The Androgen Receptor Amino-Terminal Domain Plays a Key Role in p160 Coactivator-Stimulated Gene Transcription

REFERENCES

• Aarnisalo, P., J. J. Palvimo, and J. Jänne 1998. CREB-binding protein in androgen receptor-mediated signaling. Proc. Natl. Acad. Sci. USA 95:2122–2127.
   PubMed Web of Science ®Google Scholar
• Alen, P., F. Claessens, E. Schoenmakers, J. V. Swinnen, G. Verhoeven, W. Rombauts, and J. Peeters 1999. Interaction of the putative androgen receptor-specific coactivator ARA70/ELE1α with multiple steroid receptors and identification of an internally deleted ELE1β isoform. Mol. Endocrinol. 13:117–128.
   PubMedGoogle Scholar
• Anzick, S. L., J. Kononen, R. L. Walker, D. O. Azorsa, M. M. Tanner, X. Y. Guan, G. Sauter, O. P. Kallioniemi, J. M. Trent, and J. Meltzer 1997. AIB1, a steroid receptor coactivator amplified in breast and ovarian cancer. Science 277:965–968.
   PubMed Web of Science ®Google Scholar
• Baniahmad, A., A. C. Kohne, and J. Renkawitz 1992. A transferable silencing domain is present in the thyroid hormone receptor, in the v-erbA oncogene product and in the retinoic acid receptor. EMBO J. 11:1015–1023.
   PubMedGoogle Scholar
• Bannister, A. J., and J. Kouzarides 1996. The CBP co-activator is a histone acetyltransferase. Nature 384:641–643.
   PubMed Web of Science ®Google Scholar
• Beato, M., S. Chavez, and J. Truss 1996. Transcriptional regulation by steroid hormones. Steroids 61:240–251.
   PubMedGoogle Scholar
• Beato, M., and J. Sanchez-Pacheco 1996. Interaction of steroid hormone receptors with the transcription initiation complex. Endocrine Rev. 17:587–609.
   PubMed Web of Science ®Google Scholar
• Berrevoets, C. A., P. Doesburg, K. Steketee, J. Trapman, and J. Brinkmann 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 factor 2). Mol. Endocrinol. 12:1172–1183.
   PubMed Web of Science ®Google Scholar
• Blanco, J. C. G., S. Minucci, J. Lu, X. J. Yang, K. K. Walker, H. Chen, R. M. Evans, Y. Nakatani, and J. Ozato 1998. The histone acetylase PCAF is a nuclear receptor coactivator. Genes Dev. 12:1638–1651.
   PubMed Web of Science ®Google Scholar
• Buchert, M., S. Schneider, M. T. Adams, H. P. Hefti, K. Moelling, and J. Hovens 1997. Useful vectors for the two-hybrid system in mammalian cells. BioTechniques 23:396–402.
   PubMedGoogle Scholar
• Chamberlain, N. L., D. C. Whitacre, and J. Miesfeld 1996. Delineation of two distinct type 1 activation functions in the androgen receptor amino-terminal domain. J. Biol. Chem. 271:26772–26778.
   PubMedGoogle Scholar
• Chen, H., R. J. Lin, R. L. Schiltz, D. Chakravarti, A. Nash, L. Nagy, M. L. Privalsky, Y. Nakatani, and J. Evans 1997. Nuclear receptor coactivator ACTR is a novel histone acetyltransferase and forms a multimeric activation complex with P/CAF and CBP/p300. Cell 90:569–580.
   PubMed Web of Science ®Google Scholar
• Danielian, P. S., R. White, J. A. Lees, and J. Parker 1992. Identification of a conserved region required for hormone dependent transcriptional activation by steroid hormone receptors. EMBO J. 11:1025–1033.
   PubMed Web of Science ®Google Scholar
• Ding, X. F., C. M. Anderson, H. Ma, H. Hong, R. M. Uht, P. Kushner, and J. Stallcup 1998. Nuclear receptor-binding sites of coactivators glucocorticoid receptor interaction protein 1(GRIP1) and steroid receptor coactivator 1 (SRC1): multiple motifs with different binding specificities. Mol. Endocrinol. 12:302–313.
   PubMedGoogle Scholar
• Doesburg, P., C. W. Kuil, C. A. Berrevoets, K. Steketee, P. W. Faber, E. Mulder, A. O. Brinkmann, and J. Trapman 1997. Functional in vivo interaction between the amino-terminal and the ligand binding domain of the androgen receptor. Biochemistry 36:1052–1064.
   PubMed Web of Science ®Google Scholar
• Fawell, S. E., J. A. Lees, R. White, and J. Parker 1990. Characterization and colocalization of steroid binding and dimerization activities in the mouse estrogen receptor. Cell 60:953–962.
   PubMed Web of Science ®Google Scholar
• Feng, W., R. C. J. Ribeiro, R. L. Wagner, H. Nguyen, J. W. Apriletti, R. J. Fletterick, J. D. Baxter, P. J. Kushner, and J. West 1998. Hormone-dependent coactivator binding to a hydrophobic cleft on nuclear receptors. Science 280:1747–1749.
   PubMed Web of Science ®Google Scholar
• Fronsdal, K., N. Engedal, T. Slagsvold, and J. Saatcioglu 1998. CREB binding protein is a coactivator for the androgen receptor and mediates cross-talk with AP-1. J. Biol. Chem. 273:31853–31859.
   PubMed Web of Science ®Google Scholar
• Heery, D. M., E. Kalkhoven, S. Hoare, and J. Parker 1997. A signature motif in transcriptional co-activators mediates binding to nuclear receptors. Nature 387:733–736.
   PubMed Web of Science ®Google Scholar
• Henttu, P. M. A., E. Kalkhoven, and J. Parker 1997. AF-2 activity and recruitment of steroid receptor coactivator 1 to the estrogen receptor depend on a lysine residue conserved in nuclear receptors. Mol. Cell. Biol. 17:1832–1839.
   PubMedGoogle Scholar
• Hong, H., K. Kohli, M. J. Garabedian, and J. Stallcup 1997. GRIP1, a transcriptional coactivator for the AF-2 transactivation domain of steroid, thyroid, retinoid, and vitamin D receptors. Mol. Cell. Biol. 17:2735–2744.
   PubMed Web of Science ®Google Scholar
• Hong, H., B. D. Darimont, H. Ma, L. Yang, K. R. Yamamoto, and J. Stallcup 1999. An additional region of coactivator GRIP1 required for interaction with the hormone-binding domains of a subset of nuclear receptors. J. Biol. Chem. 274:3496–3502.
   PubMed Web of Science ®Google Scholar
• Horwitz, K. B., T. A. Jackson, D. L. Bain, J. K. Richer, G. S. Takimoto, and J. Tung 1996. Nuclear receptor coactivators and corepressors. Mol. Endocrinol. 10:1167–1177.
   PubMed Web of Science ®Google Scholar
• Ikonen, T., J. J. Palvimo, and J. Jänne 1997. 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. 272:29821–29828.
   PubMedGoogle Scholar
• Jenster, G., H. A. G. M. van der Korput, C. C. J. van Groonhoven, T. H. Van der Kwast, J. Trapman, and J. Brinkmann 1991. Domains of the human androgen receptor involved in steroid binding, transcriptional activation, and subcellular localization. Mol. Endocrinol. 5:1396–1404.
   PubMed Web of Science ®Google Scholar
• Jenster, G., H. A. G. M. van der Korput, J. Trapman, and J. Brinkmann 1995. Identification of two transcription activation units in the N-terminal domain of the human androgen receptor. J. Biol. Chem. 270:7341–7346.
   PubMed Web of Science ®Google Scholar
• Jenster, G. 1998. Coactivators and corepressors as mediators of nuclear receptor function: an update. Mol. Cell. Endocrinol. 143:1–7.
   PubMed Web of Science ®Google Scholar
• Jeyakumar, M., M. R. Tanen, and J. Bagchi 1997. Analysis of the functional role of steroid receptor coactivator-1 in ligand-induced transactivation by thyroid hormone receptor. Mol. Endocrinol. 11:755–767.
   PubMedGoogle Scholar
• Kalkhoven, E., J. E. Valentin, D. M. Heery, and J. Parker 1998. Isoforms of steroid receptor co-activator 1 differ in their ability to potentiate transcription by the oestrogen receptor. EMBO J. 17:232–243.
   PubMed Web of Science ®Google Scholar
• Kamei, Y., L. Xu, T. Heinzel, J. Torchia, R. Kurokawa, B. Gloss, S.-C. Lin, R. A. Heyman, D. W. Rose, C. K. Glass, and J. Rosenfeld 1996. A CBP integrator complex mediates transcriptional activation and AP-1 inhibition by nuclear receptors. Cell 85:403–414.
   PubMed Web of Science ®Google Scholar
• Langley, E., Z. X. Zhou, and J. Wilson 1995. Evidence for an anti-parallel orientation of the ligand-activated human androgen receptor dimer. J. Biol. Chem. 270:29983–29990.
   PubMed Web of Science ®Google Scholar
• Langley, E., J. A. Kemppainen, and J. Wilson 1998. Intermolecular NH2-carboxyl-terminal interactions in androgen receptor dimerization revealed by mutations that cause androgen insensitivity. J. Biol. Chem. 273:92–101.
   PubMed Web of Science ®Google Scholar
• Lavinsky, R. M., K. Jepsen, T. Heinzel, J. Torchia, T.-M. Mullen, R. Schiff, A. L. Del-Rio, M. Ricolte, S. Ngo, J. Gemsch, S. G. Hilsenbeck, C. K. Osborne, C. K. Glass, M. G. Rosenfeld, and J. Rose 1998. Diverse signaling pathways modulate nuclear receptor recruitment of N-CoR and SMRT complexes. Proc. Natl. Acad. Sci. USA 95:2920–2925.
   PubMed Web of Science ®Google Scholar
• Leers, J., E. Treuter, and J. Gustaffson 1998. Mechanistic principles in NR box-dependent interaction between nuclear hormone receptors and the coactivator TIF2. Mol. Cell. Biol. 18:6001–6013.
   PubMedGoogle Scholar
• Li, H., P. J. Gomes, and J. Chen 1996. RAC3, a steroid/nuclear receptor-associated coactivator that is related to SRC-1 and TIF2. Proc. Natl. Acad. Sci. USA 94:8479–8484.
   Google Scholar
• Li, H., and J. Chen 1998. The receptor-associated coactivator 3 activates transcription through CREB-binding protein recruitment and autoregulation. J. Biol. Chem. 273:5948–5954.
   PubMedGoogle Scholar
• Mangelsdorf, D. J., C. Thummel, M. Beato, P. Herrlich, G. Schutz, K. Umesono, B. Blumberg, P. Kastner, M. Mark, P. Chambon, and J. Evans 1995. The nuclear receptor superfamily: the second decade. Cell 83:835–839.
   PubMed Web of Science ®Google Scholar
• Marivoet, S., M. Hertogen, G. Verhoeven, and J. Heyns 1990. Antibodies against synthetic peptide recognise the human and rat androgen receptor. J. Steroid Biochem. Mol. Biol. 37:39–45.
   PubMedGoogle Scholar
• McInerney, E. M., M. J. Tsai, B. W. O’Malley, and J. Katzenellenbogen 1996. Analysis of estrogen receptor transcriptional enhancement by a nuclear hormone receptor coactivator. Proc. Natl. Acad. Sci. USA 93:10069–10073.
   PubMed Web of Science ®Google Scholar
• Moilanen, A., N. Rouleau, T. Ikonen, J. J. Palvimo, and J. Jänne 1997. The presence of a transcription activation function in the hormone-binding domain of androgen receptor is revealed by studies in yeast cells. FEBS Lett. 412:355–358.
   PubMedGoogle Scholar
• Moilanen, A., H. Poukka, U. Karvonen, M. Häkli, O. A. Jänne, and J. Palvimo 1998. Identification of a novel RING finger protein as a coregulator in steroid receptor-mediated gene transcription. Mol. Cell. Biol. 18:5128–5139.
   PubMed Web of Science ®Google Scholar
• Moras, D., and J. Gronemeyer 1998. The nuclear receptor ligand-binding domain: structure and function. Curr. Opin. Cell Biol. 10:384–391.
   PubMed Web of Science ®Google Scholar
• Nolte, R. T., G. B. Wisely, S. Westin, J. E. Cobb, M. Lambert, R. Kurokawa, M. Rosenfeld, T. M. Willson, C. K. Glass, and J. Milburn 1998. Ligand binding and co-activator assembly of the peroxisome proliferator-activated receptor-γ. Nature 395:137–143.
   PubMed Web of Science ®Google Scholar
• Ogryzko, V. V., R. L. Schiltz, V. Russanova, B. H. Howard, and J. Nakatani 1996. The transcriptional coactivators p300 and CBP are histone acetyltransferases. Cell 87:953–959.
   PubMed Web of Science ®Google Scholar
• Onate, S. A., S. Y. Tsai, M. J. Tsai, and J. O’Malley 1995. Sequence and characterization of a coactivator for the steroid hormone receptor superfamily. Science 270:1354–1357.
   PubMed Web of Science ®Google Scholar
• Onate, S. A., V. Boonyaratanakornkit, T. E. Spencer, S. Y. Tsai, M. J. Tsai, D. P. Edwards, and J. O’Malley 1998. The steroid receptor coactivator-1 contains multiple receptor interaction domains that cooperatively enhance the activation function 1 (AF1) and AF2 domains of steroid receptors. J. Biol. Chem. 273:12101–12108.
   PubMed Web of Science ®Google Scholar
• Parker, M. G., and J. White 1996. Nuclear receptors spring into action. Nat. Struct. Biol. 3:113–115.
   PubMedGoogle Scholar
• Plaisance, S., W. VandenBerghe, E. Boone, W. Fiers, and J. Haegeman 1997. Recombination signal sequence binding protein J kappa is constitutively bound to the NF-kappa B site of the interleukin-6 promoter and acts as a negative regulatory factor. Mol. Cell. Biol. 17:3733–3743.
   PubMedGoogle Scholar
• Quigley, C. A., A. De Bellis, K. B. Marschke, M. K. El-Awady, E. M. Wilson, and J. French 1995. Androgen receptor defects: historical, clinical, and molecular perspectives. Endocrine Rev. 16:271–321.
   PubMed Web of Science ®Google Scholar
• Schmidt, S., A. Baniahmad, M. Eggert, S. Schneider, and J. Renkawitz 1998. Multiple receptor interaction domains of GRIP1 function in synergy. Nucleic Acids. Res. 26:1191–1197.
   PubMedGoogle Scholar
• Shiau, A. K., D. Barstad, P. M. Loria, L. Cheng, P. J. Kushner, D. A. Agard, and J. Greene 1999. The structural basis of estrogen receptor/coactivator recognition and the antagonism of this interaction by tamoxifen. Cell 95:927–937.
   Web of Science ®Google Scholar
• Shibata, H., T. E. Spencer, S. A. Onate, G. Jenster, S. Y. Tsai, M. J. Tsai, and J. O’Malley 1997. Role of coactivators and corepressors in the mechanism of steroid/thyroid receptor action. Recent Prog. Horm. Res. 52:141–165.
   PubMedGoogle Scholar
• Simental, J. A., M. Sar, and J. Wilson 1992. Domain functions of the androgen receptor. J. Steroid Biochem. Mol. Biol. 43:37–41.
   PubMedGoogle Scholar
• Smith, C. L., Z. Nawaz, and J. O’Malley 1997. Coactivator and corepressor regulation of the agonist/antagonist activity of the mixed antiestrogen, 4-hydroxytamoxifen. Mol. Endocrinol. 11:657–666.
   PubMed Web of Science ®Google Scholar
• Spencer, T. E., G. Jenster, M. M. Burcin, C. D. Allis, J. Zhou, C. A. Mizzen, N. J. McKenna, S. A. Onate, S. Y. Tsai, M. J. Tsai, and J. O’Malley 1997. Steroid receptor coactivator-1 is a histone acetyltransferase. Nature 389:194–198.
   PubMed Web of Science ®Google Scholar
• Suen, C. S., T. J. Berrodin, R. Mastroeni, B. J. Cheskis, C. R. Lyttle, and J. Frail 1998. A transcriptional coactivator, steroid receptor coactivator-3, selectively augments steroid receptor transcriptional activity. J. Biol. Chem. 273:27645–27653.
   PubMedGoogle Scholar
• Takeshita, A., P. M. Yen, S. Misti, G. R. Cardona, Y. Liu, and J. Chin 1996. Molecular cloning and properties of a full-length putative thyroid hormone receptor coactivator. Endocrinology 137:3594–3597.
   PubMed Web of Science ®Google Scholar
• Takeshita, A., G. R. Cardona, N. Koibuchi, C. S. Suen, and J. Chin 1997. TRAM-1, a novel 160-kDa thyroid hormone receptor activator molecule, exhibits distinct properties from steroid receptor coactivator-1. J. Biol. Chem. 272:27629–27634.
   PubMedGoogle Scholar
• Takeshita, A., P. M. Yen, M. Ikeda, G. R. Cardona, Y. Liu, N. Koibuchi, E. R. Norwitz, and J. Chin 1998. Thyroid hormone response elements differentially modulate the interactions of thyroid hormone receptors with two receptor binding domains in the steroid receptor coactivator-1. J. Biol. Chem. 273:21554–21562.
   PubMedGoogle Scholar
• Torchia, J., D. W. Rose, J. Inostroza, Y. Kamei, S. Westin, C. Glass, and J. Rosenfeld 1997. The transcriptional co-activator p/CIP binds CBP and mediates nuclear-receptor function. Nature 387:677–684.
   PubMed Web of Science ®Google Scholar
• Torchia, J., C. Glass, and J. Rosenfeld 1998. Co-activators and co-repressors in the integration of transcriptional responses. Curr. Opin. Cell. Biol. 10:373–383.
   PubMed Web of Science ®Google Scholar
• Tsai, M. J., and J. O’Malley 1994. Molecular mechanisms of action of steroid/thyroid receptor superfamily members. Annu. Rev. Biochem. 63:451–486.
   PubMed Web of Science ®Google Scholar
• Tsai, R. Y. L., and J. Reed 1997. Using a eukaryotic GST fusion vector for proteins difficult to express in E. coli. BioTechniques 23:794–800.
   PubMedGoogle Scholar
• Voegel, J. J., M. J. S. Heine, C. Zechel, P. Chambon, and J. Gronemeyer 1996. TIF2, a 160 kDa transcriptional mediator for the ligand-dependent activation function AF-2 of nuclear receptors. EMBO J. 15:3667–3675.
   PubMed Web of Science ®Google Scholar
• Voegel, J. J., M. J. S. Heine, M. Tini, V. Vivat, P. Chambon, and J. Gronemeyer 1998. The coactivator TIF2 contains three nuclear receptor-binding motifs and mediates transactivation through CBP binding-dependent and -independent pathways. EMBO J. 17:507–519.
   PubMed Web of Science ®Google Scholar
• Webb, P., P. Nguyen, J. Shinsako, C. Anderson, W. Feng, M. P. Nguyen, D. Chen, S. M. Huang, S. Subramanian, E. McKinerney, B. S. Katzenellenbogen, M. R. Stallcup, and J. Kushner 1998. Estrogen receptor activation function 1 works by binding p160 coactivator proteins. Mol. Endocrinol. 12:1605–1618.
   PubMed Web of Science ®Google Scholar
• Williams, S. P., and J. Sigler 1998. Atomic structure of progesterone complexed with its receptor. Nature 393:392–396.
   PubMed Web of Science ®Google Scholar
• Wong, C. I., Z. X. Zhou, M. Sar, and J. Wilson 1993. Steroid requirements for androgen receptor dimerization and DNA binding. J. Biol. Chem. 268:19004–19012.
   PubMedGoogle Scholar
• Wurtz, J. M., W. Bourguet, J. P. Renaud, V. Vivat, P. Chambon, D. Moras, and J. Gronemeyer 1996. A canonical structure for the ligand-binding domain of nuclear receptors. Nat. Struct. Biol. 3:87–94.
   PubMedGoogle Scholar
• Xu, J., Z. Nawaz, S. Y. Tsai, M. J. Tsai, and J. O’Malley 1996. The extreme C-terminus of the progesterone receptor contains a transcriptional repressor domain that functions through a putative corepressor. Proc. Natl. Acad. Sci. USA 93:12195–12199.
   PubMed Web of Science ®Google Scholar
• Yang, X. J., V. V. Ogryzko, J. I. Nishikawa, B. Howard, and J. Nakatani 1996. A p300/CBP-associated factor that competes with the adenoviral oncoprotein E1A. Nature 283:319–324.
   Google Scholar
• Zhou, G., R. Cummings, Y. Li, S. Mitra, H. A. Wilkinson, A. Elbrecht, J. D. Hermes, J. M. Schaeffer, R. G. Smith, and J. Moller 1998. Nuclear receptors have distinct affinities for coactivators: characterization by fluorescence resonance energy transfer. Mol. Endocrinol. 12:1594–1604.
   PubMedGoogle Scholar