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Volumn 66, Issue 1, 2006, Pages 543-553

Interplay between two hormone-independent activation domains in the androgen receptor

Author keywords

[No Author keywords available]

Indexed keywords

ANDROGEN RECEPTOR; ARGININE; LYSINE; PROTEIN P160; TAU PROTEIN; TAU PROTEIN 1; TAU PROTEIN 2; UNCLASSIFIED DRUG;

EID: 31544451068     PISSN: 00085472     EISSN: None     Source Type: Journal    
DOI: 10.1158/0008-5472.CAN-05-2389     Document Type: Article
Times cited : (81)

References (37)
  • 2
    • 4944255650 scopus 로고    scopus 로고
    • Molecular pathology of prostate cancer: The key to identifying new biomarkers of disease
    • Foley R, Hollywood D, Lawler M. Molecular pathology of prostate cancer: the key to identifying new biomarkers of disease. Endocr Relat Cancer 2004;11:477-88.
    • (2004) Endocr Relat Cancer , vol.11 , pp. 477-488
    • Foley, R.1    Hollywood, D.2    Lawler, M.3
  • 3
    • 2342558431 scopus 로고    scopus 로고
    • Androgen receptor in prostate cancer
    • Heinlein CA, Chang C. Androgen receptor in prostate cancer. Endocr Rev 2004;25:276-308.
    • (2004) Endocr Rev , vol.25 , pp. 276-308
    • Heinlein, C.A.1    Chang, C.2
  • 4
    • 4944246790 scopus 로고    scopus 로고
    • Targeting the androgen receptor: Improving outcomes for castration-resistant prostate cancer
    • Scher HI, Buchanan G, Gerald W, Butler LM, Tilley WD. Targeting the androgen receptor: improving outcomes for castration-resistant prostate cancer. Endocr Relat Cancer 2004;11:459-76.
    • (2004) Endocr Relat Cancer , vol.11 , pp. 459-476
    • Scher, H.I.1    Buchanan, G.2    Gerald, W.3    Butler, L.M.4    Tilley, W.D.5
  • 5
    • 4944235914 scopus 로고    scopus 로고
    • Symposium on androgen action in prostate cancer
    • Tindall D, Horne FM, Hruszkewycz A, et al. Symposium on androgen action in prostate cancer. Cancer Res 2004;64:7178-80.
    • (2004) Cancer Res , vol.64 , pp. 7178-7180
    • Tindall, D.1    Horne, F.M.2    Hruszkewycz, A.3
  • 7
    • 0035815749 scopus 로고    scopus 로고
    • Hormone status selects for spontaneous somatic androgen receptor variants that demonstrate specific ligand and cofactor dependent activities in autochthonous prostate cancer
    • Han G, Foster BA, Mistry S, et al. Hormone status selects for spontaneous somatic androgen receptor variants that demonstrate specific ligand and cofactor dependent activities in autochthonous prostate cancer. J Biol Chem 2001;276:11204-13.
    • (2001) J Biol Chem , vol.276 , pp. 11204-11213
    • Han, G.1    Foster, B.A.2    Mistry, S.3
  • 8
    • 0030986236 scopus 로고    scopus 로고
    • A signature motif in transcriptional co-activators mediates binding to nuclear receptors
    • Heery DM, Kalkhoven E, Hoare S, Parker MG. A signature motif in transcriptional co-activators mediates binding to nuclear receptors. Nature 1997;387:733-6.
    • (1997) Nature , vol.387 , pp. 733-736
    • Heery, D.M.1    Kalkhoven, E.2    Hoare, S.3    Parker, M.G.4
  • 9
    • 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, Rombauts W, Peeters B. The androgen receptor amino-terminal domain plays a key role in p160 coactivator-stimulated gene transcription. Mol Cell Biol 1999;19:6085-97.
    • (1999) Mol Cell Biol , vol.19 , pp. 6085-6097
    • Alen, P.1    Claessens, F.2    Verhoeven, G.3    Rombauts, W.4    Peeters, B.5
  • 10
    • 0033512783 scopus 로고    scopus 로고
    • The AF1 and AF2 domains of the androgen receptor interact with distinct regions of SRC1
    • Bevan CL, Hoare S, Claessens F, Heery DM, Parker MG. The AF1 and AF2 domains of the androgen receptor interact with distinct regions of SRC1. Mol Cell Biol 1999;19:8383-92.
    • (1999) Mol Cell Biol , vol.19 , pp. 8383-8392
    • Bevan, C.L.1    Hoare, S.2    Claessens, F.3    Heery, D.M.4    Parker, M.G.5
  • 11
    • 0346826295 scopus 로고    scopus 로고
    • Characterization of the two coactivator-interacting surfaces of the androgen receptor and their relative role in transcriptional control
    • Christiaens V, Bevan CL, Callewaert L, et al. Characterization of the two coactivator-interacting surfaces of the androgen receptor and their relative role in transcriptional control. J Biol Chem 2002;277: 49230-7.
    • (2002) J Biol Chem , vol.277 , pp. 49230-49237
    • Christiaens, V.1    Bevan, C.L.2    Callewaert, L.3
  • 12
    • 0033978514 scopus 로고    scopus 로고
    • Inhibition of p160-mediated coactivation with increasing androgen receptor polyglutamine length
    • Irvine RA, Ma H, Yu MC, Ross RK, Stallcup MR, Coetzee GA. Inhibition of p160-mediated coactivation with increasing androgen receptor polyglutamine length. Hum Mol Genet 2000;9:267-74.
    • (2000) Hum Mol Genet , vol.9 , pp. 267-274
    • Irvine, R.A.1    Ma, H.2    Yu, M.C.3    Ross, R.K.4    Stallcup, M.R.5    Coetzee, G.A.6
  • 13
    • 0030669765 scopus 로고    scopus 로고
    • Interaction between the amino- and carboxyl-terminal regions of the rat androgen receptor modulates transcriptional activity and is influenced by nuclear receptor coactivators
    • Ikonen T, Palvimo JJ, Jänne OA. Interaction between the amino- and carboxyl-terminal regions of the rat androgen receptor modulates transcriptional activity and is influenced by nuclear receptor coactivators. J Biol Chem 1997;272:29821-8.
    • (1997) J Biol Chem , vol.272 , pp. 29821-29828
    • Ikonen, T.1    Palvimo, J.J.2    Jänne, O.A.3
  • 14
    • 18744385207 scopus 로고    scopus 로고
    • Amino acids 3-13 and amino acids in and flanking the 23FxxLF27 motif modulate the interaction between the N-terminal and ligand-binding domain of the androgen receptor
    • Steketee K, Berrevoets CA, Dubbink HJ, et al. Amino acids 3-13 and amino acids in and flanking the 23FxxLF27 motif modulate the interaction between the N-terminal and ligand-binding domain of the androgen receptor. Eur J Biochem 2002;269:5780-91.
    • (2002) Eur J Biochem , vol.269 , pp. 5780-5791
    • Steketee, K.1    Berrevoets, C.A.2    Dubbink, H.J.3
  • 15
    • 0037424344 scopus 로고    scopus 로고
    • Dual function of an amino-terminal amphipatic helix in androgen receptor-mediated transactivation through specific and nonspecific response elements
    • Callewaert L, Verrijdt G, Christiaens V, Haelens A, Claessens F. Dual function of an amino-terminal amphipatic helix in androgen receptor-mediated transactivation through specific and nonspecific response elements. J Biol Chem 2003;278:8212-8.
    • (2003) J Biol Chem , vol.278 , pp. 8212-8218
    • Callewaert, L.1    Verrijdt, G.2    Christiaens, V.3    Haelens, A.4    Claessens, F.5
  • 16
    • 8344226282 scopus 로고    scopus 로고
    • Structural basis for androgen receptor interdomain and coactivator interactions suggests a transition in nuclear receptor activation function dominance
    • He B, Gampe RT, Jr, Kole AJ, et al. Structural basis for androgen receptor interdomain and coactivator interactions suggests a transition in nuclear receptor activation function dominance. Mol Cell 2004;16:425-38.
    • (2004) Mol Cell , vol.16 , pp. 425-438
    • He, B.1    Gampe Jr., R.T.2    Kole, A.J.3
  • 17
    • 0036218706 scopus 로고    scopus 로고
    • Evaluation of ligand-dependent changes in AR structure using peptide probes
    • Chang CY, McDonnell DP. Evaluation of ligand-dependent changes in AR structure using peptide probes. Mol Endocrinol 2002;16:647-60.
    • (2002) Mol Endocrinol , vol.16 , pp. 647-660
    • Chang, C.Y.1    McDonnell, D.P.2
  • 18
    • 0028904382 scopus 로고
    • Identification of two transcription activation units in the N-terminal domain of the human androgen receptor
    • Jenster G, van der Korput HA, Trapman J, Brinkmann AO. Identification of two transcription activation units in the N-terminal domain of the human androgen receptor. J Biol Chem 1995;270:7341-6.
    • (1995) J Biol Chem , vol.270 , pp. 7341-7346
    • Jenster, G.1    Van Der Korput, H.A.2    Trapman, J.3    Brinkmann, A.O.4
  • 19
    • 0029915052 scopus 로고    scopus 로고
    • Mutations in the androgen receptor gene are associated with progression of human prostate cancer to androgen independence
    • Tilley WD, Buchanan G, Hickey TE, Bentel JM. Mutations in the androgen receptor gene are associated with progression of human prostate cancer to androgen independence. Clin Cancer Res 1996;2;277-85.
    • (1996) Clin Cancer Res , vol.2 , pp. 277-285
    • Tilley, W.D.1    Buchanan, G.2    Hickey, T.E.3    Bentel, J.M.4
  • 20
    • 0037263134 scopus 로고    scopus 로고
    • DNA recognition by the androgen receptor: Evidence for an alternative DNA-dependent dimerization, and an active role of sequences flanking the response element on transactivation
    • Haelens A, Verrijdt G, Callewaert L, et al. DNA recognition by the androgen receptor: evidence for an alternative DNA-dependent dimerization, and an active role of sequences flanking the response element on transactivation. Biochem J 2003;369:141-51.
    • (2003) Biochem J , vol.369 , pp. 141-151
    • Haelens, A.1    Verrijdt, G.2    Callewaert, L.3
  • 21
    • 0036177576 scopus 로고    scopus 로고
    • Comparative analysis of the influence of the high-mobility group box 1 protein on DNA binding and transcriptional activation by the androgen, glucocorticoid, progesterone and mineralocorticoid receptors
    • Verrijdt G, Haelens A, Schoenmakers E, Rombauts W, Claessens F. Comparative analysis of the influence of the high-mobility group box 1 protein on DNA binding and transcriptional activation by the androgen, glucocorticoid, progesterone and mineralocorticoid receptors. Biochem J 2002;361:97-103.
    • (2002) Biochem J , vol.361 , pp. 97-103
    • Verrijdt, G.1    Haelens, A.2    Schoenmakers, E.3    Rombauts, W.4    Claessens, F.5
  • 22
    • 0034697359 scopus 로고    scopus 로고
    • Change of specificity mutations in androgen-selective enhancers. Evidence for a role of differential DNA binding by the androgen receptor
    • Verrijdt G, Schoenmakers E, Haelens A, et al. Change of specificity mutations in androgen-selective enhancers. Evidence for a role of differential DNA binding by the androgen receptor. J Biol Chem 2000;275: 12298-305.
    • (2000) J Biol Chem , vol.275 , pp. 12298-12305
    • Verrijdt, G.1    Schoenmakers, E.2    Haelens, A.3
  • 23
    • 0025957233 scopus 로고
    • Transcriptional activation and nuclear targeting signals of the human androgen receptor
    • Simental JA, Sar M, Lane MV, French FS, Wilson EM. Transcriptional activation and nuclear targeting signals of the human androgen receptor. J Biol Chem 1991;266: 510-8.
    • (1991) J Biol Chem , vol.266 , pp. 510-518
    • Simental, J.A.1    Sar, M.2    Lane, M.V.3    French, F.S.4    Wilson, E.M.5
  • 24
    • 0027482359 scopus 로고
    • Dominant negative regulation of trans-activation by the rat androgen receptor: Roles of the N-terminal domain and heterodimer formation
    • Palvimo JJ, Kallio PJ, Ikonen T, Mehto M, Jänne OA. Dominant negative regulation of trans-activation by the rat androgen receptor: roles of the N-terminal domain and heterodimer formation. Mol Endocrinol 1993;7: 1399-407.
    • (1993) Mol Endocrinol , vol.7 , pp. 1399-1407
    • Palvimo, J.J.1    Kallio, P.J.2    Ikonen, T.3    Mehto, M.4    Jänne, O.A.5
  • 25
    • 0028292958 scopus 로고
    • Delineation of a small region within the major transactivation domain of the human glucocorticoid receptor that mediates transactivation of gene expression
    • Dahlman-Wright K, Almlof T, McEwan IJ, Gustafsson JA, Wright AP. Delineation of a small region within the major transactivation domain of the human glucocorticoid receptor that mediates transactivation of gene expression. Proc Natl Acad Sci U S A 1994;91:1619-23.
    • (1994) Proc Natl Acad Sci U S A , vol.91 , pp. 1619-1623
    • Dahlman-Wright, K.1    Almlof, T.2    McEwan, I.J.3    Gustafsson, J.A.4    Wright, A.P.5
  • 26
    • 0040784176 scopus 로고    scopus 로고
    • Architectural principles for the structure and function of the glucocorticoid receptor tau 1 core activation domain
    • Wärnmark A, Gustafsson JA, Wright AP. Architectural principles for the structure and function of the glucocorticoid receptor tau 1 core activation domain. J Biol Chem 2000;275:15014-8.
    • (2000) J Biol Chem , vol.275 , pp. 15014-15018
    • Wärnmark, A.1    Gustafsson, J.A.2    Wright, A.P.3
  • 27
    • 0029914188 scopus 로고    scopus 로고
    • Delineation of two distinct type 1 activation functions in the androgen receptor amino-terminal domain
    • Chamberlain NU Whitacre DC, Miesfeld RL. Delineation of two distinct type 1 activation functions in the androgen receptor amino-terminal domain. J Biol Chem 1996;271:26772-8.
    • (1996) J Biol Chem , vol.271 , pp. 26772-26778
    • Chamberlain, N.U.1    Whitacre, D.C.2    Miesfeld, R.L.3
  • 28
    • 0037205522 scopus 로고    scopus 로고
    • Conformational analysis of the androgen receptor amino-terminal domain involved in transactivation. Influence of structure-stabilizing solutes and protein-protein interactions
    • Reid J, Kelly SM, Watt K, Price NC, McEwan IJ. Conformational analysis of the androgen receptor amino-terminal domain involved in transactivation. Influence of structure-stabilizing solutes and protein-protein interactions. J Biol Chem 2002;277: 20079-86.
    • (2002) J Biol Chem , vol.277 , pp. 20079-20086
    • Reid, J.1    Kelly, S.M.2    Watt, K.3    Price, N.C.4    McEwan, I.J.5
  • 29
    • 2542487192 scopus 로고    scopus 로고
    • Differential effect of small ubiquitin-like modifier [SUMO]-ylation of the androgen receptor in the control of cooperativity on selective versus canonical response elements
    • Callewaert L, Verrijdt G, Haelens A, Claessens F. Differential effect of small ubiquitin-like modifier [SUMO]-ylation of the androgen receptor in the control of cooperativity on selective versus canonical response elements. Mol Endocrinol 2004;18:1438-49.
    • (2004) Mol Endocrinol , vol.18 , pp. 1438-1449
    • Callewaert, L.1    Verrijdt, G.2    Haelens, A.3    Claessens, F.4
  • 30
    • 0033646066 scopus 로고    scopus 로고
    • Function of N-terminal transactivation domain of the estrogen receptor requires a potential α-helical structure and is negatively regulated by the a domain
    • Metivier R, Petit FG, Valotaire Y, Pakdel F. Function of N-terminal transactivation domain of the estrogen receptor requires a potential α-helical structure and is negatively regulated by the A domain. Mol Endocrinol 2000;14:1849-71.
    • (2000) Mol Endocrinol , vol.14 , pp. 1849-1871
    • Metivier, R.1    Petit, F.G.2    Valotaire, Y.3    Pakdel, F.4
  • 31
    • 0035955734 scopus 로고    scopus 로고
    • Mapping the unique activation function 3 in the progesterone B-receptor upstream segment. Two LXXLL motifs and a tryptophan residue are required for activity
    • Tung L, Shen T, Abel MG, et al. Mapping the unique activation function 3 in the progesterone B-receptor upstream segment. Two LXXLL motifs and a tryptophan residue are required for activity. J Biol Chem 2002;276: 39843-51.
    • (2002) J Biol Chem , vol.276 , pp. 39843-39851
    • Tung, L.1    Shen, T.2    Abel, M.G.3
  • 32
    • 12844274300 scopus 로고    scopus 로고
    • Mutation of the androgen receptor causes oncogenic transformation of the prostate
    • Han G, Buchanan G, Ittmann M, et al Mutation of the androgen receptor causes oncogenic transformation of the prostate. Proc Natl Acad Sci U S A 2005;102:1151-6.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 1151-1156
    • Han, G.1    Buchanan, G.2    Ittmann, M.3
  • 33
    • 0032230283 scopus 로고    scopus 로고
    • Functional interactions of the AF-2 activation domain core region of the human androgen receptor with the amino-terminal domain and with the transcriptional coactivator TIF2 [transcriptional intermediary factor2]
    • Berrevoets CA, Doesburg P, Steketee K, Trapman J, Brinkmann AO. Functional interactions of the AF-2 activation domain core region of the human androgen receptor with the amino-terminal domain and with the transcriptional coactivator TIF2 [transcriptional intermediary factor2]. Mol Endocrinol 1998;12:1172-83.
    • (1998) Mol Endocrinol , vol.12 , pp. 1172-1183
    • Berrevoets, C.A.1    Doesburg, P.2    Steketee, K.3    Trapman, J.4    Brinkmann, A.O.5
  • 34
    • 3042540196 scopus 로고    scopus 로고
    • Molecular mechanisms of androgen receptor-mediated gene regulation: Structure-function analysis of the AF-1 domain
    • McEwan IJ. Molecular mechanisms of androgen receptor-mediated gene regulation: structure-function analysis of the AF-1 domain. Endocr Relat Cancer 2004; 11:281-93.
    • (2004) Endocr Relat Cancer , vol.11 , pp. 281-293
    • McEwan, I.J.1
  • 35
    • 0034993267 scopus 로고    scopus 로고
    • Selective DNA binding by the androgen receptor as a mechanism for hormone-specific gene regulation
    • Claessens F, Verrijdt G, Schoenmakers E, et al. Selective DNA binding by the androgen receptor as a mechanism for hormone-specific gene regulation. J Steroid Biochem Mol Biol 2001;76:23-30.
    • (2001) J Steroid Biochem Mol Biol , vol.76 , pp. 23-30
    • Claessens, F.1    Verrijdt, G.2    Schoenmakers, E.3
  • 36
    • 18044371228 scopus 로고    scopus 로고
    • Androgen receptor-cofactor interactions as targets for new drug discovery
    • Chang CY, McDonnell DP. Androgen receptor-cofactor interactions as targets for new drug discovery. Trends Pharmacol Sci 2005;26:225-8.
    • (2005) Trends Pharmacol Sci , vol.26 , pp. 225-228
    • Chang, C.Y.1    McDonnell, D.P.2
  • 37
    • 0031594713 scopus 로고    scopus 로고
    • Intermolecular NH2-/carboxyl-terminal interactions in androgen receptor dimerization revealed by mutations that cause androgen insensitivity
    • Langley E, Kemppainen JA, Wilson EM. Intermolecular NH2-/carboxyl- terminal interactions in androgen receptor dimerization revealed by mutations that cause androgen insensitivity. J Biol Chem 1998;273:92-101.
    • (1998) J Biol Chem , vol.273 , pp. 92-101
    • Langley, E.1    Kemppainen, J.A.2    Wilson, E.M.3


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