메뉴 건너뛰기




Volumn 21, Issue 3, 2007, Pages 403-414

The role of cofactors in sex steroid action

Author keywords

androgen insensitivity; androgen receptor; cofactor; transcription

Indexed keywords

ANDROGEN RECEPTOR; CELL RECEPTOR; HISTONE; SEX HORMONE; STEROID RECEPTOR; TRANSCRIPTION FACTOR;

EID: 34548590196     PISSN: 1521690X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.beem.2007.07.002     Document Type: Review
Times cited : (11)

References (48)
  • 2
    • 0037154974 scopus 로고    scopus 로고
    • Combinatorial control of gene expression by nuclear receptors and coregulators
    • McKenna N.J., and O'Malley B.W. Combinatorial control of gene expression by nuclear receptors and coregulators. Cell 108 (2002) 465-474
    • (2002) Cell , vol.108 , pp. 465-474
    • McKenna, N.J.1    O'Malley, B.W.2
  • 3
  • 4
    • 34249667205 scopus 로고    scopus 로고
    • Natural disordered sequences in the amino terminal domain of nuclear receptors: lessons from the androgen and glucocorticoid receptors
    • McEwan I.J., Lavery D., Fischer K., et al. Natural disordered sequences in the amino terminal domain of nuclear receptors: lessons from the androgen and glucocorticoid receptors. Nuclear Receptor Signaling 5 (2007) e001
    • (2007) Nuclear Receptor Signaling , vol.5
    • McEwan, I.J.1    Lavery, D.2    Fischer, K.3
  • 5
    • 1542573353 scopus 로고    scopus 로고
    • Structure-activity relationship of nuclear receptor-ligand interactions
    • Greschik H., and Moras D. Structure-activity relationship of nuclear receptor-ligand interactions. Current Topics in Medicinal Chemistry 3 (2003) 1573-1599
    • (2003) Current Topics in Medicinal Chemistry , vol.3 , pp. 1573-1599
    • Greschik, H.1    Moras, D.2
  • 6
    • 0029069878 scopus 로고
    • Androgen receptor defects: historical, clinical, and molecular perspectives
    • Quigley C.A., De Bellis A., Marschke K.B., et al. Androgen receptor defects: historical, clinical, and molecular perspectives. Endocrine Reviews 16 (1995) 271-321
    • (1995) Endocrine Reviews , vol.16 , pp. 271-321
    • Quigley, C.A.1    De Bellis, A.2    Marschke, K.B.3
  • 9
    • 0034714276 scopus 로고    scopus 로고
    • Structural evidence for ligand specificity in the binding domain of the human androgen receptor, implications for pathogenic mutations
    • Matias P.M., Donner P., Coelho R., et al. Structural evidence for ligand specificity in the binding domain of the human androgen receptor, implications for pathogenic mutations. The Journal of Biological Chemistry 275 (2000) 26164-26171
    • (2000) The Journal of Biological Chemistry , vol.275 , pp. 26164-26171
    • Matias, P.M.1    Donner, P.2    Coelho, R.3
  • 10
    • 0035942197 scopus 로고    scopus 로고
    • Crystallographic structures of the ligand-binding domains of the androgen receptor and its T877A mutant complexed with the natural antagonist dihydrotestosterone
    • Sack J.S., Kish K.F., Wang C., et al. Crystallographic structures of the ligand-binding domains of the androgen receptor and its T877A mutant complexed with the natural antagonist dihydrotestosterone. Proceedings of the National Academy of Sciences of the United States of America 98 (2001) 4904-4909
    • (2001) Proceedings of the National Academy of Sciences of the United States of America , vol.98 , pp. 4904-4909
    • Sack, J.S.1    Kish, K.F.2    Wang, C.3
  • 11
    • 20044394709 scopus 로고    scopus 로고
    • The molecular mechanisms of coactivator utilization in ligand-dependent transactivation by the androgen receptor
    • Estebanez-Perpina, Moore J.M.R., Mar E., et al. The molecular mechanisms of coactivator utilization in ligand-dependent transactivation by the androgen receptor. The Journal of Biological Chemistry 280 (2005) 8060-8068
    • (2005) The Journal of Biological Chemistry , vol.280 , pp. 8060-8068
    • Estebanez-Perpina1    Moore, J.M.R.2    Mar, E.3
  • 12
    • 0031039480 scopus 로고    scopus 로고
    • Functional in vivo interaction between the amino-terminal, transactivation domain and the ligand binding domain of the androgen receptor
    • Doesburg P., Kuil C.W., Berrevoets C.A., et al. Functional in vivo interaction between the amino-terminal, transactivation domain and the ligand binding domain of the androgen receptor. Biochemistry 36 (1997) 1052-1064
    • (1997) Biochemistry , vol.36 , pp. 1052-1064
    • Doesburg, P.1    Kuil, C.W.2    Berrevoets, C.A.3
  • 13
    • 0034725648 scopus 로고    scopus 로고
    • FXXLF and WXXLF sequences mediate the NH2-terminal interaction with the ligand binding domain of the androgen receptor
    • He B., Kemppainen J.A., and Wilson E.M. FXXLF and WXXLF sequences mediate the NH2-terminal interaction with the ligand binding domain of the androgen receptor. The Journal of Biological Chemistry 275 (2000) 22986-22994
    • (2000) The Journal of Biological Chemistry , vol.275 , pp. 22986-22994
    • He, B.1    Kemppainen, J.A.2    Wilson, E.M.3
  • 15
    • 33847224474 scopus 로고    scopus 로고
    • Ligand-specific dynamics of the androgen receptor at its response element
    • Klokk T.I., Kurys P., Elbi C., et al. Ligand-specific dynamics of the androgen receptor at its response element. Molecular and Cellular Biology 27 (2007) 1823-1843
    • (2007) Molecular and Cellular Biology , vol.27 , pp. 1823-1843
    • Klokk, T.I.1    Kurys, P.2    Elbi, C.3
  • 16
    • 34247146786 scopus 로고    scopus 로고
    • Compartmentalization of androgen receptor protein-protein interactions in living cells
    • Van Royen M.E., Cunha S.M., Brink M.C., et al. Compartmentalization of androgen receptor protein-protein interactions in living cells. The Journal of Cell Biology 177 (2007) 63-72
    • (2007) The Journal of Cell Biology , vol.177 , pp. 63-72
    • Van Royen, M.E.1    Cunha, S.M.2    Brink, M.C.3
  • 17
    • 8344226282 scopus 로고    scopus 로고
    • Structural basis for androgen receptor interdomain interaction and coactivator interactions suggests a transition in nuclear activation function dominance
    • He B., Gampe R.T., Kole A.J., et al. Structural basis for androgen receptor interdomain interaction and coactivator interactions suggests a transition in nuclear activation function dominance. Molecular Cell 16 (2004) 425-438
    • (2004) Molecular Cell , vol.16 , pp. 425-438
    • He, B.1    Gampe, R.T.2    Kole, A.J.3
  • 18
    • 19344376991 scopus 로고    scopus 로고
    • Recognition and accommodation at the androgen receptor coactivator binding interface
    • Hur E., Pfaff S.J., Payne E.S., et al. Recognition and accommodation at the androgen receptor coactivator binding interface. PloS Biolology 2 (2004) e274
    • (2004) PloS Biolology , vol.2
    • Hur, E.1    Pfaff, S.J.2    Payne, E.S.3
  • 19
    • 34548560185 scopus 로고    scopus 로고
    • Li J, Zhang D, Fu J, et al. Structural and functional analysis of androgen receptor in chromatin. Molecular Endocrinology (in press), doi:10.1210/me.2006-0221 [Epub ahead of print].
  • 20
    • 0028809317 scopus 로고
    • Specificity of ligand-dependent androgen receptor stabilization: receptor domain interactions influence ligand dissociation and receptor stability
    • Zhou Z.X., Lane M.V., Kemppainen J.A., et al. Specificity of ligand-dependent androgen receptor stabilization: receptor domain interactions influence ligand dissociation and receptor stability. Molecular Endocrinology 9 (1995) 208-218
    • (1995) Molecular Endocrinology , vol.9 , pp. 208-218
    • Zhou, Z.X.1    Lane, M.V.2    Kemppainen, J.A.3
  • 21
    • 4544274492 scopus 로고    scopus 로고
    • Distinct recognition modes of FXXLF and LXXLL motifs by the androgen receptor
    • Dubbink H.J., Hersmus R., Verma C.S., et al. Distinct recognition modes of FXXLF and LXXLL motifs by the androgen receptor. Molecular Endocrinology 18 (2004) 2132-2150
    • (2004) Molecular Endocrinology , vol.18 , pp. 2132-2150
    • Dubbink, H.J.1    Hersmus, R.2    Verma, C.S.3
  • 22
    • 33646541668 scopus 로고    scopus 로고
    • Probing the functional link between androgen receptor coactivator and ligand binding sites in prostate cancer and androgen insensitivity
    • He B., Gampe R.T., Hnat A.T., et al. Probing the functional link between androgen receptor coactivator and ligand binding sites in prostate cancer and androgen insensitivity. The Journal of Biological Chemistry 281 (2006) 6648-6663
    • (2006) The Journal of Biological Chemistry , vol.281 , pp. 6648-6663
    • He, B.1    Gampe, R.T.2    Hnat, A.T.3
  • 23
    • 33744792310 scopus 로고    scopus 로고
    • Sensors and signals: a coactivator/corepressor/epigenetic code for integrating signal-dependent programs of transcriptional response
    • 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 & Development 20 (2006) 1405-1428
    • (2006) Genes & Development , vol.20 , pp. 1405-1428
    • Rosenfeld, M.G.1    Lunyak, V.V.2    Glass, C.K.3
  • 24
    • 33847076849 scopus 로고    scopus 로고
    • Chromatin modifications and their function
    • Kouzarides T. Chromatin modifications and their function. Cell 128 (2007) 693-705
    • (2007) Cell , vol.128 , pp. 693-705
    • Kouzarides, T.1
  • 25
    • 33847070442 scopus 로고    scopus 로고
    • The role of chromatin during transcription
    • Li B., Carey M., and Workman J.L. The role of chromatin during transcription. Cell 128 (2007) 707-719
    • (2007) Cell , vol.128 , pp. 707-719
    • Li, B.1    Carey, M.2    Workman, J.L.3
  • 26
    • 30344479480 scopus 로고    scopus 로고
    • Coregulators in nuclear estrogen receptor action
    • Hall J.M., and McDonnell D.P. Coregulators in nuclear estrogen receptor action. Molecular Interventions 6 (2005) 343-357
    • (2005) Molecular Interventions , vol.6 , pp. 343-357
    • Hall, J.M.1    McDonnell, D.P.2
  • 27
    • 29444461024 scopus 로고    scopus 로고
    • Changes in attitude, changes in latitude: nuclear receptors remodelling chromatin to regulate transcription
    • Chen J., Kinyamu H.K., and Archer T.K. Changes in attitude, changes in latitude: nuclear receptors remodelling chromatin to regulate transcription. Molecular Endocrinology 20 (2006) 1-13
    • (2006) Molecular Endocrinology , vol.20 , pp. 1-13
    • Chen, J.1    Kinyamu, H.K.2    Archer, T.K.3
  • 28
    • 18844451820 scopus 로고    scopus 로고
    • Mediator and the mechanism of transcriptional activation
    • Kornberg R.D. Mediator and the mechanism of transcriptional activation. Trends in Biochemical Sciences 30 (2005) 235-239
    • (2005) Trends in Biochemical Sciences , vol.30 , pp. 235-239
    • Kornberg, R.D.1
  • 29
    • 18844394569 scopus 로고    scopus 로고
    • Dynamic regulation of pol II transcription by the mammalian Mediator complex
    • Malik S., and Roeder R.G. Dynamic regulation of pol II transcription by the mammalian Mediator complex. Trends in Biochemical Sciences 30 (2005) 256-263
    • (2005) Trends in Biochemical Sciences , vol.30 , pp. 256-263
    • Malik, S.1    Roeder, R.G.2
  • 31
    • 0032784653 scopus 로고    scopus 로고
    • The androgen receptor amino-terminal domain plays a key role in p160 coactivator-stimulated gene transcription
    • Alen P., Claessens F., Verhoeven G., et al. The androgen receptor amino-terminal domain plays a key role in p160 coactivator-stimulated gene transcription. Molecular and Cellular Biology 19 (1999) 6085-6097
    • (1999) Molecular and Cellular Biology , vol.19 , pp. 6085-6097
    • Alen, P.1    Claessens, F.2    Verhoeven, G.3
  • 32
    • 33746639616 scopus 로고    scopus 로고
    • Androgen receptor ligand-binding domain interaction and nuclear receptor specificity of FXXLF and LXXLL motifs as determined by L/F swapping
    • Dubbink H.J., Hersmus R., Pike A.C.W., et al. Androgen receptor ligand-binding domain interaction and nuclear receptor specificity of FXXLF and LXXLL motifs as determined by L/F swapping. Molecular Endocrinology 20 (2006) 1742-1755
    • (2006) Molecular Endocrinology , vol.20 , pp. 1742-1755
    • Dubbink, H.J.1    Hersmus, R.2    Pike, A.C.W.3
  • 33
    • 0037155790 scopus 로고    scopus 로고
    • The FXXLF motif mediates androgen receptor-specific interactions with coregulators
    • He B., Minges J.T., Lee L.W., et al. The FXXLF motif mediates androgen receptor-specific interactions with coregulators. The Journal of Biological Chemistry 277 (2002) 10226-10235
    • (2002) The Journal of Biological Chemistry , vol.277 , pp. 10226-10235
    • He, B.1    Minges, J.T.2    Lee, L.W.3
  • 34
    • 33745838579 scopus 로고    scopus 로고
    • Novel FXXFF and FXXMF motifs in androgen receptor cofactors mediate high affinity and specific interactions with the ligand-binding domain
    • Van de Wijngaart D.J., Van Royen M.E., Hersmus R., et al. Novel FXXFF and FXXMF motifs in androgen receptor cofactors mediate high affinity and specific interactions with the ligand-binding domain. The Journal of Biological Chemistry 281 (2006) 19407-19416
    • (2006) The Journal of Biological Chemistry , vol.281 , pp. 19407-19416
    • Van de Wijngaart, D.J.1    Van Royen, M.E.2    Hersmus, R.3
  • 35
    • 13444304134 scopus 로고    scopus 로고
    • Melanoma antigen gene protein MAGE-11 regulates androgen receptor function by modulating the interdomain interaction
    • Bai S., He B., and Wilson E.M. Melanoma antigen gene protein MAGE-11 regulates androgen receptor function by modulating the interdomain interaction. Molecular and Cellular Biology 25 (2005) 1238-1257
    • (2005) Molecular and Cellular Biology , vol.25 , pp. 1238-1257
    • Bai, S.1    He, B.2    Wilson, E.M.3
  • 36
    • 0036219918 scopus 로고    scopus 로고
    • Androgen receptor (AR) coregulators: an overview
    • Heinlein C.A., and Chang C. Androgen receptor (AR) coregulators: an overview. Endocrine Reviews 23 (2002) 175-200
    • (2002) Endocrine Reviews , vol.23 , pp. 175-200
    • Heinlein, C.A.1    Chang, C.2
  • 37
    • 14844364364 scopus 로고    scopus 로고
    • BAF57 governs androgen receptor action and androgen-dependent proliferation through SWI/SNF
    • Link K.A., Burd C.J., Williams E., et al. BAF57 governs androgen receptor action and androgen-dependent proliferation through SWI/SNF. Molecular and Cellular Biology 25 (2005) 2200-2215
    • (2005) Molecular and Cellular Biology , vol.25 , pp. 2200-2215
    • Link, K.A.1    Burd, C.J.2    Williams, E.3
  • 38
    • 31544475671 scopus 로고    scopus 로고
    • Biochemical characterization of androgen receptor-interacting protein 4
    • Domanskyi A., Virtanen K.T., Palvimo J.J., et al. Biochemical characterization of androgen receptor-interacting protein 4. Biochemical Journal 393 (2006) 789-795
    • (2006) Biochemical Journal , vol.393 , pp. 789-795
    • Domanskyi, A.1    Virtanen, K.T.2    Palvimo, J.J.3
  • 39
    • 0037044767 scopus 로고    scopus 로고
    • A coregulatory role for the TRAP-Mediator complex in androgen receptor-mediated gene expression
    • Wang Q., Sharma D., Ren Y., et al. A coregulatory role for the TRAP-Mediator complex in androgen receptor-mediated gene expression. The Journal of Biological Chemistry 277 (2002) 42852-42858
    • (2002) The Journal of Biological Chemistry , vol.277 , pp. 42852-42858
    • Wang, Q.1    Sharma, D.2    Ren, Y.3
  • 40
    • 0038514176 scopus 로고    scopus 로고
    • An extended LXXLL motif sequence determines the nuclear receptor binding specificity of TRAP220
    • Coulthart V.H., Matsuda S., and Heery D.M. An extended LXXLL motif sequence determines the nuclear receptor binding specificity of TRAP220. The Journal of Biological Chemistry 278 (2003) 10942-10951
    • (2003) The Journal of Biological Chemistry , vol.278 , pp. 10942-10951
    • Coulthart, V.H.1    Matsuda, S.2    Heery, D.M.3
  • 41
    • 0343415609 scopus 로고    scopus 로고
    • The glucocorticoid receptor: rapid exchange with regulatory sites
    • McNally J.G., Mueller W.G., Walker D., et al. The glucocorticoid receptor: rapid exchange with regulatory sites. Science 287 (2000) 1262-1265
    • (2000) Science , vol.287 , pp. 1262-1265
    • McNally, J.G.1    Mueller, W.G.2    Walker, D.3
  • 42
    • 1942454739 scopus 로고    scopus 로고
    • The androgen receptor ligand-binding domain stabilizes DNA binding in living cells
    • Farla P., Hersmus R., Geverts B., et al. The androgen receptor ligand-binding domain stabilizes DNA binding in living cells. Journal of Structural Biology 147 (2004) 50-61
    • (2004) Journal of Structural Biology , vol.147 , pp. 50-61
    • Farla, P.1    Hersmus, R.2    Geverts, B.3
  • 43
    • 0013537360 scopus 로고    scopus 로고
    • Dynamic behavior of transcription factors on a natural promoter in living cells
    • Becker M., Baumann C., John S., et al. Dynamic behavior of transcription factors on a natural promoter in living cells. EMBO Reports 3 (2002) 1188-1194
    • (2002) EMBO Reports , vol.3 , pp. 1188-1194
    • Becker, M.1    Baumann, C.2    John, S.3
  • 44
    • 33645820442 scopus 로고    scopus 로고
    • Transcription in four dimensions: Nuclear receptor-directed initiation of gene expression
    • Metivier R., Reid G., and Gannon F. Transcription in four dimensions: Nuclear receptor-directed initiation of gene expression. EMBO Reports 7 (2006) 1439-1446
    • (2006) EMBO Reports , vol.7 , pp. 1439-1446
    • Metivier, R.1    Reid, G.2    Gannon, F.3
  • 45
  • 46
    • 0029022770 scopus 로고
    • Rubinstein-Taybi syndrome caused by mutations in the transcriptional co-activator CBP
    • Petrij F., Giles R.H., Dauwerse H.G., et al. Rubinstein-Taybi syndrome caused by mutations in the transcriptional co-activator CBP. Nature 376 (1995) 348-351
    • (1995) Nature , vol.376 , pp. 348-351
    • Petrij, F.1    Giles, R.H.2    Dauwerse, H.G.3
  • 47
    • 1042290351 scopus 로고    scopus 로고
    • The SWI/SNF complex - chromatin and cancer
    • Roberts C.W.M., and Orkin S.H. The SWI/SNF complex - chromatin and cancer. Nature Reviews. Cancer 4 (2004) 133-142
    • (2004) Nature Reviews. Cancer , vol.4 , pp. 133-142
    • Roberts, C.W.M.1    Orkin, S.H.2
  • 48
    • 0030797902 scopus 로고    scopus 로고
    • AIB1, a steroid receptor coactivator amplified in breast and ovarian cancer
    • Anzick S.L., Kononen J., Walker R.L., et al. AIB1, a steroid receptor coactivator amplified in breast and ovarian cancer. Science 277 (1997) 965-968
    • (1997) Science , vol.277 , pp. 965-968
    • Anzick, S.L.1    Kononen, J.2    Walker, R.L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.