메뉴 건너뛰기




Volumn 13, Issue 2, 1999, Pages 286-296

Estrogen receptor domains E and F: Role in dimerization and interaction with coactivator RIP-140

Author keywords

[No Author keywords available]

Indexed keywords

ESTROGEN RECEPTOR;

EID: 0032961682     PISSN: 08888809     EISSN: None     Source Type: Journal    
DOI: 10.1210/mend.13.2.0244     Document Type: Article
Times cited : (66)

References (48)
  • 1
    • 0023808861 scopus 로고
    • The estrogen receptor binds tightly to its responsive element as a ligand-induced homodimer
    • 1. Kumar V, Chambon P 1988 The estrogen receptor binds tightly to its responsive element as a ligand-induced homodimer. Cell 55:145-156
    • (1988) Cell , vol.55 , pp. 145-156
    • Kumar, V.1    Chambon, P.2
  • 2
    • 0022773520 scopus 로고
    • Localization of the oestradiol-binding and putative DNA binding domains of the human oestrogen receptor
    • 2. Kumar V, Green S, Staub A, Chambon P 1986 Localization of the oestradiol-binding and putative DNA binding domains of the human oestrogen receptor. EMBO J 5:2231-2236
    • (1986) EMBO J , vol.5 , pp. 2231-2236
    • Kumar, V.1    Green, S.2    Staub, A.3    Chambon, P.4
  • 4
    • 0024317270 scopus 로고
    • The human estrogen receptor has two independent nonacidic transcriptional activation functions
    • 4. 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
  • 5
    • 84995870933 scopus 로고
    • Human estrogen receptor transactivational capacity is determined by both cellular and promoter context and mediated by two functionally distinct intramolecular regions
    • 5. Tzukerman MT, Esty A, Santiso-Mere D, Danielian P, Parker MG, Stein RB, Pike JW, McDonnell DP 1994 Human estrogen receptor transactivational capacity is determined by both cellular and promoter context and mediated by two functionally distinct intramolecular regions. Mol Endocrinol 8:21-30
    • (1994) Mol Endocrinol , vol.8 , pp. 21-30
    • Tzukerman, M.T.1    Esty, A.2    Santiso-Mere, D.3    Danielian, P.4    Parker, M.G.5    Stein, R.B.6    Pike, J.W.7    McDonnell, D.P.8
  • 6
    • 0030910962 scopus 로고    scopus 로고
    • Identification of a third autonomous activation domain within the human estrogen receptor
    • 6. Norris JD, Fan D, Kemer SA, McDonnell DP 1997 Identification of a third autonomous activation domain within the human estrogen receptor. Mol Endocrinol 11:747-754
    • (1997) Mol Endocrinol , vol.11 , pp. 747-754
    • Norris, J.D.1    Fan, D.2    Kemer, S.A.3    McDonnell, D.P.4
  • 7
    • 0028305554 scopus 로고
    • A highly conserved region in the hormone-binding domain of the human estrogen receptor functions as an efficient transactivation domain in yeast
    • 7. Pierrat B, Heery DM, Chambon P, Losson R 1994 A highly conserved region in the hormone-binding domain of the human estrogen receptor functions as an efficient transactivation domain in yeast. Gene 143:193-200
    • (1994) Gene , vol.143 , pp. 193-200
    • Pierrat, B.1    Heery, D.M.2    Chambon, P.3    Losson, R.4
  • 8
    • 0027365669 scopus 로고
    • The crystal structure of the estrogen receptor DNA-binding domain bound to DNA: How receptors discriminate between their response elements
    • 8. Schwabe JWR, Chapman L, Finch JT, Rhodes D 1993 The crystal structure of the estrogen receptor DNA-binding domain bound to DNA: how receptors discriminate between their response elements. Cell 75:567-578
    • (1993) Cell , vol.75 , pp. 567-578
    • Schwabe, J.W.R.1    Chapman, L.2    Finch, J.T.3    Rhodes, D.4
  • 9
    • 0030477196 scopus 로고    scopus 로고
    • Steroid receptor transcriptional synergy is potentiated by disruption of the DNA-binding domain dimer interface
    • 9. Liu W, Wang J, Yu G, Pearce D 1996 Steroid receptor transcriptional synergy is potentiated by disruption of the DNA-binding domain dimer interface. Mol Endocrinol 10:1399-1406
    • (1996) Mol Endocrinol , vol.10 , pp. 1399-1406
    • Liu, W.1    Wang, J.2    Yu, G.3    Pearce, D.4
  • 10
    • 0029058152 scopus 로고
    • The carboxy-terminal F domain of the human estrogen receptor: Role in the transcriptional activity of the receptor and the effectiveness of antiestrogens as estrogen antagonists
    • 10. Montano MM, Muller V, Trobaugh A, Katzenellenbogen BS 1995 The carboxy-terminal F domain of the human estrogen receptor: role in the transcriptional activity of the receptor and the effectiveness of antiestrogens as estrogen antagonists. Mol Endocrinol 9:814-825
    • (1995) Mol Endocrinol , vol.9 , pp. 814-825
    • Montano, M.M.1    Muller, V.2    Trobaugh, A.3    Katzenellenbogen, B.S.4
  • 14
    • 0029850086 scopus 로고    scopus 로고
    • RIP-140 interacts with multiple nuclear receptors by means of two distinct sites
    • 14. L'Horset F, Dauvois S, Heery DM, Cavailles V, Parker MG 1996 RIP-140 interacts with multiple nuclear receptors by means of two distinct sites. Mol Cell Biol 16:6029-6036
    • (1996) Mol Cell Biol , vol.16 , pp. 6029-6036
    • L'Horset, F.1    Dauvois, S.2    Heery, D.M.3    Cavailles, V.4    Parker, M.G.5
  • 15
    • 0025329841 scopus 로고
    • Characterization and colocalization of steroid binding and dimerization activities in the mouse estrogen receptor
    • 15. Fawell SE, Lees JA, White R, Parker MG 1990a Characterization and colocalization of steroid binding and dimerization activities in the mouse estrogen receptor. Cell 60:953-962
    • (1990) Cell , vol.60 , pp. 953-962
    • Fawell, S.E.1    Lees, J.A.2    White, R.3    Parker, M.G.4
  • 16
    • 0027462304 scopus 로고
    • Human estrogen bound to an estrogen response element bends DNA
    • 16. Nardulli AM, Greene GL, Shapiro DJ 1993 Human estrogen bound to an estrogen response element bends DNA. Mol Endocrinol 7:331-340
    • (1993) Mol Endocrinol , vol.7 , pp. 331-340
    • Nardulli, A.M.1    Greene, G.L.2    Shapiro, D.J.3
  • 17
    • 0025267297 scopus 로고
    • Uterine estrogen receptor interaction with estrogen-responsive DNA sequences in vitro: Effects of ligand binding on receptor-DNA complexes
    • 17. Curtis SW, Korach KS 1990 Uterine estrogen receptor interaction with estrogen-responsive DNA sequences in vitro: effects of ligand binding on receptor-DNA complexes. Mol Endocrinol 4:276-286
    • (1990) Mol Endocrinol , vol.4 , pp. 276-286
    • Curtis, S.W.1    Korach, K.S.2
  • 18
    • 0025159830 scopus 로고
    • Estrogen receptor binding to a DNA response element in vitro is not dependent upon estradiol
    • 18. Murdoch FE, Meier DA, Furlow JD, Grunwald K, Gorski J 1990 Estrogen receptor binding to a DNA response element in vitro is not dependent upon estradiol. Biochemistry 29:8377-8385
    • (1990) Biochemistry , vol.29 , pp. 8377-8385
    • Murdoch, F.E.1    Meier, D.A.2    Furlow, J.D.3    Grunwald, K.4    Gorski, J.5
  • 19
    • 0025302841 scopus 로고
    • Human estrogen receptor forms multiple protein-DNA complexes
    • 19. Brown M, Sharp P 1990 Human estrogen receptor forms multiple protein-DNA complexes. J Biol Chem 265:11238
    • (1990) J Biol Chem , vol.265 , pp. 11238
    • Brown, M.1    Sharp, P.2
  • 20
    • 0027521287 scopus 로고
    • Transcriptional activation by the estrogen receptor requires a conformational change in the ligand binding domain
    • 20. Beekman JM, Allan GF, Tsai SY, Tsai M-J, O'Malley BW 1993 Transcriptional activation by the estrogen receptor requires a conformational change in the ligand binding domain. Mol Endocrinol 7:1266-1274
    • (1993) Mol Endocrinol , vol.7 , pp. 1266-1274
    • Beekman, J.M.1    Allan, G.F.2    Tsai, S.Y.3    Tsai, M.-J.4    O'Malley, B.W.5
  • 21
    • 0028786569 scopus 로고
    • Yeast two-hybrid system demonstrates that estrogen receptor dimerization is ligand-dependent in vivo
    • 21. Wang H, Peters GA, Zeng X, Tang M, Ip W, Khan S 1995 Yeast two-hybrid system demonstrates that estrogen receptor dimerization is ligand-dependent in vivo. J Biol Chem 270:23322-23329
    • (1995) J Biol Chem , vol.270 , pp. 23322-23329
    • Wang, H.1    Peters, G.A.2    Zeng, X.3    Tang, M.4    Ip, W.5    Khan, S.6
  • 22
    • 0023895442 scopus 로고
    • The human oestrogen receptor functions in yeast
    • 22. Metzger D, White JH, Chambon P 1988 The human oestrogen receptor functions in yeast. Nature 334:31-36
    • (1988) Nature , vol.334 , pp. 31-36
    • Metzger, D.1    White, J.H.2    Chambon, P.3
  • 23
    • 0025695563 scopus 로고
    • Expression and characterization of an active human estrogen receptor as a ubiquitin fusion protein from Escherichia coli
    • 23. Wittcliff JL, Wenz LL, Dong J, Nawaz Z, Butt TR 1990 Expression and characterization of an active human estrogen receptor as a ubiquitin fusion protein from Escherichia coli. J Biol Chem 265:22016-22022
    • (1990) J Biol Chem , vol.265 , pp. 22016-22022
    • Wittcliff, J.L.1    Wenz, L.L.2    Dong, J.3    Nawaz, Z.4    Butt, T.R.5
  • 24
    • 0026689357 scopus 로고
    • Ligand-dependent and -independent function of the transactivation regions of the human estrogen receptor in yeast
    • 24. Pham TA, Hwung YP, Santiso-Mere D, McDonnell DP, O'Malley BW 1992 Ligand-dependent and -independent function of the transactivation regions of the human estrogen receptor in yeast. Mol Endocrinol 6:1043-1050
    • (1992) Mol Endocrinol , vol.6 , pp. 1043-1050
    • Pham, T.A.1    Hwung, Y.P.2    Santiso-Mere, D.3    McDonnell, D.P.4    O'Malley, B.W.5
  • 25
    • 0026636455 scopus 로고
    • Human estrogen receptor regulation in a yeast model system and studies on receptor agonists and antagonists
    • 25. Lyttle CR, Damian-Matsumura P, Juul H, Butt TR 1992 Human estrogen receptor regulation in a yeast model system and studies on receptor agonists and antagonists. J Steroid Biochem Mol Biol 42:677-684
    • (1992) J Steroid Biochem Mol Biol , vol.42 , pp. 677-684
    • Lyttle, C.R.1    Damian-Matsumura, P.2    Juul, H.3    Butt, T.R.4
  • 26
    • 0026639625 scopus 로고
    • Protein interaction cloning in yeast: Identification of mammalian proteins that react with the leucine zipper of Jun
    • 26. Chevray PM, Nathans D 1992 Protein interaction cloning in yeast: identification of mammalian proteins that react with the leucine zipper of Jun. Proc Natl Acad Sci 89:5789-5793
    • (1992) Proc Natl Acad Sci , vol.89 , pp. 5789-5793
    • Chevray, P.M.1    Nathans, D.2
  • 27
    • 0031029849 scopus 로고    scopus 로고
    • RIP 140 enhances nuclear receptor-dependent transcription in vivo in yeast
    • 27. Joyeux A, Cavailles P, Balaguer P, Nicolas JC 1997 RIP 140 enhances nuclear receptor-dependent transcription in vivo in yeast. Mol Endocrinol 11:193-202
    • (1997) Mol Endocrinol , vol.11 , pp. 193-202
    • Joyeux, A.1    Cavailles, P.2    Balaguer, P.3    Nicolas, J.C.4
  • 28
    • 0028217807 scopus 로고
    • The human estrogen receptor hormone binding domain dimerizes independently of ligand activation
    • 28. Salomonsson M, Haggblad J, O'Malley B, Sitbon G 1994 The human estrogen receptor hormone binding domain dimerizes independently of ligand activation. J Steroid Biochem Mol Biol 48:447-452
    • (1994) J Steroid Biochem Mol Biol , vol.48 , pp. 447-452
    • Salomonsson, M.1    Haggblad, J.2    O'Malley, B.3    Sitbon, G.4
  • 29
    • 0029092610 scopus 로고
    • Correlation of two-hybrid affinity data with in vitro measurements
    • 29. Estojak J, Brent R, Golemis EA 1995 Correlation of two-hybrid affinity data with in vitro measurements. Mol Cell Biol 15:5820-5829
    • (1995) Mol Cell Biol , vol.15 , pp. 5820-5829
    • Estojak, J.1    Brent, R.2    Golemis, E.A.3
  • 31
    • 0030986236 scopus 로고    scopus 로고
    • A signature motif in transcriptional co-activators mediates binding to nuclear receptors
    • 31. Heery DM, Kalkhoven E, Hoare S, Parker MG 1997 A signature motif in transcriptional co-activators mediates binding to nuclear receptors. Nature 387:733-736
    • (1997) Nature , vol.387 , pp. 733-736
    • Heery, D.M.1    Kalkhoven, E.2    Hoare, S.3    Parker, M.G.4
  • 32
    • 0029970860 scopus 로고    scopus 로고
    • The extreme C terminus of the progesterone receptor contains a transcriptional repressor domain that functions through a putative corepressor
    • 32. Xu J, Nawaz Z, Tsai SY, Tsai MJ, O'Malley BW 1996 The extreme C terminus of the progesterone receptor contains a transcriptional repressor domain that functions through a putative corepressor. Proc Natl Acad Sci USA 29:12195-12199
    • (1996) Proc Natl Acad Sci USA , vol.29 , pp. 12195-12199
    • Xu, J.1    Nawaz, Z.2    Tsai, S.Y.3    Tsai, M.J.4    O'Malley, B.W.5
  • 33
    • 0029120606 scopus 로고
    • An antiestrogen: A phosphotyrosyl peptide that blocks dimerization of the human estrogen receptor
    • 33. Arnold SF, Notides AC 1995 An antiestrogen: a phosphotyrosyl peptide that blocks dimerization of the human estrogen receptor. Proc Natl Acad Sci USA 92:7475-7479
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 7475-7479
    • Arnold, S.F.1    Notides, A.C.2
  • 34
    • 0027771134 scopus 로고
    • An assessment of the rale of domain F and pest sequences in estrogen receptor half-life and bioactivity
    • 34. Pakdel F, LeGoff P, Katzenellenbogen BS 1993 An assessment of the rale of domain F and pest sequences in estrogen receptor half-life and bioactivity. J Steroid Biochem Mol Biol 46:663-672
    • (1993) J Steroid Biochem Mol Biol , vol.46 , pp. 663-672
    • Pakdel, F.1    LeGoff, P.2    Katzenellenbogen, B.S.3
  • 35
    • 0026653659 scopus 로고
    • The mechanism of RU486 antagonism is dependent on the conformation of the carboxy-terminal tail of the human progesterone receptor
    • 35. Vegeto E, Allan GF, Schrader WT, Tsai MJ, McDonnell DP, O'Malley BW 1992 The mechanism of RU486 antagonism is dependent on the conformation of the carboxy-terminal tail of the human progesterone receptor. Cell 69:703-713
    • (1992) Cell , vol.69 , pp. 703-713
    • Vegeto, E.1    Allan, G.F.2    Schrader, W.T.3    Tsai, M.J.4    McDonnell, D.P.5    O'Malley, B.W.6
  • 37
    • 0029074491 scopus 로고
    • Estrogen regulates the expression of several different estrogen receptor mrna isoforms in rat pituitary
    • 37. Friend KE, Ang LW, Shupnik MA 1995 Estrogen regulates the expression of several different estrogen receptor mRNA isoforms in rat pituitary. Proc Natl Acad Sci USA 92:4367-4371
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 4367-4371
    • Friend, K.E.1    Ang, L.W.2    Shupnik, M.A.3
  • 38
    • 0029049398 scopus 로고
    • Human estrogen receptor messenger RNA variants in both normal and tumor breast tissues
    • 38. Gotteland M, Desauty G, Delarue JC, Liu L, May E 1995 Human estrogen receptor messenger RNA variants in both normal and tumor breast tissues. Mol Cell Endocrinol 112:1-13
    • (1995) Mol Cell Endocrinol , vol.112 , pp. 1-13
    • Gotteland, M.1    Desauty, G.2    Delarue, J.C.3    Liu, L.4    May, E.5
  • 39
    • 0029883734 scopus 로고    scopus 로고
    • Expression of estrogen receptor variants in normal and neoplastic human uterus
    • 39. Hu C, Hyderm SM, Needleman DS, Baker VV 1996 Expression of estrogen receptor variants in normal and neoplastic human uterus. Mol Cell Endocrinol 118:173-179
    • (1996) Mol Cell Endocrinol , vol.118 , pp. 173-179
    • Hu, C.1    Hyderm, S.M.2    Needleman, D.S.3    Baker, V.V.4
  • 40
    • 0025699486 scopus 로고
    • Estrogen receptor variants in human breast cancer
    • 40. Murphy LC 1990 Estrogen receptor variants in human breast cancer. Mol Cell Endocrinol 74:C83-C86
    • (1990) Mol Cell Endocrinol , vol.74
    • Murphy, L.C.1
  • 41
    • 0026622048 scopus 로고
    • Role of estrogen receptor variants in the development of hormone resistance in breast cancer
    • 41. Sluyser M 1992 Role of estrogen receptor variants in the development of hormone resistance in breast cancer. Clin Biochem 25:407-414
    • (1992) Clin Biochem , vol.25 , pp. 407-414
    • Sluyser, M.1
  • 43
    • 0027865308 scopus 로고
    • Expression of estrogen receptor variants
    • 43. Fuqua SAW, Allred DC, Auchus RJ 1993 Expression of estrogen receptor variants. J Cell Biochem 17G [Suppl]: 194-197
    • (1993) J Cell Biochem , vol.17 G , Issue.SUPPL. , pp. 194-197
    • Fuqua, S.A.W.1    Allred, D.C.2    Auchus, R.J.3
  • 45
    • 0030593681 scopus 로고    scopus 로고
    • ERβ: Identification and characterization of a novel human estrogen receptor
    • 45. Mosselman S, Polman J, Dijkema R 1996 ERβ: identification and characterization of a novel human estrogen receptor. FEBS Lett 392:49-53
    • (1996) FEBS Lett , vol.392 , pp. 49-53
    • Mosselman, S.1    Polman, J.2    Dijkema, R.3
  • 47
    • 0029945839 scopus 로고    scopus 로고
    • Steroid hormones, receptors, and antagonists
    • 47. Jensen EV 1996 Steroid hormones, receptors, and antagonists. Ann NY Acad Sci 784:1-17
    • (1996) Ann Ny Acad Sci , vol.784 , pp. 1-17
    • Jensen, E.V.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.