Recruitment of p160 Coactivators to Androgen Receptors

  • M. Parker
  • C. Bevan
Conference paper
Part of the Ernst Schering Research Foundation Workshop book series (SCHERING FOUND, volume 6)

Abstract

Androgens control the proliferation of target cells and a number of physiological responses by means of receptors that function as ligand-dependent transcription factors. Androgen receptors (AR) function either directly by binding to response elements in the vicinity of the promoter or indirectly by modulating the activity of other transcription factors. In common with other nuclear receptors the AR is likely to undergo a characteristic conformational change upon ligand binding that allows the recruitment of cofactors which are required to stimulate transcription of target genes [1, 2, 3]. It first became obvious that nuclear receptors require common cofactors to activate transcription when “squelching” between different receptors was observed: the expression of one active receptor inhibited the activity of a second, implying the existence of an essential limiting cofactor [4].

Keywords

Estrogen Glutamine Tamoxifen Androgen Acetyl 

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References

  1. 1.
    Mangelsdorf DJ, Thummel C, Beato M, Herrlich P, Schutz G, Umesono K, Blumberg B, Kastner P, Mark M, Chambon P, Evans RE (1995) The nuclear receptor superfamily: the second decade. Cell 83: 835–839PubMedCrossRefGoogle Scholar
  2. 2.
    Parker MG, White R (1996) Nuclear receptors spring into action. Nature Structural Biology 3: 113–115PubMedCrossRefGoogle Scholar
  3. 3.
    Glass CK, Rose DW, Rosenfeld MG (1997) Nuclear receptor coactivators. Current Opinion in Cell Biology 9: 222–232PubMedCrossRefGoogle Scholar
  4. 4.
    Tasset D, Tora L, Fromental C, Scheer E, Chambon P (1990) Distinct classes of transcriptional activating domains function by different mechanisms. Cell 62: 1177–1187PubMedCrossRefGoogle Scholar
  5. 5.
    Kadanoga JT (1998) Eukaryotic transcription: an interlaced network of transcription factors and chromatin-modifying machines. Cell 92: 307–313CrossRefGoogle Scholar
  6. 6.
    Freedman LP (1999) Increasing the complexity of coactivation in nuclear receptor signaling. Cell 97: 5–8PubMedCrossRefGoogle Scholar
  7. 7.
    Jenster G, van der Korput H, Trapman J, Brinkmann AO (1995) Identification of two transcription activation units in the N-terminal domain of the human androgen receptor. J. Biol. Chem. 270: 7341–46Google Scholar
  8. 8.
    Bevan CL, Hoare S, Claessens F, Heery DM, Parker MG (1999) The AF1 and AF2 domains of the androgen receptor interact with distinct regions of SRC1. Mol Cell Biol 20: 8383–8392Google Scholar
  9. 9.
    Darimont BD, Wagner RL, Apriletti JW, Stallcup MR, Kushner PJ, Baxter JD, Fletterick RJ, Yamamoto KR (1998) Structure and specificity of nuclear receptor-coactivator interactions. Genes Dev 12: 3343–56PubMedCrossRefGoogle Scholar
  10. 10.
    Mak HY, Hoare S, Henttu PMA, Parker MG (1999) Molecular determinants of the estrogen receptor-coactivator interface. Molecular Cellular Biology 19: 3895–3903Google Scholar
  11. 11.
    Nolte RT, Wisely GB, Westin S, Cobb JE, Lambert MH, Kurokawa R, Rosenfeld MG, Willson TM, Glass CK, Milburn MV (1998) Ligand binding and co-activator assembly of the peroxisome proliferator-activated receptor-gamma. Nature 395: 137–43PubMedCrossRefGoogle Scholar
  12. 12.
    Shiau AK, Barstad D, Loria PM, Cheng L, Kushner PJ, Agard DA, Greene GL (1998) The structural basis of estrogen receptor/coactivator recognition and the antagonism of this interaction by tamoxifen. Cell 95: 927–937PubMedCrossRefGoogle Scholar
  13. 13.
    Kalkhoven E, Valentine JE, Heery DM, Parker MG (1998) Isoforms of steroid receptor coactivator 1 differ in their ability to potentiate transcription by the oestrogen receptor. EMBO J 17: 232–243PubMedCrossRefGoogle Scholar
  14. 14.
    Doesburg P, Kuil CW, Berrevoets CA, Steketee K, Faber PW, Mulder E, Brinkmann AO, Trapman J (1997) Functional in vivo interaction between the amino-terminal, transactivating domain and the ligand binding domain of the androgen receptor. Biochemistry 36: 1052–1064PubMedCrossRefGoogle Scholar
  15. 15.
    Berrevoets CA, Doesburg P, Sketetee K, Trapman J, Brinkmann AO (1998) Functional interactions of the AF-2 domain core region of the human androgen receptor with the amino-terminal domain and with the transcriptional coactivator TIF-2 (transcriptional intermediary factor-2). Mol Endocrinol 12: 1172–1183PubMedCrossRefGoogle Scholar
  16. 16.
    Ikonen T, Palvimo JJ, Janne OA (1998) Heterodimerization is mainly responsible for the dominant negative activity of amino-terminally truncated rat androgen receptor forms. FEBS Lett 430: 393–6PubMedCrossRefGoogle Scholar
  17. 17.
    Langley E, Kemppainen JA, E.M. W (1998) Intermolecular NH2-/carboxyterminal interactions in androgen receptor dimerization revealed by mutations that cause androgen insensitivity. J Biol Chem 273: 92–101Google Scholar
  18. 18.
    Voegel JJ, Heine MJ, Tini M, Vivat V, Chambon P, Gronemeyer H (1998) The coactivator TIF2 contains three nuclear receptor-binding motifs and mediates transactivation through CBP binding-dependent and -independent pathways. EMBO J 17: 507–19PubMedCrossRefGoogle Scholar
  19. 19.
    Torchia J, Rose DW, Inostroza J, Kamei Y, Westin S, Glass CK, Rosenfeld MG (1997) The transcriptional co-activator p/CIP binds CBP and mediates nuclear-receptor function. Nature 387: 677–684PubMedCrossRefGoogle Scholar
  20. 20.
    Ikonen T, Palvimo JJ, Janne OA (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: 29821–29828PubMedCrossRefGoogle Scholar
  21. 21.
    Fronsdal K, Engedal N, Slagsvold T, Saatcioglu F (1998) CREB binding protein is a coactivator for the androgen receptor and mediates cross-talk with AP-1. J Biol Chem 273: 31853–31859PubMedCrossRefGoogle Scholar
  22. 22.
    Spencer TE, Jenster G, Burcin MM, Allis CD, Zhou J, Mizzen CA, McKenna NJ, Onate SA, Tsai SY, Tsai M-J, O’Malley BW (1997) Steroid receptor coactivator-1 is a histone acetyltransferase. Nature 389: I94–198Google Scholar
  23. 23.
    Chen D, Ma H, Hing H, Koh SS, Huang S-M, Schurter BT, Aswad DW, Stallcup M R (1999) Regulation of transcription by a protein methyltransferase. Science 284: 2174–2177PubMedCrossRefGoogle Scholar

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© Springer-Verlag Berlin Heidelberg 2000

Authors and Affiliations

  • M. Parker
  • C. Bevan

There are no affiliations available

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