What are comparative studies telling us about the mechanism of ERβ action in the ERE-dependent E2 signaling pathway?

Journal of Steroid Biochemistry and Molecular Biology

Volumn 109, Issue 3-5, 2008, Pages 266-272

  Li, Xiaodong ^a   Huang, Jing ^a   Fluharty, Brian R ^a   Huang, Yanfang ^a   Nott, Stephanie L ^a   Muyan, Mesut ^a  

^a UNIVERSITY OF ROCHESTER MEDICAL CENTER   (United States)

Author keywords

ER ERE interaction; ERE; Estrogen; Estrogen receptor; Transcription

Indexed keywords

ESTROGEN; ESTROGEN RECEPTOR BETA; PALINDROMIC DNA; PROTEASOME; UBIQUITIN;

AMINO TERMINAL SEQUENCE; ARTICLE; DNA SEQUENCE; DNA TRANSCRIPTION; ESTROGEN ACTIVITY; ESTROGEN BINDING; HUMAN; IN VITRO STUDY; PATHOPHYSIOLOGY; PROTEIN DNA INTERACTION;

ANIMALS; CELL NUCLEUS; ESTROGEN RECEPTOR ALPHA; ESTROGEN RECEPTOR BETA; ESTROGENS; HUMANS; RESPONSE ELEMENTS; SIGNAL TRANSDUCTION;

EID: 43849112522     PISSN: 09600760     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jsbmb.2008.03.001     Document Type: Article

References (79)

1. Hall J.M., Couse J.F., and Korach K.S. The multifaceted mechanisms of estradiol and estrogen receptor signaling. J. Biol. Chem. 276 (2001) 36869-36872
2. Nilsson S., and Gustafsson J.A. Estrogen receptor action. Crit. Rev. Eukaryot. Gene Expr. 12 (2002) 237-257
3. Klinge C.M. Estrogen receptor interaction with estrogen response elements. Nucleic Acids Res. 29 (2001) 2905-2919
4. Yi P., Driscoll M.D., Huang J., Bhagat S., Hilf R., Bambara R.A., and Muyan M. The effects of estrogen-responsive element- and ligand-induced structural changes on the recruitment of cofactors and transcriptional responses by ERα and ERβ. Mol. Endocrinol. 16 (2002) 674-693
5. Loven M.A., Wood J.R., and Nardulli A.M. Interaction of estrogen receptors α and β with estrogen response elements. Mol. Cell Endocrinol. 181 (2001) 151-163
6. Kuiper G.G., Carlsson B., Grandien K., Enmark E., Haggblad J., Nilsson S., and Gustafsson J.A. Comparison of the ligand binding specificity and transcript tissue distribution of estrogen receptors α and β. Endocrinology 138 (1997) 863-870
7. Cowley S.M., and Parker M.G. A comparison of transcriptional activation by ERα and ERβ. J. Steroid Biochem. Mol. Biol. 69 (1999) 165-175
8. McInerney E.M., Weis K.E., Sun J., Mosselman S., and Katzenellenbogen B.S. Transcription activation by the human estrogen receptor subtype β (ERβ) studied with ERβ and ERα receptor chimeras. Endocrinology 139 (1998) 4513-4522
9. Hall J.M., and McDonnell D.P. The estrogen receptor β-isoform (ERβ) of the human estrogen receptor modulates ERα transcriptional activity and is a key regulator of the cellular response to estrogens and antiestrogens. Endocrinology 140 (1999) 5566-5578
10. Yi P., Bhagat S., Hilf R., Bambara R.A., and Muyan M. Differences in the abilities of estrogen receptors to integrate activation functions are critical for subtype-specific transcriptional responses. Mol. Endocrinol. 16 (2002) 1810-1827
11. Bai Y., and Giguere V. Isoform-selective interactions between estrogen receptors and steroid receptor coactivators promoted by estradiol and ErbB-2 signaling in living cells. Mol. Endocrinol. 17 (2003) 589-599
12. Zheng F.F., Wu R.C., Smith C.L., and O'Malley B.W. Rapid estrogen-induced phosphorylation of the SRC-3 coactivator occurs in an extranuclear complex containing estrogen receptor. Mol. Cell Biol. 25 (2005) 8273-8284
13. Stenoien D.L., Patel K., Mancini M.G., Dutertre M., Smith C.L., O'Malley B.W., and Mancini M.A. FRAP reveals that mobility of oestrogen receptor-α is ligand- and proteasome-dependent. Nat. Cell Biol. 3 (2001) 15-23
14. Nunez A.M., Berry M., Imler J.L., and Chambon P. The 5′ flanking region of the pS2 gene contains a complex enhancer region responsive to oestrogens, epidermal growth factor, a tumour promoter (TPA), the c-Ha-ras oncoprotein and the c-jun protein. EMBO J. 8 (1989) 823-829
15. Berry M., Nunez A.M., and Chambon P. Estrogen-responsive element of the human pS2 gene is an imperfectly palindromic sequence. Proc. Natl. Acad. Sci. U.S.A. 86 (1989) 1218-1222
16. Shang Y., Hu X., DiRenzo J., Lazar M.A., and Brown M. Cofactor dynamics and sufficiency in estrogen receptor-regulated transcription. Cell 103 (2000) 843-852
17. Reid G., Hubner M.R., Metivier R., Brand H., Denger S., Manu D., Beaudouin J., Ellenberg J., and Gannon F. Cyclic, proteasome-mediated turnover of unliganded and liganded ERα on responsive promoters is an integral feature of estrogen signaling. Mol. Cell 11 (2003) 695-707
18. Metivier R., Penot G., Carmouche R.P., Hubner M.R., Reid G., Denger S., Manu D., Brand H., Kos M., Benes V., and Gannon F. Transcriptional complexes engaged by apo-estrogen receptor-α isoforms have divergent outcomes. EMBO J. 23 (2004) 3653-3666
19. Webb P., Nguyen P., Shinsako J., Anderson C., Feng W., Nguyen M.P., Chen D., Huang S.M., Subramanian S., McKinerney E., Katzenellenbogen B.S., Stallcup M.R., and Kushner P.J. Estrogen receptor activation function 1 works by binding p160 coactivator proteins. Mol. Endocrinol. 12 (1998) 1605-1618
20. Lonard D.M., Nawaz Z., Smith C.L., and O'Malley B.W. The 26S proteasome is required for estrogen receptor-α and coactivator turnover and for efficient estrogen receptor-α transactivation. Mol. Cell 5 (2000) 939-948
21. Wurtz J.M., Bourguet W., Renaud J.P., Vivat V., Chambon P., Moras D., and Gronemeyer H. A canonical structure for the ligand-binding domain of nuclear receptors. Nat. Str. Biol. 3 (1996) 87-94
22. Pike A.C. Lessons learnt from structural studies of the oestrogen receptor. Best Pract. Res. Clin. Endocrinol. Metab. 20 (2006) 1-14
23. Tamrazi A., and Katzenellenbogen J.A. Site-specific fluorescent labeling of estrogen receptors and structure-activity relationships of ligands in terms of receptor dimer stability. Methods Enzymol. 364 (2003) 37-53
24. Brzozowski A.M., Pike A.C., Dauter Z., Hubbard R.E., Bonn T., Engstrom O., Ohman L., Greene G.L., Gustafsson J.A., and Carlquist M. Molecular basis of agonism and antagonism in the oestrogen receptor. Nature 389 (1997) 753-758
25. Reese J.C., and Katzenellenbogen B.S. Examination of the DNA-binding ability of estrogen receptor in whole cells: implications for hormone-independent transactivation and the actions of antiestrogens. Mol. Cell Biol. 12 (1992) 4531-4538
26. Nye A.C., Rajendran R.R., Stenoien D.L., Mancini M.A., Katzenellenbogen B.S., and Belmont A.S. Alteration of large-scale chromatin structure by estrogen receptor. Mol. Cell Biol. 22 (2002) 3437-3449
27. Chen H.W., Lin R.J., Xie W., Wilpitz D., and Evans R.M. Regulation of hormone-induced histone hyperacetylation and gene activation via acetylation of an acetylase. Cell 98 (1999) 675-686
28. Pratt W.B., Gehring U., and Toft D.O. Molecular chaperoning of steroid hormone receptors. Exs 77 (1996) 79-95
29. Oesterreich S. Scaffold attachment factors SAFB1 and SAFB2: Innocent bystanders or critical players in breast tumorigenesis?. J. Cell Biochem. 90 (2003) 653-661
30. Romine L.E., Wood J.R., Lamia L.A., Prendergast P., Edwards D.P., and Nardulli A.M. The high mobility group protein 1 enhances binding of the estrogen receptor DNA binding domain to the estrogen response element. Mol. Endocrinol. 12 (1998) 664-674
31. Loven M.A., Muster N., Yates J.R., and Nardulli A.M. A novel estrogen receptor α-associated protein, template-activating factor Iβ, inhibits acetylation and transactivation. Mol. Endocrinol. 17 (2003) 67-78
32. Loven M.A., Davis R.E., Curtis C.D., Muster N., Yates J.R., and Nardulli A.M. A novel estrogen receptor α-associated protein alters receptor-deoxyribonucleic acid interactions and represses receptor-mediated transcription. Mol. Endocrinol. 18 (2004) 2649-2659
33. Metivier R., Penot G., Hubner M.R., Reid G., Brand H., Kos M., and Gannon F. Estrogen receptor-α directs ordered, cyclical, and combinatorial recruitment of cofactors on a natural target promoter. Cell 115 (2003) 751-763
34. Endoh H., Maruyama K., Masuhiro Y., Kobayashi Y., Goto M., Tai H., Yanagisawa J., Metzger D., Hashimoto S., and Kato S. Purification and identification of p68 RNA helicase acting as a transcriptional coactivator specific for the activation function 1 of human estrogen receptor α. Mol. Cell Biol. 19 (1999) 5363-5372
35. Warnmark A., Wikstrom A., Wright A.P., Gustafsson J.A., and Hard T. The N-terminal regions of estrogen receptor α and β are unstructured in vitro and show different TBP binding properties. J. Biol. Chem. 276 (2001) 45939-45944
36. Zhu P., Baek S.H., Bourk E.M., Ohgi K.A., Garcia-Bassets I., Sanjo H., Akira S., Kotol P.F., Glass C.K., Rosenfeld M.G., and Rose D.W. Macrophage/cancer cell interactions mediate hormone resistance by a nuclear receptor derepression pathway. Cell 124 (2006) 615-629
37. Wijayaratne A.L., and McDonnell D.P. The human estrogen receptor-α is a ubiquitinated protein whose stability is affected differentially by agonists, antagonists, and selective estrogen receptor modulators. J. Biol. Chem. 276 (2001) 35684-35692
38. Valley C.C., Metivier R., Solodin N.M., Fowler A.M., Mashek M.T., Hill L., and Alarid E.T. Differential regulation of estrogen-inducible proteolysis and transcription by the estrogen receptor alpha N terminus. Mol. Cell Biol. 25 (2005) 5417-5428
39. Tateishi Y., Kawabe Y., Chiba T., Murata S., Ichikawa K., Murayama A., Tanaka K., Baba T., Kato S., and Yanagisawa J. Ligand-dependent switching of ubiquitin-proteasome pathways for estrogen receptor. EMBO J. 23 (2004) 4813-4823
40. Sentis S., Le Romancer M., Bianchin C., Rostan M.C., and Corbo L. Sumoylation of the estrogen receptor α hinge region regulates its transcriptional activity. Mol. Endocrinol. 19 (2005) 2671-2684
41. Wang C., Fu M., Angeletti R.H., Siconolfi-Baez L., Reutens A.T., Albanese C., Lisanti M.P., Katzenellenbogen B.S., Kato S., Hopp T., Fuqua S.A., Lopez G.N., Kushner P.J., and Pestell R.G. Direct acetylation of the estrogen receptor α hinge region by p300 regulates transactivation and hormone sensitivity. J. Biol. Chem. 276 (2001) 18375-18383
42. Schwabe J.W., Neuhaus D., and Rhodes D. Solution structure of the DNA-binding domain of the oestrogen receptor. Nature 348 (1990) 458-461
43. Schwabe J.W., Chapman L., Finch J.T., and Rhodes D. The crystal structure of the estrogen receptor DNA-binding domain bound to DNA: how receptors discriminate between their response elements. Cell 75 (1993) 567-578
44. Li X., Huang J., Yi P., Bambara R.A., Hilf R., and Muyan M. Single-chain estrogen receptors (ERs) reveal that the ERα/β heterodimer emulates functions of the ERα dimer in genomic estrogen signaling pathways. Mol. Cell Biol. 24 (2004) 7681-7694
45. Pike A.C., Brzozowski A.M., Hubbard R.E., Bonn T., Thorsell A.G., Engstrom O., Ljunggren J., Gustafsson J.A., and Carlquist M. Structure of the ligand-binding domain of oestrogen receptor β in the presence of a partial agonist and a full antagonist. EMBO J. 18 (1999) 4608-4618
46. Huang J., Li X., Maguire C.A., Hilf R., Bambara R.A., and Muyan M. Binding of estrogen receptor β to estrogen response element in situ is independent of estradiol and impaired by its amino terminus. Mol. Endocrinol. 19 (2005) 2696-2712
47. Huang J., Li X., Yi P., Hilf R., Bambara R.A., and Muyan M. Targeting estrogen responsive elements (EREs): design of potent transactivators for ERE-containing genes. Mol. Cell Endocrinol. 218 (2004) 65-78
48. Moore P.A., Ruben S.M., and Rosen C.A. Conservation of transcriptional activation functions of the NF-κB p50 and p65 subunits in mammalian cells and Saccharomyces cerevisiae. Mol. Cell Biol. 13 (1993) 1666-1674
49. Triezenberg S.J., Kingsbury R.C., and McKnight S.L. Functional dissection of VP16, the trans-activator of herpes simplex virus immediate early gene expression. Genes Dev. 2 (1988) 718-729
50. Klein-Hitpass L., Kaling M., and Ryffel G.U. Synergism of closely adjacent estrogen-responsive elements increases their regulatory potential. J. Mol. Biol. 201 (1988) 537-544
51. Tyulmenkov V.V., Jernigan S.C., and Klinge C.M. Comparison of transcriptional synergy of estrogen receptors α and β from multiple tandem estrogen response elements. Mol. Cell Endocrinol. 165 (2000) 151-161
52. Beekman J.M., Allan G.F., Tsai S.Y., Tsai M.J., and O'Malley B.W. Transcriptional activation by the estrogen receptor requires a conformational change in the ligand binding domain. Mol. Endocrinol. 7 (1993) 1266-1274
53. Kraus W.L., McInerney E.M., and Katzenellenbogen B.S. Ligand-dependent, transcriptionally productive association of the amino- and carboxyl-terminal regions of a steroid hormone nuclear receptor. Proc. Natl. Acad. Sci. U.S.A. 92 (1995) 12314-12318
54. Tora L., White J., Brou C., Tasset D., Webster N., Scheer E., and Chambon P. The human estrogen receptor has two independent nonacidic transcriptional activation functions. Cell 59 (1989) 477-487
55. Tzukerman M.T., Esty A., Santiso-Mere D., Danielian P., Parker M.G., Stein R.B., Pike J.W., and McDonnell D.P. Human estrogen receptor transactivational capacity is determined by both cellular and promoter context and mediated by two functionally distinct intramolecular regions. Mol. Endocrinol. 8 (1994) 21-30
56. McInerney E.M., Tsai M.J., O'Malley B.W., and Katzenellenbogen B.S. Analysis of estrogen receptor transcriptional enhancement by a nuclear hormone receptor coactivator. Proc. Natl. Acad. Sci. U.S.A. 93 (1996) 10069-10073
57. Ali S., Metzger D., Bornert J.M., and Chambon P. Modulation of transcriptional activation by ligand-dependent phosphorylation of the human oestrogen receptor A/B region. EMBO J. 12 (1993) 1153-1160
58. Kato S., Endoh H., Masuhiro Y., Kitamoto T., Uchiyama S., Sasaki H., Masushige S., Gotoh Y., Nishida E., Kawashima H., Metzger D., and Chambon P. Activation of the estrogen receptor through phosphorylation by mitogen-activated protein kinase. Science 270 (1995) 1491-1494
59. Benecke A., Chambon P., and Gronemeyer H. Synergy between estrogen receptor α activation functions AF1 and AF2 mediated by transcription intermediary factor TIF2. EMBO Rep. 1 (2000) 151-157
60. Chen J.D., and Evans R.M. A transcriptional co-repressor that interacts with nuclear hormone receptors. Nature 377 (1995) 454-457
61. Zamir I., Harding H.P., Atkins G.B., Horlein A., Glass C.K., Rosenfeld M.G., and Lazar M.A. A nuclear hormone receptor corepressor mediates transcriptional silencing by receptors with distinct repression domains. Mol. Cell Biol. 16 (1996) 5458-5465
62. Jepsen K., and Rosenfeld M.G. Biological roles and mechanistic actions of co-repressor complexes. J. Cell Sci. 115 (2002) 689-698
63. Perissi V., Aggarwal A., Glass C.K., Rose D.W., and Rosenfeld M.G. A corepressor/coactivator exchange complex required for transcriptional activation by nuclear receptors and other regulated transcription factors. Cell 116 (2004) 511-526
64. Perissi V., and Rosenfeld M.G. Controlling nuclear receptors: the circular logic of cofactor cycles. Nat. Rev. Mol. Cell Biol. 6 (2005) 542-554
65. Rosenfeld M.G., Lunyak V.V., and Glass C.K. Sensors and signals: a coactivator/corepressor/epigenetic code for integrating signal-dependent programs of transcriptional response. Genes Dev. 20 (2006) 1405-1428
66. Hu X., and Lazar M.A. The CoRNR motif controls the recruitment of corepressors by nuclear hormone receptors. Nature 402 (1999) 93-96
67. Perissi V., Staszewski L.M., McInerney E.M., Kurokawa R., Krones A., Rose D.W., Lambert M.H., Milburn M.V., Glass C.K., and Rosenfeld M.G. Molecular determinants of nuclear receptor-corepressor interaction. Genes Dev. 13 (1999) 3198-3208
68. Smith C.L., Nawaz Z., and O'Malley B.W. Coactivator and corepressor regulation of the agonist/antagonist activity of the mixed antiestrogen, 4-hydroxytamoxifen. Mol. Endocrinol. 11 (1997) 657-666
69. Lavinsky R.M., Jepsen K., Heinzel T., Torchia J., Mullen T.M., Schiff R., Del-Rio A.L., Ricote M., Ngo S., Gemsch J., Hilsenbeck S.G., Osborne C.K., Glass C.K., Rosenfeld M.G., and Rose D.W. Diverse signaling pathways modulate nuclear receptor recruitment of N-CoR and SMRT complexes. Proc. Natl. Acad. Sci. U.S.A. 95 (1998) 2920-2925
70. Webb P., Nguyen P., and Kushner P.J. Differential SERM effects on corepressor binding dictate ERα activity in vivo. J. Biol. Chem. 278 (2003) 6912-6920
71. Metivier R., Petit F.G., Valotaire Y., and Pakdel F. Function of N-terminal transactivation domain of the estrogen receptor requires a potential alpha-helical structure and is negatively regulated by the A domain. Mol. Endocrinol. 14 (2000) 1849-1871
72. Sathya G., Yi P., Bhagat S., Bambara R.A., Hilf R., and Muyan M. Structural regions of ERα critical for synergistic transcriptional responses contain co-factor interacting surfaces. Mol. Cell Endocrinol. 192 (2002) 171-185
73. Webb P., Valentine C., Nguyen P., Price Jr. R.H., Marimuthu A., West B.L., Baxter J.D., and Kushner P.J. ERβ binds N-CoR in the presence of estrogens via an LXXLL-like motif in the N-CoR C-terminus. Nucl. Recept. 1 (2003) 4
74. Gao Z., Chiao P., Zhang X., Zhang X., Lazar M.A., Seto E., Young H.A., and Ye J. Coactivators and corepressors of NF-κB in IκB α gene promoter. J. Biol. Chem. 280 (2005) 21091-21098
75. Tremblay G.B., Tremblay A., Labrie F., and Giguere V. Dominant activity of activation function 1 (AF-1) and differential stoichiometric requirements for AF-1 and -2 in the estrogen receptor α-β heterodimeric complex. Mol. Cell Biol. 19 (1999) 1919-1927
76. Tremblay A., Tremblay G.B., Labrie F., and Giguere V. Ligand-independent recruitment of SRC-1 to estrogen receptor β through phosphorylation of activation function AF-1. Mol. Cell 3 (1999) 513-519
77. Kushner P.J., Agard D.A., Greene G.L., Scanlan T.S., Shiau A.K., Uht R.M., and Webb P. Estrogen receptor pathways to AP-1. J. Steroid Biochem. Mol. Biol. 74 (2000) 311-317
78. Safe S. Transcriptional activation of genes by 17β-estradiol through estrogen receptor-Sp1 interactions. Vitam. Horm. 62 (2001) 231-252
79. Levin E.R. Cellular functions of plasma membrane estrogen receptors. Steroids 67 (2002) 471-475