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Volumn 9, Issue 5, 2013, Pages 326-332

Ligand-binding dynamics rewire cellular signaling via estrogen receptor-α

Author keywords

[No Author keywords available]

Indexed keywords

DIETHYLSTILBESTROL; DNA; DNA BINDING PROTEIN; ESTROGEN; ESTROGEN RECEPTOR ALPHA; GREB1 PROTEIN; LIGAND; PROTEIN TYROSINE KINASE; TAMOXIFEN; UNCLASSIFIED DRUG;

EID: 84879115207     PISSN: 15524450     EISSN: 15524469     Source Type: Journal    
DOI: 10.1038/nchembio.1214     Document Type: Article
Times cited : (52)

References (50)
  • 2
    • 84857190619 scopus 로고    scopus 로고
    • Evidence for dynamics in proteins as a mechanism for ligand dissociation
    • Carroll, M.J. et al. Evidence for dynamics in proteins as a mechanism for ligand dissociation. Nat. Chem. Biol. 8, 246-252 (2012).
    • (2012) Nat. Chem. Biol , vol.8 , pp. 246-252
    • Carroll, M.J.1
  • 3
    • 0032446607 scopus 로고    scopus 로고
    • The structural basis of estrogen receptor/coactivator recognition and the antagonism of this interaction by tamoxifen
    • Shiau, A.K. et al. The structural basis of estrogen receptor/coactivator recognition and the antagonism of this interaction by tamoxifen. Cell 95, 927-937 (1998).
    • (1998) Cell , vol.95 , pp. 927-937
    • Shiau, A.K.1
  • 4
    • 38749144353 scopus 로고    scopus 로고
    • CBP Is a dosage-dependent regulator of nuclear factor-κB suppression by the estrogen receptor
    • Nettles, K.W. et al. CBP Is a dosage-dependent regulator of nuclear factor-κB suppression by the estrogen receptor. Mol. Endocrinol. 22, 263-272 (2008).
    • (2008) Mol. Endocrinol , vol.22 , pp. 263-272
    • Nettles, K.W.1
  • 5
    • 77958157879 scopus 로고    scopus 로고
    • Coupling of receptor conformation and ligand orientation determine graded activity
    • Bruning, J.B. et al. Coupling of receptor conformation and ligand orientation determine graded activity. Nat. Chem. Biol. 6, 837-843 (2010).
    • (2010) Nat. Chem. Biol , vol.6 , pp. 837-843
    • Bruning, J.B.1
  • 6
    • 84855795379 scopus 로고    scopus 로고
    • Ligand and receptor dynamics contribute to the mechanism of graded PPARγ agonism
    • Hughes, T.S. et al. Ligand and receptor dynamics contribute to the mechanism of graded PPARγ agonism. Structure 20, 139-150 (2012).
    • (2012) Structure , vol.20 , pp. 139-150
    • Hughes, T.S.1
  • 7
    • 79955031227 scopus 로고    scopus 로고
    • Direct detection of structurally resolved dynamics in a multiconformation receptor-ligand complex
    • Carroll, M.J. et al. Direct detection of structurally resolved dynamics in a multiconformation receptor-ligand complex. J. Am. Chem. Soc. 133, 6422-6428 (2011).
    • (2011) J. Am. Chem. Soc , vol.133 , pp. 6422-6428
    • Carroll, M.J.1
  • 8
    • 0033637703 scopus 로고    scopus 로고
    • Cofactor dynamics and sufficiency in estrogen receptor-regulated transcription
    • Shang, Y., Hu, X., DiRenzo, J., Lazar, M.A. & Brown, M. Cofactor dynamics and sufficiency in estrogen receptor-regulated transcription. Cell 103, 843-852 (2000).
    • (2000) Cell , vol.103 , pp. 843-852
    • Shang, Y.1    Hu, X.2    Direnzo, J.3    Lazar, M.A.4    Brown, M.5
  • 9
    • 65249167505 scopus 로고    scopus 로고
    • DNA binding site sequence directs glucocorticoid receptor structure and activity
    • Meijsing, S.H. et al. DNA binding site sequence directs glucocorticoid receptor structure and activity. Science 324, 407-410 (2009).
    • (2009) Science , vol.324 , pp. 407-410
    • Meijsing, S.H.1
  • 10
    • 0029796605 scopus 로고    scopus 로고
    • Different regions in activation function-1 of the human estrogen receptor required for antiestrogen-and estradiol-dependent transcription activation
    • McInerney, E.M. & Katzenellenbogen, B.S. Different regions in activation function-1 of the human estrogen receptor required for antiestrogen-and estradiol-dependent transcription activation. J. Biol. Chem. 271, 24172-24178 (1996).
    • (1996) J. Biol. Chem , vol.271 , pp. 24172-24178
    • McInerney, E.M.1    Katzenellenbogen, B.S.2
  • 11
    • 15544371000 scopus 로고    scopus 로고
    • Ligand control of coregulator recruitment to nuclear receptors
    • Nettles, K.W. & Greene, G.L. Ligand control of coregulator recruitment to nuclear receptors. Annu. Rev. Physiol. 67, 309-333 (2005).
    • (2005) Annu. Rev. Physiol , vol.67 , pp. 309-333
    • Nettles, K.W.1    Greene, G.L.2
  • 12
    • 0032213219 scopus 로고    scopus 로고
    • Structure and specificity of nuclear receptor-coactivator interactions
    • Darimont, B.D. et al. Structure and specificity of nuclear receptor-coactivator interactions. Genes Dev. 12, 3343-3356 (1998).
    • (1998) Genes Dev , vol.12 , pp. 3343-3356
    • Darimont, B.D.1
  • 13
    • 0029012163 scopus 로고
    • Crystal structure of the ligand-binding domain of the human nuclear receptor RXR-α
    • Bourguet, W., Ruff, M., Chambon, P., Gronemeyer, H. & Moras, D. Crystal structure of the ligand-binding domain of the human nuclear receptor RXR-α. Nature 375, 377-382 (1995).
    • (1995) Nature , vol.375 , pp. 377-382
    • Bourguet, W.1    Ruff, M.2    Chambon, P.3    Gronemeyer, H.4    Moras, D.5
  • 14
    • 18244393501 scopus 로고    scopus 로고
    • Structural basis for antagonist-mediated recruitment of nuclear co-repressors by PPARα
    • Xu, H.E. et al. Structural basis for antagonist-mediated recruitment of nuclear co-repressors by PPARα. Nature 415, 813-817 (2002).
    • (2002) Nature , vol.415 , pp. 813-817
    • Xu, H.E.1
  • 15
    • 34547653666 scopus 로고    scopus 로고
    • Structural plasticity in the oestrogen receptor ligand-binding domain
    • erratum 8, 610 (2007)
    • Nettles, K.W. et al. Structural plasticity in the oestrogen receptor ligand-binding domain. EMBO Rep. 8, 563-568 (2007); erratum 8, 610 (2007).
    • (2007) EMBO Rep. , vol.8 , pp. 563-568
    • Nettles, K.W.1
  • 16
    • 20044371621 scopus 로고    scopus 로고
    • Identification of pathway-selective estrogen receptor ligands that inhibit NF-κB transcriptional activity
    • Chadwick, C.C. et al. Identification of pathway-selective estrogen receptor ligands that inhibit NF-κB transcriptional activity. Proc. Natl. Acad. Sci. USA 102, 2543-2548 (2005).
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 2543-2548
    • Chadwick, C.C.1
  • 17
    • 1242294391 scopus 로고    scopus 로고
    • Allosteric control of ligand selectivity between estrogen receptors α and β: Implications for other nuclear receptors
    • Nettles, K.W. et al. Allosteric control of ligand selectivity between estrogen receptors α and β: implications for other nuclear receptors. Mol. Cell 13, 317-327 (2004).
    • (2004) Mol. Cell , vol.13 , pp. 317-327
    • Nettles, K.W.1
  • 18
    • 84870535838 scopus 로고    scopus 로고
    • Structural mechanisms of allostery and autoinhibition in JNK family kinases
    • Laughlin, J.D. et al. Structural mechanisms of allostery and autoinhibition in JNK family kinases. Structure 20, 2174-2184 (2012).
    • (2012) Structure , vol.20 , pp. 2174-2184
    • Laughlin, J.D.1
  • 19
    • 0037192501 scopus 로고    scopus 로고
    • Molecular determinants for the tissue specificity of SERMs
    • Shang, Y. & Brown, M. Molecular determinants for the tissue specificity of SERMs. Science 295, 2465-2468 (2002).
    • (2002) Science , vol.295 , pp. 2465-2468
    • Shang, Y.1    Brown, M.2
  • 20
    • 0031452274 scopus 로고    scopus 로고
    • Structures of Src-family tyrosine kinases
    • Sicheri, F. & Kuriyan, J. Structures of Src-family tyrosine kinases. Curr. Opin. Struct. Biol. 7, 777-785 (1997).
    • (1997) Curr. Opin. Struct. Biol , vol.7 , pp. 777-785
    • Sicheri, F.1    Kuriyan, J.2
  • 21
    • 0030986236 scopus 로고    scopus 로고
    • A signature motif in transcriptional co-activators mediates binding to nuclear receptors
    • Heery, D.M., Kalkhoven, E., Hoare, S. & Parker, M.G. A signature motif in transcriptional co-activators mediates binding to nuclear receptors. Nature 387, 733-736 (1997).
    • (1997) Nature , vol.387 , pp. 733-736
    • Heery, D.M.1    Kalkhoven, E.2    Hoare, S.3    Parker, M.G.4
  • 22
    • 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. 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).
    • (1990) EMBO J. , vol.9 , pp. 2811-2818
    • Berry, M.1    Metzger, D.2    Chambon, P.3
  • 23
    • 0026341234 scopus 로고
    • Antiestrogen can establish nonproductive receptor complexes and alter chromatin structure at target enhancers
    • Pham, T.A. et al. Antiestrogen can establish nonproductive receptor complexes and alter chromatin structure at target enhancers. Proc. Natl. Acad. Sci. USA 88, 3125-3129 (1991).
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 3125-3129
    • Pham, T.A.1
  • 24
    • 34247898925 scopus 로고    scopus 로고
    • Raloxifene and ICI182,780 increase estrogen receptor-α association with a nuclear compartment via overlapping sets of hydrophobic amino acids in activation function 2 helix 12
    • Lupien, M. et al. Raloxifene and ICI182,780 increase estrogen receptor-α association with a nuclear compartment via overlapping sets of hydrophobic amino acids in activation function 2 helix 12. Mol. Endocrinol. 21, 797-816 (2007).
    • (2007) Mol. Endocrinol , vol.21 , pp. 797-816
    • Lupien, M.1
  • 26
    • 69249110003 scopus 로고    scopus 로고
    • Normal and cancer-related functions of the p160 steroid receptor co-activator (SRC) family
    • Xu, J., Wu, R.C. & O'Malley, B.W. Normal and cancer-related functions of the p160 steroid receptor co-activator (SRC) family. Nat. Rev. Cancer 9, 615-630 (2009).
    • (2009) Nat. Rev. Cancer , vol.9 , pp. 615-630
    • Xu, J.1    Wu, R.C.2    O'Malley, B.W.3
  • 27
    • 21644489751 scopus 로고    scopus 로고
    • GREB 1 is a critical regulator of hormone dependent breast cancer growth
    • Rae, J.M. et al. GREB 1 is a critical regulator of hormone dependent breast cancer growth. Breast Cancer Res. Treat. 92, 141-149 (2005).
    • (2005) Breast Cancer Res. Treat , vol.92 , pp. 141-149
    • Rae, J.M.1
  • 28
    • 33748679908 scopus 로고    scopus 로고
    • A cell-type-specific transcriptional network required for estrogen regulation of cyclin D1 and cell cycle progression in breast cancer
    • Eeckhoute, J., Carroll, J.S., Geistlinger, T.R., Torres-Arzayus, M.I. & Brown, M. A cell-type-specific transcriptional network required for estrogen regulation of cyclin D1 and cell cycle progression in breast cancer. Genes Dev. 20, 2513-2526 (2006).
    • (2006) Genes Dev , vol.20 , pp. 2513-2526
    • Eeckhoute, J.1    Carroll, J.S.2    Geistlinger, T.R.3    Torres-Arzayus, M.I.4    Brown, M.5
  • 29
    • 23844448634 scopus 로고    scopus 로고
    • Knockdown of c-Myc expression by RNAi inhibits MCF-7 breast tumor cells growth in vitro and in vivo
    • Wang, Y.H. et al. Knockdown of c-Myc expression by RNAi inhibits MCF-7 breast tumor cells growth in vitro and in vivo. Breast Cancer Res. 7, R220-R228 (2005).
    • (2005) Breast Cancer Res , vol.7
    • Wang, Y.H.1
  • 30
    • 80052290466 scopus 로고    scopus 로고
    • Estrogen induces c-myc gene expression via an upstream enhancer activated by the estrogen receptor and the AP-1 transcription factor
    • Wang, C. et al. Estrogen induces c-myc gene expression via an upstream enhancer activated by the estrogen receptor and the AP-1 transcription factor. Mol. Endocrinol. 25, 1527-1538 (2011).
    • (2011) Mol. Endocrinol , vol.25 , pp. 1527-1538
    • Wang, C.1
  • 31
    • 84863066879 scopus 로고    scopus 로고
    • Identification of estrogen receptor dimer selective ligands reveals growth-inhibitory effects on cells that co-express ERα and ERβ
    • Powell, E. et al. Identification of estrogen receptor dimer selective ligands reveals growth-inhibitory effects on cells that co-express ERα and ERβ. PLoS ONE 7, e30993 (2012).
    • (2012) PLoS ONE , vol.7
    • Powell, E.1
  • 32
    • 33646728919 scopus 로고    scopus 로고
    • GREB1 is a novel androgen-regulated gene required for prostate cancer growth
    • Rae, J.M. et al. GREB1 is a novel androgen-regulated gene required for prostate cancer growth. Prostate 66, 886-894 (2006).
    • (2006) Prostate , vol.66 , pp. 886-894
    • Rae, J.M.1
  • 33
    • 0035976933 scopus 로고    scopus 로고
    • Estrogen response elements alter coactivator recruitment through allosteric modulation of estrogen receptor β conformation
    • Loven, M.A., Likhite, V.S., Choi, I. & Nardulli, A.M. Estrogen response elements alter coactivator recruitment through allosteric modulation of estrogen receptor β conformation. J. Biol. Chem. 276, 45282-45288 (2001).
    • (2001) J. Biol. Chem , vol.276 , pp. 45282-45288
    • Loven, M.A.1    Likhite, V.S.2    Choi, I.3    Nardulli, A.M.4
  • 34
    • 0036185782 scopus 로고    scopus 로고
    • Allosteric regulation of estrogen receptor structure, function, and coactivator recruitment by different estrogen response elements
    • Hall, J.M., McDonnell, D.P. & Korach, K.S. Allosteric regulation of estrogen receptor structure, function, and coactivator recruitment by different estrogen response elements. Mol. Endocrinol. 16, 469-486 (2002).
    • (2002) Mol. Endocrinol , vol.16 , pp. 469-486
    • Hall, J.M.1    McDonnell, D.P.2    Korach, K.S.3
  • 35
    • 33644996796 scopus 로고    scopus 로고
    • Novel arylpyrazole compounds selectively modulate glucocorticoid receptor regulatory activity
    • Wang, J.C. et al. Novel arylpyrazole compounds selectively modulate glucocorticoid receptor regulatory activity. Genes Dev. 20, 689-699 (2006).
    • (2006) Genes Dev , vol.20 , pp. 689-699
    • Wang, J.C.1
  • 36
    • 0141963219 scopus 로고    scopus 로고
    • Full-length estrogen receptor α and its ligand-binding domain adopt different conformations upon binding ligand
    • Bapat, A.R. & Frail, D.E. Full-length estrogen receptor α and its ligand-binding domain adopt different conformations upon binding ligand. J. Steroid Biochem. Mol. Biol. 86, 143-149 (2003).
    • (2003) J. Steroid Biochem. Mol. Biol , vol.86 , pp. 143-149
    • Bapat, A.R.1    Frail, D.E.2
  • 37
    • 14844353602 scopus 로고    scopus 로고
    • Delineation of a unique protein-protein interaction site on the surface of the estrogen receptor
    • Kong, E.H. et al. Delineation of a unique protein-protein interaction site on the surface of the estrogen receptor. Proc. Natl. Acad. Sci. USA 102, 3593-3598 (2005).
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 3593-3598
    • Kong, E.H.1
  • 38
    • 56749130032 scopus 로고    scopus 로고
    • Structure of the intact PPAR-γ-RXR-nuclear receptor complex on DNA
    • Chandra, V. et al. Structure of the intact PPAR-γ-RXR-nuclear receptor complex on DNA. Nature 456, 350-356 (2008).
    • (2008) Nature , vol.456 , pp. 350-356
    • Chandra, V.1
  • 39
    • 79955581636 scopus 로고    scopus 로고
    • Common architecture of nuclear receptor heterodimers on DNA direct repeat elements with different spacings
    • Rochel, N. et al. Common architecture of nuclear receptor heterodimers on DNA direct repeat elements with different spacings. Nat. Struct. Mol. Biol. 18, 564-570 (2011).
    • (2011) Nat. Struct. Mol. Biol , vol.18 , pp. 564-570
    • Rochel, N.1
  • 40
    • 1942425955 scopus 로고    scopus 로고
    • Interaction of estrogen receptor α with 3-methyladenine DNA glycosylase modulates transcription and DNA repair
    • Likhite, V.S., Cass, E.I., Anderson, S.D., Yates, J.R. & Nardulli, A.M. Interaction of estrogen receptor α with 3-methyladenine DNA glycosylase modulates transcription and DNA repair. J. Biol. Chem. 279, 16875-16882 (2004).
    • (2004) J. Biol. Chem , vol.279 , pp. 16875-16882
    • Likhite, V.S.1    Cass, E.I.2    Anderson, S.D.3    Yates, J.R.4    Nardulli, A.M.5
  • 41
    • 84857145742 scopus 로고    scopus 로고
    • The nuclear receptor signalling scaffold: Insights from full-length structures
    • Nwachukwu, J.C. & Nettles, K.W. The nuclear receptor signalling scaffold: insights from full-length structures. EMBO J. 31, 251-253 (2012).
    • (2012) EMBO J. , vol.31 , pp. 251-253
    • Nwachukwu, J.C.1    Nettles, K.W.2
  • 43
    • 82355163442 scopus 로고    scopus 로고
    • Minireview: Recent advances in extranuclear steroid receptor actions
    • Hammes, S.R. & Levin, E.R. Minireview: recent advances in extranuclear steroid receptor actions. Endocrinology 152, 4489-4495 (2011).
    • (2011) Endocrinology , vol.152 , pp. 4489-4495
    • Hammes, S.R.1    Levin, E.R.2
  • 44
    • 84867665597 scopus 로고    scopus 로고
    • The orphan nuclear receptor Nur77 regulates LKB1 localization and activates AMPK
    • Zhan, Y.Y. et al. The orphan nuclear receptor Nur77 regulates LKB1 localization and activates AMPK. Nat. Chem. Biol. 8, 807-904 (2012).
    • (2012) Nat. Chem. Biol , vol.8 , pp. 807-904
    • Zhan, Y.Y.1
  • 45
    • 84861528159 scopus 로고    scopus 로고
    • Inhibition of β-catenin signaling by nongenomic action of orphan nuclear receptor Nur77
    • Sun, Z. et al. Inhibition of β-catenin signaling by nongenomic action of orphan nuclear receptor Nur77. Oncogene 31, 2653-2667 (2012).
    • (2012) Oncogene , vol.31 , pp. 2653-2667
    • Sun, Z.1
  • 46
    • 84879122903 scopus 로고    scopus 로고
    • National Research Council (U.S.). (eds. Connelly, T. & Sharp, P.) 12 (National Academies Press, Washington, D.C.)
    • National Research Council (U.S.). A New Biology for the 21st Century (eds. Connelly, T. & Sharp, P.) 12 (National Academies Press, Washington, D.C., 2009).
    • (2009) A New Biology for the 21st Century
  • 47
    • 76449098262 scopus 로고    scopus 로고
    • PHENIX: A comprehensive Python-based system for macromolecular structure solution
    • Adams, P.D. et al. PHENIX: a comprehensive Python-based system for macromolecular structure solution. Acta Crystallogr. D Biol. Crystallogr. 66, 213-221 (2010).
    • (2010) Acta Crystallogr. D Biol. Crystallogr , vol.66 , pp. 213-221
    • Adams, P.D.1
  • 48
    • 7544226311 scopus 로고    scopus 로고
    • PRODRG: A tool for high-throughput crystallography of protein-ligand complexes
    • Schüttelkopf, A.W. & van Aalten, D.M. PRODRG: a tool for high-throughput crystallography of protein-ligand complexes. Acta Crystallogr. D Biol. Crystallogr. 60, 1355-1363 (2004).
    • (2004) Acta Crystallogr. D Biol. Crystallogr , vol.60 , pp. 1355-1363
    • Schüttelkopf, A.W.1    Van Aalten, D.M.2
  • 49


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