Abstract
The androgen receptor, like the other nuclear receptors, consists of three canonical domains: the aminoterminal domain (NTD), the DNA-binding domain (DBD) and the ligand-binding domain (LBD). The flexible hinge between the DBD and LBD can also be considered as a separate entity. Each of these domains has multiple functions. The NTD harbors two interdependent transactivation functions Tau-1 and Tau-5, two SUMOylation sites that seem to control cooperativity of the AR, and an 23FQNLF27 motif that interacts with high affinity with the ligand-binding domain. The DBD is involved in the correct interactions of the AR with its response elements, but it also contains a nuclear export signal as well as a nuclear translocation signal. The hinge region controls the interactions of the AR with selective AREs. It harbors an acetylation and a phosphorylation acceptor site, overlaps with the nuclear translocation signal, and seems involved in the control of the steady state of the AR. The LBD binds its natural agonists with high affinity; it interacts with heat-shock protein complexes when unbound and with a series of coregulators when bound by agonists. Many of these coregulators harbor motifs that resemble the 23FQNLF27-motif of the NTD.
Clearly, the domains of the AR do not function independently, but rather act in concert with each other and with other proteins during androgen activation of transcription. The overall activity of the AR as a transcription factor is codetermined by such communications, and also by the nature of the response element or enhancer it is binding to.
This is a preview of subscription content, log in via an institution to check access.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
References
Alen, P., Claessens, F., Verhoeven, G., Rombauts, W. and Peeters, B.1999. The androgen receptor amino-terminal domain plays a key role in p160 coactivator-stimulated gene transcription. Mol. Cell. Biol. 19:6085–6097.
Avila, D.M., Zoppi, S. and McPhaul, M.J.2001. The androgen receptor (AR) in syndromes of androgen insensitivity and in prostate cancer. J. Steroid Biochem. Mol. Biol. 76:135–142.
BaiS., He, B. and Wilson, E.M.2005Melanoma antigen gene protein MAGE-11 regulates androgen receptor function by modulating the interdomain interaction. Mol. Cell Biol.25:12380–1257.
Barbulescu, K., Geserick, C., Schüttke, I., Schleuning, W. and Haendler, B.2001. New androgen response elements in the murine pem promoter mediate selective transactivation. Mol. Endocrinol. 15:1803–1816.
Berrevoets, C.A., Doesburg, P., Steketee, K., Trapman, J. and Brinkmann, A.O.1998. 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. 12:1172–1183.
Bevan, C.L., Hoare, S., Claessens, F., Heery, D.M. and Parker, M.G.1999. The AF1 and AF2 domains of the androgen receptor interact with distinct regions of SRC1. Mol. Cell. Biol. 19:8383–8392.
Black, B.E., Holaska, J.M., Rastinejad, F. and Paschal, B.M.2001. DNA binding domains of diverse nuclear receptors function as nuclear export signals. Curr. Biol. 11:1749–1758.
Blok, L.J., de Ruiter, P.E. and Brinkmann, A.O.1996. Androgen receptor phosphorylation. Endocr. Res. 22:197–219.
Buchanan, G., Yang, M., Cheong, A., Harris, J.M., Irvine, R.A., Lambert, P.F., Moore, N.L., Raynor, M., Neufling, P.J., Coetzee, G.A. and Tilley, W.D.2004. Structural and functional consequences of glutamine tract variation in the androgen receptor. Hum. Mol. Genet.13:1677–1692.
Buchanan, G., Ricciardelli, C., Harris, J.M., Prescott, J., Yu, Z.C., Jia, L., Butler, L.M., Marshall, V.R., Scher, H.I., Gerald, W.L., Coetzee, G.A. and Tilley, W.D.2007. Control of androgen receptor signaling in prostate cancer by the cochaperone small glutamine-rich tetratricopeptide repeat containing proteinα. Cancer Res. 67:1–10.
Burd, C.J., Petre, C.E., Moghadam, H., Wilson, E.M. and Knudsen, K.E.2005. Cyclin D1 binding to the androgen receptor NH2-terminal domain inhibits activation function 2 association and reveals dual roles for AR corepression. Mol. Endocrinol. 19:607–620.
Callewaert, L., Christiaens, V., Haelens, A., Verrijdt, G., Verhoeven, G. and Claessens, F.2003. Implications of a polyglutamine tract in the function of the human androgen receptor. Biochem. Biophys. Res. Commun. 306:46–52.
Callewaert, L., Verrijdt, G., Haelens, A. and Claessens, F.2004. 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. 18:1438–1449.
Callewaert, L., Van Tilborgh, N. and Claessens, F.2006. Interplay between two hormone-independent activation domains in the androgen receptor. Cancer Res. 66:543–553.
Cato, A.C., Henderson, D. and Ponta, H.1987. The hormone response element of the mouse mammary tumour virus DNA mediates the progestin and androgen induction of transcription in the proviral long terminal repeat region. EMBO J. 6:363–368.
Celis, L., Claessens, F., Peeters, B., Heyns, W., Verhoeven, G. and Rombauts, W.1993. Proteins interacting with an androgen-responsive unit in the C3(1) gene intron. Mol. Cell. Endocrinol. 94:165–172.
Chamberlain, N.L., Whitacre, D.C. and Miesfeld, R.L.1996. Delineation of two distinct type 1 activation functions in the androgen receptor amino-terminal domain. J. Biol. Chem. 271:26772–26778.
Christiaens, V., Bevan, C.L., Callewaert, L., Haelens, A., Verrijdt, G., Rombauts, W. and Claessens, F.2002. Characterization of two co-activator interacting surfaces of the androgen receptor and their relative role in transcriptional control. J. Biol. Chem. 277:49230–49237.
Claessens, F. and Gewirth, D.2004. DNA recognition by nuclear receptors. Essays Biochem. 40:59–72.
Claessens, F., Celis, L., Peeters, B., Heyns, W., Verhoeven, G. and Rombauts, W.1989. Functional characterization of an androgen response element in the first intron of the C3(1) gene of prostatic binding protein. Biochem. Biophys. Res. Commun. 164:833–840.
Claessens, F., Rushmere, N.K., Davies, P., Celis, L., Peeters, B. and Rombauts, W.A.1990. Sequence-specific binding of androgen-receptor complexes to prostatic binding protein genes. Mol. Cell. Endocrinol. 74:203–212.
Claessens, F., Alen, P., Devos, A., Peeters, B., Verhoeven, G. and Rombauts, W.1996. The androgen-specific probasin response element 2 interacts differentially with androgen and glucocorticoid receptors. J. Biol. Chem. 271:19013–19016.
Dedhar, S., Rennie, P.S., Shago, M., Hagesteijn, C.Y., Yang, H., Filmus, J., Hawley, R.G., Bruchovsky, N., Cheng, H., Matusik, R.J. and Giguére, V.1994. Inhibition of nuclear hormone receptor activity by calreticulin. Nature367:480–483.
Dehm, S.M. and Tindall, D.J.2007. Androgen receptor structural and functional elements: role and regulation in prostate cancer. Mol. Endocrinol.21:2855–2863.
Dehm, S.M., Regan, K.M., Schmidt, L.J. and Tindall, D.J.2007. Selective role of an NH2terminal WxxLF motif for aberrant androgen receptor activation in androgen depletion independent prostate cancer cells. Cancer Res.67:10067–10077.
Denison, S.H., Sands, A. and Tindall, D.J.1989. A tyrosine aminotransferase glucocorticoid response element also mediates androgen enhancement of gene expression. Endocrinology124:1091–1093.
Doesburg, P., Kuil, C.W., Berrevoets, C.A., Steketee, K., Faber, P.W., Mulder, E., Brinkmann, A.O. and Trapman, J.1997. Functional in vivo interaction between the amino-terminal, transactivation domain and the ligand binding domain of the androgen receptor. Biochemistry36:1052–1064.
Fang, Y., Fliss, A.E., Robins, D.M. and Caplan, A.J.1996. Hsp90 regulates androgen receptor hormone binding affinity in vivo. J. Biol. Chem. 271:28697–28702.
Faus, H. and Haendler, B.2007. Post-translational modifications of steroid receptors. Biomed. Pharmacother. 60:520–528.
Freiman, R.N. and Tjian, R.2003. Regulating the regulators: lysine modifications make their mark. Cell112:11–17.
Fu, M., Wang, C., Reutens, A.T., Wang, J., Angeletti, R.H., Siconolfi-Baez, L., Ogryzko, V., Avantaggiati, M.L. and Pestell, R.G.2000. p300 and p300/cAMP-response element-binding protein-associated factor acetylate the androgen receptor at sites governing hormone-dependent transactivation. J. Biol. Chem. 275:20853–50860.
Fu, M., Wang, C., Wang, J., Zhang, X., Sakamaki, T., Yeung, Y.G., Chang, C., Hopp, T., Fuqua, S.A., Jaffray, E., Hay, R.T., Palvimo, J.J., Jänne, O.A. and Pestell, R.G.2002. Androgen receptor acetylation governs trans activation and MEKK1-induced apoptosis without affecting in vitro sumoylation and trans-repression function. Mol. Cell. Biol.22:3373–3388.
Gaughan, L., Logan, I.R., Cook, S., Neal, D.E. and Robson, C.N.2002. Tip60 and histone deacetylase 1 regulate androgen receptor activity through changes to the acetylation status of the receptor. J. Biol. Chem. 277:25904–25913.
Gelmann, E.P.2002. Molecular biology of the androgen receptor. J. Clin. Oncol. 20:3001–3015.
Gobinet, J., Poujol, N. and Sultan, C.2002. Molecular action of androgens. Mol. Cell. Endocrinol. 198:15–24.
Gottlieb, B., Beitel, L.K., Lumbroso, R., Pinsky, L. and Trifiro, M.1999. Update of the androgen receptor gene mutations database. Hum. Mutat. 14:103–114.
Greenland, K.J. and Zajac, J.D.2004. Kennedy's disease: pathogenesis and clinical approaches. Intern. Med. J. 34:279–286.
Haelens, A., Verrijdt, G., Callewaert, L., Chrsitiaens, V., Schauwaers, K., Peeters, B., Rombauts, W. and Claessens, F.2003. 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. 369:141–151.
Haelens, A., Tanner, T., Denayer, S., Callewaert, L. and Claessens, F.2007. The hinge region regulates DNA binding, nuclear translocation, and transactivation of the androgen receptor. Cancer Res. 67:4514–4523.
Ham, J., Thomson, A., Needham, M., Webb, P. and Parker, M.G.1988. Characterization of response elements for androgens, glucocorticoids and progestins in mouse mammary tumour virus. Nucleic Acids Res. 16:5263–5276.
He, B., Kemppainen, J.A., Voegel, J.J., Gronemeyer, H. and Wilson, E.M.1999. Activation function 2 in the human androgen receptor ligand binding domain mediates interdomain communication with the NH(2)-terminal domain. J. Biol. Chem. 274:37219–37225.
He, B., Bai, S., Hnat, A.T., Kalman, R.I., Minges, J.T., Patterson, C. and Wilson, E.M.2004a. An androgen receptor NH2-terminal conserved motif interacts with the COOH terminus of the Hsp70-interacting protein (CHIP). J. Biol. Chem.279:30643–30653.
He, B., Gampe, R.T., Kole, A.J., Mnat, A.T., Stanley, T.B., An, G., Stewart, E.L., Kalman, R.I., Minges, J.T. and Wilson, E.M.2004b. Structural basis for androgen receptor interdomain and coactivator interactions suggests a transition in nuclear receptor activation function dominance. Mol. Cell16:425–438.
Heemers, H., Verrijdt, G., Organe, S., Claessens, F., Heyns, W., Verhoeven, G. and Swinnen, J.V.2004. Identification of an androgen response element in intron 8 of the sterol regulatory element-binding protein cleavage-activating protein gene allowing direct regulation by the androgen receptor. J. Biol. Chem. 279:30880–30887.
Heemers, H.V., Regan, K.M., Dehm, S.M. and Tindall, D.J.2007. Androgen induction of the androgen receptor coactivator four and a half LIM domain protein-2: evidence for a role for serum response factor in prostate cancer. Cancer Res. 67:10592–10599.
Heinlein, C.A. and Chang, C.2002. Androgen receptor (AR) coregulators: an overview. Endocr. Rev. 23:175–200.
Huang, Z.Q., Li, J., Sachs, L.M., Cole, P.A. and Wong, J.2003. A role for cofactor-cofactor and cofactor-histone interactions in targeting p300, SWI/SNF and Mediator for transcription. EMBO J. 22:2146–2155.
Iordanidou, P., Aggelidou, E., Demetriades, C. and Hadzopoulou-Cladaras, M.2005. Distinct amino acid residues may be involved in coactivator and ligand interactions in hepatocyte nuclear factor-4α. J. Biol. Chem. 280:21810–21819.
Irvine, R.A., Ma, H., Yu, M.C., Ross, R.K., Stallcup, M.R. and Coetzee, G.A.2000. Inhibition of p160-mediated coactivation with increasing androgen receptor polyglutamine length. Hum. Mol. Genet. 9:267–274.
Jenster, G., Trapman, J. and Brinkmann, A.O.1993. Nuclear import of the human androgen receptor. Biochem. J. 293:761–768.
Jenster, G., van der Korput, J.A., Trapman, J. and Brinkmann, A.O.1995. Identification of two transcription activation units in the N-terminal domain of the human androgen receptor. J. Biol. Chem. 270:7341–7346.
Jeong, B.C., Hong, C.Y., Chattopadhyay, S., Park, J.H., Gong, E.Y., Kim, H.J., Chun, S.Y. and Lee, K.2004. Androgen receptor corepressor-19 kDa (ARR19), a leucine-rich protein that represses the transcriptional activity of androgen receptor through recruitment of histone deacetylase. Mol. Endocrinol. 18:13–25.
Langley, E., Zhou, Z.X. and Wilson, E.M.1995. Evidence for an anti-parallel orientation of the ligand-activated human androgen receptor dimer. J. Biol. Chem. 270:29983–29990.
Lee, S.R., Ramos, S.M., Ko, A., Masiello, D., Swanson, K.D., Lu, M.L. and Balk, S.P.2002. AR and ER interaction with a p21-activated kinase (PAK6). Mol. Endocrinol. 16:85–99.
Lee, D.Y., Ianculescu, I., Purcell, D., Zhang, X., Cheng, X. and Stallcup, M.R.2007. Surface-scanning mutational analysis of protein arginine methyltransferase 1: roles of specific amino acids in methyltransferase substrate specificity, oligomerization, and coactivator function. Mol. Endocrinol. 21:1381–1393.
Lewis, B.A. and Reinberg, D.2003. The mediator coactivator complex: functional and physical roles in transcriptional regulation. J. Cell. Sci. 116:3667–3675.
Li, X.Y., Boudjelal, M., Xiao, J.H., Peng, Z.H., Asuru, A., Kang, S., Fisher, G.J. and Voorhees, J.J.1999. 1,25-Dihydroxyvitamin D3 increases nuclear vitamin D3 receptors by blocking ubiquitin/proteasome-mediated degradation in human skin. Mol. Endocrinol.13:1686–1694.
Li, J., Zhang, D., Fu, J., Huang, Z. and Wong, J. 2007. Structural and functional analysis of androgen receptor in chromatin. Mol. Endocrinol.
Liao, G., Chen, L.Y., Zhang, A., Godavarthy, A., Xia, F., Ghosh, J.C., Li, H. and Chen, J.D.2003. Regulation of androgen receptor activity by the nuclear corepressor SMRT. J. Biol. Chem. 278:5052–5061.
Lin, H.K., Hu, Y.C., Lee, D.K. and Chang, C.2004. Regulation of androgen receptor signaling by PTEN (phosphatase and tensin homolog deleted on chromosome 10) tumor suppressor through distinct mechanisms in prostate cancer cells. Mol. Endocrinol. 18:2409–2423.
Link, K.A., Burd, C.J., Williams, E., Marshall, T., Rosson, G., Henry, E., Weissman, B. and Knudsen, K.E.2005. BAF57 governs androgen receptor action and androgen-dependent proliferation through SWI/SNF. Mol. Cell. Biol. 25:2200–2215.
Liu, G., Wang, H. and Wang, Z.2003. Identification of a highly conserved domain in the androgen receptor that suppresses the DNA-binding domain-DNA interactions. J. Biol. Chem. 278:14956–14960.
Luisi, B.F., Xu, W.X., Otwinowski, Z., Freedman, L.P., Yamamoto, K.R. and Sigler, P.B.1991. Crystallographic analysis of the interaction of the glucocorticoid receptor with DNA. Nature352(6335):497–505.
Matias, P.M., Donner, P., Coelho, R., Thomaz, M., Peixoto, C., Mecedo, S., Otto, N., Joschko, S., Scholz, P., Wegg, A., Bäsler, S., Schäfer, M., Egner, U. and Carrondo, M.A.2000. Structural evidence for ligand specificity in the binding domain of the human androgen receptor. J. Biol. Chem. 275:26164–26171.
McEwan, I.J.2004. Molecular mechanisms of androgen receptor-mediated gene regulation: structure-function analysis of the AF-1 domain. Endocr. Relat. Cancer11:281–293.
McEwan, I.J., Lavery, D., Fischer, K. and Watt, K.2007. Natural disordered sequences in the amino terminal domain of nuclear receptors: lessons from the androgen and glucocorticoid receptors. Nucl. Recept. Signal. 5:e001.
Metzger, E., Müller, J.M., Ferrari, S., Buettner, R. and Schüle, R.2003A novel inducible transactivation domain in the androgen receptor: implications for PRK in prostate cancer. EMBO J.22:270–280.
Nascimento, A.S., Dias, S.M.G., Nunes, F.M., Aparicio, R., Ambrosio, A.L.B., Bleicher, L., Figueira, A.C.M., Santos, M.A.M., Neto, M.O., Fischer, H., Togashi, M., Craievich, A.F., Garratt, R.C., Baxter, J.D., Webb, P. and Plikaripov, I.2006. Structural rearrangements in the thyroid hormone receptor hinge domain and their putative role in the receptor function. J. Mol. Biol. 360:586–598.
Poukka, H., Karvonen, U., Janne, O.A. and Palvimo, J.J.2000a. Covalent modification of the androgen receptor by small ubiquitin-like modifier 1 (SUMO-1). Proc. Natl. Acad. Sci. USA97:14145–14150.
Poukka, H., Karvonen, U., Yoshikawa, N., Tanaka, H., Palvimo, J.J. and Jänne, O.A.2000b. The RING finger protein SNURF modulates nuclear trafficking of the androgen receptor. J. Cell. Sci. 113:2991–3001.
Rastinejad, F., Wagner, T., Zhao, Q. and Khorasanizadeh, S.2000. Structure of the RXRRAR DNA-binding complex on the retinoic acid response element DR1. EMBO J. 19:1045–1054.
Rechsteiner, M. and Rogers, S.W.1996. PEST sequences and regulation by proteolysis. Trends Biochem. Sci. 21:267–271.
Rees, I., Lee, S., Kim, H. and Tsai, FTF.2006. The E3 ubiquitin ligase CHIP binds the androgen receptor in a phosphorylation-dependent manner. Biochim. Biophys. Acta1764:1073–1079.
Sack, J.S., Kish, K.F., Wang, C., Attar, R.M., Kiefer, S.E., An, Y., Wu, G.Y., Scheffler, J.E., Salvati, M.E., Krystek, S.R., Weinmann, R. and Einsphar, H.M.2001. Crystallographic structures of the ligand-binding domains of the androgen receptor and its T877A mutant complexed with the natural agonist dihydrotestosterone. Proc. Natl. Acad. Sci. USA. 98:4904–4909.
Saporita, A.J., Zhang, Q., Navai, N., Dincer, Z., Hahn, J., Cai, X. and Wang, Z.2003. Identification and characterization of a ligand-regulated nuclear export signal in androgen receptor. J. Biol. Chem. 278:41998–42005.
Schoenmakers, E., Alen, P., Verrijdt, G., Peeters, B., Verhoeven, G., Rombauts, W. and Claessens, F.1999. Differential DNA binding by the androgen and glucocorticoid receptors involves the second Zn-finger and C-terminal extension of the DNA-binding domains. Biochem. J. 341:515–521.
Schoenmakers, E., Verrijdt, G., Peeters, B., Verhoeven, G., Rombauts, W. and Claessens, F.2000. Differences in DNA binding characteristics of the androgen and glucocorticoid receptors can determine hormone-specific responses. J. Biol. Chem. 275:12290–12297.
Shaffer, P., Jivan, A., Dollins, D.E., Claessens, F. and gewirth, D.T.2004. Structural basis of androgen receptor binding to selective androgen response elements. Proc. Natl. Acad. Sci. 101:4758–4763.
Sheflin, L., Keegan, B., Zhang, W. and Spaulding, S.W.2000. Inhibiting proteasomes in human Hep3B and LNCaP cells increases endogenous androgen receptor levels. Biochem. Biophys. Res. Commun. 276:144–150.
Shin, S. and Verma, I.M.2003. BRCA2 cooperates with histone acetyltransferases in androgen receptor-mediated transcription. Proc. Natl. Acad. Sci. USA100:7201–7206.
Sleddens, H.F., Oostra, B.A., Brinkmann, A.O. and Trapman, J.1992. Trinucleotide repeat polymorphism in the androgen receptor gene (AR). Nucleic Acids Res. 20:1427.
Tanner, T., Claessens, F. and Haelens, A.2004. The hinge region of the androgen receptor plays a role in proteasome-mediated transcriptional activation. Ann. NY Acad. Sci. 1030:587–592.
Tilley, W.D., Buchanan, G., Hickey, T.E. and Bentel, J.M.1996. Mutations in the androgen receptor gene are associated with progression of human prostate cancer to androgen independence. Clin. Cancer Res. 2:277–285.
Van Royen, M.E., Cunha, S.M., Brink, M.C., Mattern, K.A., Nigg, A.L., Dubbink, H.J., Verschure, P.J., Trapman, J. and Houtsmuller, A.2007. Compartmentalization of androgen receptor protein-protein interactions in living cells. J. Cell. Biol. 177:63–72.
Veldscholte, J., Berrevoets, C.A., Zegers, N.D., van der Kwast, T.H., Grootegoed, J.A. and Mulder, E.1992. Hormone-induced dissociation of the androgen receptor-heat-shock protein complex: use of a new monoclonal antibody to distinguish transformed from nontransformed receptors. Biochemistry31:7422–7430.
Verrijdt, G., Schoenmakers, E., Alen, P., Haelens, A., Peeters, B., Rombauts, W. and Claessens, F.1999. Androgen specificity of a response unit upstream of the human secretory component gene is mediated by differential receptor binding to an essential androgen response element. Mol. Endocrinol. 13:1558–1570.
Verrijdt, G., Schoenmakers, E., Haelens, A., Peeters, B., Verhoeven, G., Rombauts, W. and Claessens, F.2000. Change of specificity mutations in androgen-selective enhancers: evidence for a role of differential DNA binding by the androgen receptor. J. Biol. Chem. 275:12298–12305.
Verrijdt, G., Tanner, T., Moehren, U., Callewaert, L., Haelens, A. and Claessens, F.2006. Biochem. Soc. Trans. 34:1089–1094.
Vijayvargia, R., May, M.S. and Fondell, J.D.2007. A coregulatory role for the mediator complex in prostate cancer cell proliferation and gene expression. Cancer Res. 67:4034–4041.
Wang, Q., Lu, J.H. and Yong, E.L.2001. Ligand- and coactivator-mediated transactivation function 2 (AF2) of the androgen receptor ligand-binding domain is inhibited by the cognate hinge region. J. Biol. Chem. 276:7493–7499.
Wang, Q., Li, W., Liu, X.S., Carroll, J.S., Jänne, O.A., Keeton, E.K., Chinnaiyan, A.M., Pienta, K.J. and Brown, M.2007. A hierarchical network of transcription factors governs androgen receptor-dependent prostate cancer growth. Mol. Cell27:380–392.
Werner, R., Holterhus, P.M., Binder, G., Schwartz, H.P., Morlot, M., Struve, D., Marschke, C. and Hiort, O.2006. The A645D mutation in the hinge region of the human androgen receptor (AR) gene modulates AR activity, depending on the context of the polymorphic glutamine and glycine repeats. J. Clin. Endocrinol. Metab. 91:3515–3520.
Xu, P., Liu, Y., Shan, S., Kong, Y., Zhou, Q., Li, M., Ding, J., Xie, Y. and Wang, Y.2004. Molecular mechanism for the potentiation of the transcriptional activity of human liver receptor homolog 1 by steroid receptor coactivator-1. Mol. Endocrinol. 18:1887–1905.
Zhou, Z.X., Sar, M., Simental, J.A., Lane, M.V. and Wilson, E.M.1994. A ligand-dependent bipartite nuclear targeting signal in the human androgen receptor. Requirement for the DNA-binding domain and modulation by NH2-terminal and carboxyl-terminal sequences. J. Biol. Chem.269:13115–13123.
Zhou, Z.X., Kemppainen, J.A. and Wilson, E.M.1995. Identification of three proline-directed phosphorylation sites in the human androgen receptor. Mol. Endocrinol.9:605 615.
Zhu, P., Baek, S.H., Bourk, E.M., Garcia-Bassets, I., Sanjo, H., Akira, S., Kotol, P.F., Glass, C.K., Rosenfeld, R.M. and Rose, D.W.2006. Macrophage/cancer cell interactions mediate hormone resistance by a nuclear receptor derepression pathway. Cell124:615–629.
Zuccarello, D., Ferlin, A., Vinanzi, C., Prana, E., Callewaert, L., Claessens, F., Brinkmann, O.A. and Foresta, C.2007. Detailed functional studies on androgen receptor mild mutations demonstrate their association with male infertility. Clin. Endocrinol. 68:580–588.
Acknowledgments
We are grateful to the members of the Molecular Endocrinology Laboratory of Leuven for helpful discussions. This laboratory has been supported by the “Fonds voor Wetenschappelijk Onderzoek-Vlaanderen (FWO),” by a U.S. Army Prostate Cancer Research Program grant, by a “Geconcerteerde Onderzoeksactie K.U. Leuven,” and by a grant of the Association for International Cancer Research (AICR).
Author information
Authors and Affiliations
Editor information
Rights and permissions
Copyright information
© 2009 Springer Science+Business Media, LLC
About this chapter
Cite this chapter
Claessens, F., Tanner, T., Haelens, A. (2009). Multitasking and Interplay Between the Androgen Receptor Domains. In: Mohler, J., Tindall, D. (eds) Androgen Action in Prostate Cancer. Springer, New York, NY. https://doi.org/10.1007/978-0-387-69179-4_17
Download citation
DOI: https://doi.org/10.1007/978-0-387-69179-4_17
Published:
Publisher Name: Springer, New York, NY
Print ISBN: 978-0-387-69177-0
Online ISBN: 978-0-387-69179-4
eBook Packages: Biomedical and Life SciencesBiomedical and Life Sciences (R0)