesono K, Noonan DJ, Heyman RA, Evans RM (1992) Convergence of 9-cis retinoic acid and peroxisome proliferator signaling pathways through heterodimer formation of their receptors. Nature 358: 771-774
    • (1992) Nature , vol.358 , pp. 771-774
    • Kliewer, S.A.1    Umesono, K.2    Noonan, D.J.3    Heyman, R.A.4    Evans, R.M.5
  • 35
    • 0027447461 scopus 로고
    • Fatty acids and retinoids control lipid metabolism through activation of peroxisome proliferator-activated receptor-retinoid X receptor heterodimers
    • Keller H, Dreyer C, Medin J, Mahfoudi A, Ozato K, Wahli W (1993) Fatty acids and retinoids control lipid metabolism through activation of peroxisome proliferator-activated receptor-retinoid X receptor heterodimers. Proc Natl Acad Sci USA 90:2160-2164
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 2160-2164
    • Keller, H.1    Dreyer, C.2    Medin, J.3    Mahfoudi, A.4    Ozato, K.5    Wahli, W.6
  • 37
    • 0026646635 scopus 로고
    • Drosophila ultraspiracle modulates ecdysone receptor function via heterodimer formation
    • Yao T-P, Segraves WA, Oro EA, McKeown M, Evans RM (1992) Drosophila ultraspiracle modulates ecdysone receptor function via heterodimer formation. Cell 71:63-72
    • (1992) Cell , vol.71 , pp. 63-72
    • Yao, T.-P.1    Segraves, W.A.2    Oro, E.A.3    McKeown, M.4    Evans, R.M.5
  • 39
    • 0026536522 scopus 로고
    • Retinoid X receptor is an auxiliary protein for thyroid hormone and retinoic acid receptors
    • Zhang Z-K, Hoffmann B, Tran P, Graupner G, Pfahl M (1992) Retinoid X receptor is an auxiliary protein for thyroid hormone and retinoic acid receptors. Nature 355:441-446
    • (1992) Nature , vol.355 , pp. 441-446
    • Zhang, Z.-K.1    Hoffmann, B.2    Tran, P.3    Graupner, G.4    Pfahl, M.5
  • 40
    • 0025270737 scopus 로고
    • Nuclear receptor that identifies a novel retinoic acid response pathway
    • Mangelsdorf DJ, Ong ES, Dyck JA, Evans RM (1990) Nuclear receptor that identifies a novel retinoic acid response pathway. Nature 345:224-229
    • (1990) Nature , vol.345 , pp. 224-229
    • Mangelsdorf, D.J.1    Ong, E.S.2    Dyck, J.A.3    Evans, R.M.4
  • 44
    • 0027488078 scopus 로고
    • Formation of RXR homodimers leads to repression of T3 response: Hormonal cross-talk by ligand induced squelching
    • Lehmann JM, Zhang X-K, Graupner G, Lee M-O, Hermann T, Hoffmann B, Pfahl M (1993) Formation of RXR homodimers leads to repression of T3 response: Hormonal cross-talk by ligand induced squelching. Mol Cell Biol 13:7698-7707
    • (1993) Mol Cell Biol , vol.13 , pp. 7698-7707
    • Lehmann, J.M.1    Zhang, X.-K.2    Graupner, G.3    Lee, M.-O.4    Hermann, T.5    Hoffmann, B.6    Pfahl, M.7
  • 45
    • 0027185416 scopus 로고
    • Retinoid X receptors stimulate and 9-cis retinoic acid inhibits 1, 25-dihydroxyvitamin D3-activated expression of the rat osteocalcin gene
    • MacDonald PN, Dowd DR, Nakajima S, Galligan MA, Reeder MC, Haussler CA, Ozato K, Haussler MR (1993) Retinoid X receptors stimulate and 9-cis retinoic acid inhibits 1, 25-dihydroxyvitamin D3-activated expression of the rat osteocalcin gene. Mol Cell Biol 13:5907-5917
    • (1993) Mol Cell Biol , vol.13 , pp. 5907-5917
    • Macdonald, P.N.1    Dowd, D.R.2    Nakajima, S.3    Galligan, M.A.4    Reeder, M.C.5    Haussler, C.A.6    Ozato, K.7    Haussler, M.R.8
  • 46
    • 0026756154 scopus 로고
    • COUP orphan receptors are negative regulators of retinoic acid response pathways
    • Tran P, Zhang X-K, Gilles S, Hermann T, Lehmann JM, Pfahl M (1992) COUP orphan receptors are negative regulators of retinoic acid response pathways. Mol Cell Biol 12:4666-4676
    • (1992) Mol Cell Biol , vol.12 , pp. 4666-4676
    • Tran, P.1    Zhang, X.-K.2    Gilles, S.3    Hermann, T.4    Lehmann, J.M.5    Pfahl, M.6
  • 48
    • 0026754182 scopus 로고
    • Repression by ARP-1 sensitizes apolipoprotcin AI gene responsiveness to RXRa and retinoic acid
    • Windom RL, Rhee M, Karathanasis K (1992) Repression by ARP-1 sensitizes apolipoprotcin AI gene responsiveness to RXRa and retinoic acid. Mol Cell Biol 12:3380-3389
    • (1992) Mol Cell Biol , vol.12 , pp. 3380-3389
    • Windom, R.L.1    Rhee, M.2    Karathanasis, K.3
  • 49
    • 0026738479 scopus 로고
    • Chicken ovalbumin upstream promoter transcription factor (COUP-TF) dimers bind to different GGTCA response elements, allowing COUP-TF to repress hormonal induction of the vitamin D3, thyroid hormone, and retinoic acid receptors
    • Cooney AJ, Tsai SY, O’Malley BW, Tsai MJ (1992) Chicken ovalbumin upstream promoter transcription factor (COUP-TF) dimers bind to different GGTCA response elements, allowing COUP-TF to repress hormonal induction of the vitamin D3, thyroid hormone, and retinoic acid receptors. Mol Cell Biol 12:4153-4163
    • (1992) Mol Cell Biol , vol.12 , pp. 4153-4163
    • Cooney, A.J.1    Tsai, S.Y.2    O’malley, B.W.3    Tsai, M.J.4
  • 51
    • 0025122035 scopus 로고
    • The Drosophila seven-up gene, a member of the steroid receptor gene superfamily, controls photoreceptor cell fates
    • Mlodzik M, Hiromi Y, Weber U, Goodman CS, Rubin GM (1990) The Drosophila seven-up gene, a member of the steroid receptor gene superfamily, controls photoreceptor cell fates. Cell 60:211-224
    • (1990) Cell , vol.60 , pp. 211-224
    • Mlodzik, M.1    Hiromi, Y.2    Weber, U.3    Goodman, C.S.4    Rubin, G.M.5
  • 53
    • 0026610642 scopus 로고
    • Triiodothyronine (T3) decreases binding to DNA by Te-receptor homodimers but not receptor-auxiliary protein heterodimers
    • Yen PM, Darling DS, Carter RL, Forgione M, Umeda PK, Chin WW (1992) Triiodothyronine (T3) decreases binding to DNA by Te-receptor homodimers but not receptor-auxiliary protein heterodimers. J Biol Chem 267:3565-3568
    • (1992) J Biol Chem , vol.267 , pp. 3565-3568
    • Yen, P.M.1    Darling, D.S.2    Carter, R.L.3    Forgione, M.4    Umeda, P.K.5    Chin, W.W.6
  • 55
    • 0026688440 scopus 로고
    • All-trans and 9-cis retinoic acid induction of CRABP II transcription is mediated by RAR-RXR heterodimers bound to DR1 and DR2 repeated motifs
    • Durand B, Saunders M, Leroy P, Leid M, Chambon P (1992) All-trans and 9-cis retinoic acid induction of CRABP II transcription is mediated by RAR-RXR heterodimers bound to DR1 and DR2 repeated motifs. Cell 71: 73-83
    • (1992) Cell , vol.71 , pp. 73-83
    • Durand, B.1    Saunders, M.2    Leroy, P.3    Leid, M.4    Chambon, P.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.