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Volumn 44, Issue 2, 2005, Pages 790-798

Interplay of flexibility and stability in the control of estrogen receptor activity

Author keywords

[No Author keywords available]

Indexed keywords

COMPLEXATION; DISSOCIATION; DNA; PROTEINS; STOICHIOMETRY;

EID: 12144251362     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0483716     Document Type: Article
Times cited : (7)

References (56)
  • 1
    • 0036151490 scopus 로고    scopus 로고
    • TBP dynamics in living human cells: Constitutive association of TBP with mitotic chromosomes
    • Chen, D., Hinkley, C. S., Henry, R. W., and Huang, S. (2002) TBP dynamics in living human cells: constitutive association of TBP with mitotic chromosomes, Mol. Biol. Cell 13, 276-284.
    • (2002) Mol. Biol. Cell , vol.13 , pp. 276-284
    • Chen, D.1    Hinkley, C.S.2    Henry, R.W.3    Huang, S.4
  • 2
    • 0343415609 scopus 로고    scopus 로고
    • The glucocorticoid receptor: Rapid exchange with regulatory sites in living cells
    • McNally, J. G., Muller, W. G., Walker, D., Wolford, R., and Hager, G. L. (2000) The glucocorticoid receptor: rapid exchange with regulatory sites in living cells, Science 287, 1262-1265.
    • (2000) Science , vol.287 , pp. 1262-1265
    • McNally, J.G.1    Muller, W.G.2    Walker, D.3    Wolford, R.4    Hager, G.L.5
  • 3
    • 0035793376 scopus 로고    scopus 로고
    • Protein dynamics: Implications for nuclear architecture and gene expression
    • Misteli, T. (2001) Protein dynamics: implications for nuclear architecture and gene expression, Science 291, 843-847.
    • (2001) Science , vol.291 , pp. 843-847
    • Misteli, T.1
  • 5
    • 0042767995 scopus 로고    scopus 로고
    • The dynamics of chromosome organization and gene regulation
    • Spector, D. L. (2003) The dynamics of chromosome organization and gene regulation. Annu. Rev. Biochem. 72, 573-608.
    • (2003) Annu. Rev. Biochem. , vol.72 , pp. 573-608
    • Spector, D.L.1
  • 6
    • 0035839136 scopus 로고    scopus 로고
    • Translating the histone code
    • Jenuwein, T., and Allis, C. D. (2001) Translating the histone code, Science 293, 1074-1080.
    • (2001) Science , vol.293 , pp. 1074-1080
    • Jenuwein, T.1    Allis, C.D.2
  • 7
    • 0035924326 scopus 로고    scopus 로고
    • Selectivity of chromatin-remodelling cofactors for ligand-activated transcription
    • Lemon, B., Inouye, C., King, D. S., and Tjian, R. (2001) Selectivity of chromatin-remodelling cofactors for ligand-activated transcription, Nature 414, 924-928.
    • (2001) Nature , vol.414 , pp. 924-928
    • Lemon, B.1    Inouye, C.2    King, D.S.3    Tjian, R.4
  • 8
    • 0036532111 scopus 로고    scopus 로고
    • Protein dynamics in the nuclear compartment
    • Hager, G. L., Elbi, C., and Becker, M. (2002) Protein dynamics in the nuclear compartment, Curr. Opin. Genet. Dev. 12, 137-141.
    • (2002) Curr. Opin. Genet. Dev. , vol.12 , pp. 137-141
    • Hager, G.L.1    Elbi, C.2    Becker, M.3
  • 9
    • 0034611785 scopus 로고    scopus 로고
    • High mobility of proteins in the mammalian cell nucleus
    • Phair, R. D., and Misteli, T. (2000) High mobility of proteins in the mammalian cell nucleus, Nature 404, 604-609.
    • (2000) Nature , vol.404 , pp. 604-609
    • Phair, R.D.1    Misteli, T.2
  • 10
    • 0035954427 scopus 로고    scopus 로고
    • Kinetics of core histones in living human cells: Little exchange of H3 and H4 and some rapid exchange of H2B
    • Kimura, H., and Cook, P. R. (2001) Kinetics of core histones in living human cells: little exchange of H3 and H4 and some rapid exchange of H2B, J. Cell. Biol. 153, 1341-1353.
    • (2001) J. Cell. Biol. , vol.153 , pp. 1341-1353
    • Kimura, H.1    Cook, P.R.2
  • 11
    • 0037150683 scopus 로고    scopus 로고
    • Disassembly of transcriptional regulatory complexes by molecular chaperones
    • Freeman, B. C., and Yamamoto, K. R. (2002) Disassembly of transcriptional regulatory complexes by molecular chaperones, Science 296, 2232-2235.
    • (2002) Science , vol.296 , pp. 2232-2235
    • Freeman, B.C.1    Yamamoto, K.R.2
  • 13
    • 0031983379 scopus 로고    scopus 로고
    • Localization and functions of steroid hormone receptors
    • Yamashita, S. (1998) Localization and functions of steroid hormone receptors, Histol. Histopathol. 13, 255-270.
    • (1998) Histol. Histopathol. , vol.13 , pp. 255-270
    • Yamashita, S.1
  • 16
    • 0029012163 scopus 로고
    • Crystal structure of the ligand-binding domain of the human nuclear receptor RXR-alpha
    • Bourguet, W., Ruff, M., Chambon, P., Gronemeyer, H., and Moras, D. (1995) Crystal structure of the ligand-binding domain of the human nuclear receptor RXR-alpha, Nature 375, 377-382.
    • (1995) Nature , vol.375 , pp. 377-382
    • Bourguet, W.1    Ruff, M.2    Chambon, P.3    Gronemeyer, H.4    Moras, D.5
  • 20
    • 0030601135 scopus 로고    scopus 로고
    • Phosphorylation of purified estradiol-liganded estrogen receptor by casein kinase II increases estrogen response element binding but does not alter ligand stability
    • Tzeng, D. Z., and Klinge, C. (1996) Phosphorylation of purified estradiol-liganded estrogen receptor by casein kinase II increases estrogen response element binding but does not alter ligand stability, Biochem. Biophys. Res. Commun. 223, 554-560.
    • (1996) Biochem. Biophys. Res. Commun. , vol.223 , pp. 554-560
    • Tzeng, D.Z.1    Klinge, C.2
  • 21
    • 0038813724 scopus 로고    scopus 로고
    • Regulation of estrogen receptor alpha-mediated transcription by a direct interaction with protein phosphatase 2A
    • Lu, Q., Surks, H. K., Ebling, H., Baur, W. E., Brown, D., Pallas, D. C., and Karas, R. H. (2003) Regulation of estrogen receptor alpha-mediated transcription by a direct interaction with protein phosphatase 2A, J. Biol. Chem. 278, 4639-4645.
    • (2003) J. Biol. Chem. , vol.278 , pp. 4639-4645
    • Lu, Q.1    Surks, H.K.2    Ebling, H.3    Baur, W.E.4    Brown, D.5    Pallas, D.C.6    Karas, R.H.7
  • 23
    • 0032486380 scopus 로고    scopus 로고
    • RAP46 is a negative regulator of glucocorticoid receptor action and hormone-induced apoptosis
    • Kullmann, M., Schneikert, J., Moll, J., Heck, S., Zeiner, M., Gehring, U., and Cato, A. C. (1998) RAP46 is a negative regulator of glucocorticoid receptor action and hormone-induced apoptosis, J. Biol. Chem. 273, 14620-14625.
    • (1998) J. Biol. Chem. , vol.273 , pp. 14620-14625
    • Kullmann, M.1    Schneikert, J.2    Moll, J.3    Heck, S.4    Zeiner, M.5    Gehring, U.6    Cato, A.C.7
  • 24
    • 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
    • Montano, M. M., Muller, V., Trobaugh, A., and Katzenellenbogen, B. S. (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
  • 25
    • 0022653964 scopus 로고
    • Human oestrogen receptor cDNA: Sequence, expression and homology to v-erb-A
    • Green, S., Walter, P., Kumar, V., Krust, A., Bornert, J. M., Argos, P., and Chambon, P. (1986) Human oestrogen receptor cDNA: sequence, expression and homology to v-erb-A, Nature 320, 134-139.
    • (1986) Nature , vol.320 , pp. 134-139
    • Green, S.1    Walter, P.2    Kumar, V.3    Krust, A.4    Bornert, J.M.5    Argos, P.6    Chambon, P.7
  • 27
    • 0034283016 scopus 로고    scopus 로고
    • Identification of a new isoform of the human estrogen receptor-alpha (hER-alpha) that is encoded by distinct transcripts and that is able to repress hER-alpha activation function 1
    • Flouriot, G., Brand, H., Denger, S., Metivier, R., Kos, M., Reid, G., Sonntag-Buck, V., and Gannon, F. (2000) Identification of a new isoform of the human estrogen receptor-alpha (hER-alpha) that is encoded by distinct transcripts and that is able to repress hER-alpha activation function 1, EMBO J. 247, 4688-4700.
    • (2000) EMBO J. , vol.247 , pp. 4688-4700
    • Flouriot, G.1    Brand, H.2    Denger, S.3    Metivier, R.4    Kos, M.5    Reid, G.6    Sonntag-Buck, V.7    Gannon, F.8
  • 29
    • 0035878743 scopus 로고    scopus 로고
    • Estrogen receptor interaction with estrogen response elements
    • Klinge, C. M. (2001) Estrogen receptor interaction with estrogen response elements, Nucleic Acids Res. 29, 2905-2919.
    • (2001) Nucleic Acids Res. , vol.29 , pp. 2905-2919
    • Klinge, C.M.1
  • 30
    • 0027365669 scopus 로고
    • The crystal structure of the estrogen receptor DNA-binding domain bound to DNA: How receptors discriminate between their response elements
    • Schwabe, J. W., Chapman, L., Finch, J. T., and 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.1    Chapman, L.2    Finch, J.T.3    Rhodes, D.4
  • 31
    • 0037040967 scopus 로고    scopus 로고
    • Differential modulation of DNA conformation by estrogen receptors alpha and beta
    • Schultz, J. R., Loven, M. A., Melvin, V. M., Edwards, D. P., and Nardulli, A. M. (2002) Differential modulation of DNA conformation by estrogen receptors alpha and beta, J. Biol. Chem. 277, 8702-8707.
    • (2002) J. Biol. Chem. , vol.277 , pp. 8702-8707
    • Schultz, J.R.1    Loven, M.A.2    Melvin, V.M.3    Edwards, D.P.4    Nardulli, A.M.5
  • 32
    • 0025313903 scopus 로고
    • Full-length sequence and in vitro expression of rainbow trout estrogen receptor cDNA
    • Pakdel, F., Le Gac, F., Le Goff, P., and Valotaire, Y. (1990) Full-length sequence and in vitro expression of rainbow trout estrogen receptor cDNA, Mol. Cell. Endocrinol. 71, 195-204.
    • (1990) Mol. Cell. Endocrinol. , vol.71 , pp. 195-204
    • Pakdel, F.1    Le Gac, F.2    Le Goff, P.3    Valotaire, Y.4
  • 33
    • 0030606153 scopus 로고    scopus 로고
    • Transcriptional and posttranscriptional regulation of rainbow trout estrogen receptor and vitellogenin gene expression
    • Flouriot, G., Pakdel, F., and Valotaire, Y. (1996) Transcriptional and posttranscriptional regulation of rainbow trout estrogen receptor and vitellogenin gene expression, Mol. Cell. Endocrinol. 124, 173-183.
    • (1996) Mol. Cell. Endocrinol. , vol.124 , pp. 173-183
    • Flouriot, G.1    Pakdel, F.2    Valotaire, Y.3
  • 34
    • 0030828374 scopus 로고    scopus 로고
    • Differential regulation of two genes implicated in fish reproduction: Vitellogenin and estrogen receptor genes
    • Flouriot, G., Pakdel, F., Ducouret, B., Ledrean, Y., and Valotaire, Y. (1997) Differential regulation of two genes implicated in fish reproduction: vitellogenin and estrogen receptor genes, Mol. Reprod. Dev. 48, 317-323.
    • (1997) Mol. Reprod. Dev. , vol.48 , pp. 317-323
    • Flouriot, G.1    Pakdel, F.2    Ducouret, B.3    Ledrean, Y.4    Valotaire, Y.5
  • 35
    • 0034463492 scopus 로고    scopus 로고
    • Two estrogen receptor (ER) isoforms with different estrogen dependencies are generated from the trout ER gene
    • Pakdel, F., Metivier, R., Flouriot, G., and Valotaire, Y. (2000) Two estrogen receptor (ER) isoforms with different estrogen dependencies are generated from the trout ER gene, Endocrinology 141, 571-580.
    • (2000) Endocrinology , vol.141 , pp. 571-580
    • Pakdel, F.1    Metivier, R.2    Flouriot, G.3    Valotaire, Y.4
  • 36
    • 0028857010 scopus 로고
    • Differential functional activities of rainbow trout and human estrogen receptors expressed in the yeast Saccharomyces cerevisiae
    • Petit, F. G., Valotaire, Y., and Pakdel, F. (1995) Differential functional activities of rainbow trout and human estrogen receptors expressed in the yeast Saccharomyces cerevisiae, Eur. J. Biochem. 233, 584-592.
    • (1995) Eur. J. Biochem. , vol.233 , pp. 584-592
    • Petit, F.G.1    Valotaire, Y.2    Pakdel, F.3
  • 38
    • 0034969440 scopus 로고    scopus 로고
    • Allosteric modulation of estrogen receptor conformation by different estrogen response elements
    • Wood, J. R., Likhite, V. S., Loven, M. A., and Nardulli, A. M. (2001) Allosteric modulation of estrogen receptor conformation by different estrogen response elements, Mol. Endocrinol. 15, 1114-1126.
    • (2001) Mol. Endocrinol. , vol.15 , pp. 1114-1126
    • Wood, J.R.1    Likhite, V.S.2    Loven, M.A.3    Nardulli, A.M.4
  • 39
    • 1042301372 scopus 로고    scopus 로고
    • Interplay between estrogen response element sequence and ligands controls in vivo binding of estrogen receptor to regulated genes
    • Krieg, A. J., Krieg, S. A., Ahn, B. S., and Shapiro, D. J. (2004) Interplay between estrogen response element sequence and ligands controls in vivo binding of estrogen receptor to regulated genes, J. Biol. Chem. 279, 5025-5034.
    • (2004) J. Biol. Chem. , vol.279 , pp. 5025-5034
    • Krieg, A.J.1    Krieg, S.A.2    Ahn, B.S.3    Shapiro, D.J.4
  • 40
    • 0032524648 scopus 로고    scopus 로고
    • A yeast recombinant aquaporin mutant that is not expressed or mistargeted in Xenopus oocyte can be functionally analyzed in reconstituted proteoliposomes
    • Lagree, V., Pellerin, I., Hubert, J. F., Tacnet, F., Le Caherec, F., Roudier, N., Thomas, D., Gouranton, J., and Deschamps, S. (1998) A yeast recombinant aquaporin mutant that is not expressed or mistargeted in Xenopus oocyte can be functionally analyzed in reconstituted proteoliposomes, J. Biol. Chem. 273, 12422-12426.
    • (1998) J. Biol. Chem. , vol.273 , pp. 12422-12426
    • Lagree, V.1    Pellerin, I.2    Hubert, J.F.3    Tacnet, F.4    Le Caherec, F.5    Roudier, N.6    Thomas, D.7    Gouranton, J.8    Deschamps, S.9
  • 41
    • 0017288499 scopus 로고
    • Exposure of tryptophanyl residues in proteins. Quantitative determination by fluorescence quenching studies
    • Eftink, M. R., and Ghiron, C. A. (1976) Exposure of tryptophanyl residues in proteins. Quantitative determination by fluorescence quenching studies, Biochemistry 15, 672-680.
    • (1976) Biochemistry , vol.15 , pp. 672-680
    • Eftink, M.R.1    Ghiron, C.A.2
  • 42
    • 0017571023 scopus 로고
    • Exposure of tryptophanyl residues and protein dynamics
    • Eftink, M. R., and Ghiron, C. A. (1977) Exposure of tryptophanyl residues and protein dynamics, Biochemistry 16, 5546-5551.
    • (1977) Biochemistry , vol.16 , pp. 5546-5551
    • Eftink, M.R.1    Ghiron, C.A.2
  • 43
    • 0003373982 scopus 로고    scopus 로고
    • Preliminary investigation of the interaction between the R2R3 DNA binding domain of the oncoprotein C-Myb and DNA fragments
    • Jamin, N., Tilly, V. L., Zargarian, L., Besancon-Yoshpe, J., Lirsac, P. N., Gabrielsen, O. S., and Toma, F. (1996) Preliminary investigation of the interaction between the R2R3 DNA binding domain of the oncoprotein C-Myb and DNA fragments, Int. J. Quantum Chem. 59, 333-341.
    • (1996) Int. J. Quantum Chem. , vol.59 , pp. 333-341
    • Jamin, N.1    Tilly, V.L.2    Zargarian, L.3    Besancon-Yoshpe, J.4    Lirsac, P.N.5    Gabrielsen, O.S.6    Toma, F.7
  • 44
    • 0027214299 scopus 로고
    • Fluorescence anisotropy assays implicate protein-protein interactions in regulating trp repressor DNA binding
    • LeTilly, V., and Royer, C. A. (1993) Fluorescence anisotropy assays implicate protein-protein interactions in regulating trp repressor DNA binding, Biochemistry 32, 7753-7758.
    • (1993) Biochemistry , vol.32 , pp. 7753-7758
    • LeTilly, V.1    Royer, C.A.2
  • 45
    • 0034235830 scopus 로고    scopus 로고
    • Quantitative characterization of the interaction between purified human estrogen receptor alpha and DNA using fluorescence anisotropy
    • Boyer, M., Poujol, N., Margeat, E., and Royer, C. A. (2000) Quantitative characterization of the interaction between purified human estrogen receptor alpha and DNA using fluorescence anisotropy, Nucleic Acids Res. 28, 2494-2502.
    • (2000) Nucleic Acids Res. , vol.28 , pp. 2494-2502
    • Boyer, M.1    Poujol, N.2    Margeat, E.3    Royer, C.A.4
  • 47
    • 0016289101 scopus 로고
    • Stacking specificity and polarization. Comparative synopsis of affinity data
    • Lawaczeck, R., and Wagner, K. G. (1974) Stacking specificity and polarization. Comparative synopsis of affinity data, Biopolymers 13, 2003-2314.
    • (1974) Biopolymers , vol.13 , pp. 2003-2314
    • Lawaczeck, R.1    Wagner, K.G.2
  • 48
    • 0021115982 scopus 로고
    • The stacking interactions in 7-methylguanine-tryptophan systems, a model study for the interaction between the 'cap' structure of mRNA and its binding protein
    • Ishida, T., Katsuta, M., Inoue, M., Yamagata, Y., and Tomita, K. (1983) The stacking interactions in 7-methylguanine-tryptophan systems, a model study for the interaction between the 'cap' structure of mRNA and its binding protein, Biochem. Biophys. Res. Commun. 115, 849-854.
    • (1983) Biochem. Biophys. Res. Commun. , vol.115 , pp. 849-854
    • Ishida, T.1    Katsuta, M.2    Inoue, M.3    Yamagata, Y.4    Tomita, K.5
  • 49
    • 0016663420 scopus 로고
    • Interactions of aromatic residues of proteins with nucleic acids. Fluorescence studies of the binding of oligopeptides containing tryptophan and tyrosine residues to polynucleotides
    • Brun, F., Toulme, J. J., and Helene, C. (1975) Interactions of aromatic residues of proteins with nucleic acids. Fluorescence studies of the binding of oligopeptides containing tryptophan and tyrosine residues to polynucleotides, Biochemistry 14, 558-563.
    • (1975) Biochemistry , vol.14 , pp. 558-563
    • Brun, F.1    Toulme, J.J.2    Helene, C.3
  • 50
    • 0021287681 scopus 로고
    • 3H]estriol to induce maximal cooperativity of the estrogen receptor
    • 3H]estriol to induce maximal cooperativity of the estrogen receptor, J. Steroid Biochem. 20, 1027-1032.
    • (1984) J. Steroid Biochem. , vol.20 , pp. 1027-1032
    • Sasson, S.1    Notides, A.C.2
  • 51
    • 0022360933 scopus 로고
    • Modulation of the estrogen receptor's affinity for DNA by estradiol
    • Skafar, D. F., and Notides, A. C. (1985) Modulation of the estrogen receptor's affinity for DNA by estradiol, J. Biol. Chem. 260, 12208-12213.
    • (1985) J. Biol. Chem. , vol.260 , pp. 12208-12213
    • Skafar, D.F.1    Notides, A.C.2
  • 52
    • 0030805890 scopus 로고    scopus 로고
    • Binding of the estrogen receptor to DNA. The role of waters
    • Kosztin, D., Bishop, T. C., and Schulten, K. (1997) Binding of the estrogen receptor to DNA. The role of waters, Biophys. J. 73, 557-570.
    • (1997) Biophys. J. , vol.73 , pp. 557-570
    • Kosztin, D.1    Bishop, T.C.2    Schulten, K.3
  • 53
    • 0035946567 scopus 로고    scopus 로고
    • The dissociation rate of estrogen receptor alpha from the consensus estrogen response element
    • Szatkowski Ozers, M., Hill, J. J., Ervin, K., Royer, C. A., and Gorski, J. (2001) The dissociation rate of estrogen receptor alpha from the consensus estrogen response element, Mol. Cell. Endocrinol. 175, 101-109.
    • (2001) Mol. Cell. Endocrinol. , vol.175 , pp. 101-109
    • Szatkowski Ozers, M.1    Hill, J.J.2    Ervin, K.3    Royer, C.A.4    Gorski, J.5
  • 54
    • 0029952990 scopus 로고    scopus 로고
    • Direct study of DNA-protein interactions in repressed and active chromatin in living cells
    • Kladde, M. P., Xu, M., and Simpson, R. T. (1996) Direct study of DNA-protein interactions in repressed and active chromatin in living cells, EMBO J. 15, 6290-6300.
    • (1996) EMBO J. , vol.15 , pp. 6290-6300
    • Kladde, M.P.1    Xu, M.2    Simpson, R.T.3
  • 55
    • 0029560401 scopus 로고
    • Quantitative determination of DNA-binding parameters for the human estrogen receptor in a solid-phase, nonseparation assay
    • Carlsson, B., and Haggblad, J. (1995) Quantitative determination of DNA-binding parameters for the human estrogen receptor in a solid-phase, nonseparation assay, Anal. Biochem. 232, 172-179.
    • (1995) Anal. Biochem. , vol.232 , pp. 172-179
    • Carlsson, B.1    Haggblad, J.2


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