19
Views
2
CrossRef citations to date
0
Altmetric
Original Article

Proteins Accompanying the Estrogen Receptor α and β: A Model for Studying Protein Hetero-Complexes

, &
Pages 427-442 | Received 06 Apr 2000, Published online: 11 Jul 2009

References

  • Anzick S. L., Kononen J., Walker R. L., Azorsa D. O., Tanner M. M., Guan X. Y., Sauter G., Kallioniemi O. P., Trent J. M., Meltzer P. S. “AIB1, a steroid receptor coactivator amplified in breast and ovarian cancer”. Science 1997; 277: 965–968
  • Bannister AJ, Kouzarides T. “The CBP co-activator is a histone acetyltransferase”. Nature 1996; 384: 641–643
  • Brady M. E., Ozanne D. M., Gaughan L., Waite I., Cook S., Neal D. E., Robson C. N. “Tip60 is a nuclear hormone receptor coactivator”. J. Biol. Chem 1999; 274: 17599–17604
  • Caira F, Antonson P., Pelto-Huikko M, Treuter E., Gustafsson J. A. “Cloning and characterization of RAP250, a novel nuclear receptor coactivator”. J. Biol. Chem 2000; 275: 5308–5317
  • Carrello A., Ingley E., Minchin R. F., Tsai S., Ratajczak T. “The common tetratricopeptide repeat acceptor site for steroid receptor-associated immunophilins and hop is located in the dimerization domain of Hsp90”. J. Biol. Chem 1999; 274: 2682–2689
  • Cavailles V., Dauvois S., Danielian P. S., Parker M. G. “Interaction of proteins with transcriptionally active estrogen receptors”. Proc. Natl. Acad. Sci. USA 1994; 91: 10009–10013
  • Cavailles V., Dauvois S., L'Horset F., Lopez G., Hoare S., Kushner PJ, Parker M. G. “Nuclear factor RIP 140 modulates transcriptional activation by the estrogen receptor”. Embo. J 1995; 14: 3741–3751
  • Chen S., Prapapanich V., Rimerman R. A., Honoré B., Smith D. F. “Interactions of p60, a mediator of progesterone receptor assembly, with heat shock proteins hsp90 and hsp70”. Mol. Endocrinol 1996; 10: 682–693
  • Couse J. F., Hewitt S. C., Bunch D. O., Sar M., Walker V. R., Davis B. J., Korach K. S. “Postnatal sex reversal of the ovaries in mice lacking estrogen receptors alpha and beta”. Science 1999; 286: 2328–2331
  • Eng F. C., Barsalou A., Akutsu N., Mercier I., Zechel C, Mader S., White J. H. “Different classes of coactivators recognize distinct but overlapping binding sites on the estrogen receptor ligand binding domain”. J. Biol. Chem 1998; 273: 28371–28377
  • Evans R. M. “The steroid and thyroid hormone receptor superfamily”. Science 1988; 240: 889–895
  • Fivash M., Towler E. M., Fisher R. J. “BIAcore for macromolecular interaction”. Curr. Opin. Biotechnol 1998; 9: 97–101
  • Freeman B. C., Toft D. O., Morimoto R. I. “Molecular chaperone machines: chaperone activities of the cyclophilin Cyp-40 and the steroid aporeceptor-associated protein p23”. Science 1996; 274: 1718–1720
  • Freeman B. C., Felts S. J., Toft D. O., Yamamoto K. R. “The p23 molecular chaperones act at a late step in intracellular receptor action to differentially affect ligand efficacies”. Genes Dev 2000; 14: 422–434
  • Glaser R. W. “Antigen-antibody binding and mass transport by convection and diffusion to a surface: a two-dimensional computer model of binding and dissociation kinetics”. Anal. Biochem 1993; 213: 152–161
  • Graumann K., Jungbauer A. “Quantitative assessment of complex formation of nuclear-receptor accessory proteins”. Biochem. J 2000; 345: 627–636
  • Grenert J. P., Johnson B. D., Toft D. O. “The importance of ATP binding and hydrolysis by hsp90 in formation and function of protein heterocomplexes”. J. Biol. Chem 1999; 274: 17525–17533
  • Heery D. M., Kalkhoven E., Hoare S., Parker M. G. “A signature motif in transcriptional co-activators mediates binding to nuclear receptors”. Nature 1997; 387: 733–736
  • Heinzel T., Lavinsky R. M., Mullen T. M., Soderstrom M., Laherty CD, Torchia J., Yang W. M., Brard G., Ngo S. D., Davie J. R., Seto E., Eisenman R. N., Rose D. W., Glass C. K., Rosenfeld M. G. “A complex containing N-CoR, mSin3 and histone deacetylase mediates transcriptional repression”. Nature 1997; 387: 43–48
  • Hill A. V. “The possible effects of aggregation of the molecules of hemoglobin on its dissociation”. J. Physiol. (Lond) 1910; iv–vii
  • Hong H., Kohli K., Garabedian M. J., Stallcup M. R. “GRIP1, a transcriptional coactivator for the AF-2 transactivation domain of steroid, thyroid, retinoid, and vitamin D receptors”. Mol. Cell Biol 1997; 17: 2735–2744
  • Horwitz K. B., Jackson T. A., Bain D. L., Richer J. K., Takimoto G. S., Tung L. “Nuclear receptor coactivators and corepressors”. Mol. Endocrinol 1996; 10: 1167–1177
  • Huang S. M., Stallcup M. R. “Mouse zacl, a transcriptional coactivator and repressor for nuclear receptors”. Mol. Cell Biol 2000; 20: 1855–1867
  • Johansson L., Bavner A., Thomsen J. S., Farnegardh M., Gustafsson J. A., Treuter E. “The orphan nuclear receptor SHP utilizes conserved LXXLL-related motifs for interactions with ligand-activated estrogen receptors”. Mol. Cell Biol 2000; 20: 1124–1133
  • Johnson J. L., Toft D. O. “Binding of p23 and hsp90 during assembly with the progesterone receptor”. Mol. Endocrinol 1995; 9: 670–678
  • Kanelakis K. C., Morishima Y., Dittmar K. D., Galigniana M. D., Takayama S., Reed J. C., Pratt W. B. “Differential effects of the hsp70-binding protein BAG-1 on glucocorticoid receptor folding by the hsp90-based chaperone machinery”. J. Biol. Chem 1999; 274: 34134–34140
  • Kazlauskas A., Poellinger L., Pongratz I. “Evidence that the co-chaperone p23 regulates ligand responsiveness of the dioxin (Aryl hydrocarbon) receptor”. J. Biol. Chem 1999; 274: 13519–13524
  • Kosano H., Stensgard B., Charlesworth M. C., McMahon N., Toft D. “The assembly of progesterone receptor-hsp90 complexes using purified proteins”. J. Biol. Chem 1998; 273: 32973–32979
  • Kraus W. L., Kadonaga J. T. “p300 and estrogen receptor cooperatively activate transcription via differential enhancement of initiation and reinitiation”. Genes Dev 1998; 12: 331–342
  • Krege J. H., Hodgin J. B., Couse J. F., Enmark E., Warner M, Mahler J. F., Sar M, Korach K. S., Gustafsson J. A., Smithies O. “Generation and reproductive phenotypes of mice lacking estrogen receptor beta”. Proc. Natl. Acad. Sci. USA 1998; 95: 15677–15682
  • Kuiper G. G., Enmark E., Pelto-Huikko M., Nilsson S., Gustafsson J. A. “Cloning of a novel receptor expressed in rat prostate and ovary”. Proc. Natl. Acad. Sci. USA 1996; 93: 5925–5930
  • Langmuir I. “The adsorption of gases on plane surfaces of glass, mica and platinum”. J. Am. Chem. Soc.M 1918; 1361–1403
  • Lavinsky R. M., Jepsen K., Heinzel T., Torchia J., Mullen T. M., Schiff R., Del-Rio A. L., Ricote M., Ngo S., Gemsch J., Hilsenbeck S. G., Osborne C. K., Glass C. K., Rosenfeld M. G., Rose D. W. “Diverse signaling pathways modulate nuclear receptor recruitment of N-CoR and SMRT complexes”. Proc. Natl. Acad. Sci. USA 1998; 95: 2920–2925
  • Lee S. K., Anzick S. L., Choi J. E., Bubendorf L., Guan X. Y., Jung Y. K., Kallioniemi O. P., Kononen J., Trent J. M., Azorsa D., Jhun B. H., Cheong J. H., Lee Y. C., Meltzer P. S., Lee J. W. “A nuclear factor ASC-2, as a cancer-amplified transcriptional coactivator essential for ligand-dependent transactivation by nuclear receptors in vivo”. J. Biol. Chem. 1999; 274: 34283–34293
  • Leo C., Chen J. D. “The SRC family of nuclear receptor coactivators”. Gene 2000; 245: 1–11
  • Leo C, Li H., Chen J. D. “Differential mechanisms of nuclear receptor regulation by receptor-associated coactivator 3”. J. Biol. Chem 2000; 275: 5976–5982
  • Li H., Gomes P. J., Chen J. D. “RAC3, a steroid/nuclear receptor-associated coactivator that is related to SRC-1 and TIF2”. Proc. Natl. Acad. Sci. USA 1997; 94: 8479–8484
  • Morishima Y., Kanelakis K., Silverstein A., Dittmar K., Estrada L., Pratt W. “The hsp organizer protein hop enhances the rate of but is not essential for glucocorticoid receptor folding by the multiprotein Hsp90-based chaperone system”. J. Biol. Chem 2000; 275: 6894–6900
  • Mosselman S., Polman J., Dijkema R. “ER beta: identification and characterization of a novel human estrogen receptor”. FEBS Lett 1996; 392: 49–53
  • Myszka D. G., He X., Dembo M., Morton T. A., Goldstein B. “Extending the range of rate constants available from BIACORE: interpreting mass transport-influenced binding data”. Biophys. J 1998; 75: 583–594
  • Norris J. D., Fan D., Stallcup M. R., McDonnell D. P. “Enhancement of estrogen receptor transcriptional activity by the coactivator GRIP-1 highlights the role of activation function 2 in determining estrogen receptor pharmacology”. J. Biol. Chem 1998; 273: 6679–6688
  • Ogawa S., Inoue S., Watanabe T., Hiroi H., Orimo A., Hosoi T, Ouchi Y., Muramatsu M. “The complete primary structure of human estrogen receptor beta (hER beta) and its heterodimerization with ER alpha in vivoin vitro”. Biochem. Biophys. Res. Commun. 1998; 243: 122–126
  • Onate S. A., Tsai S. Y., Tsai M. J., O'Malley B. W. “Sequence and characterization of a coactivator for the steroid hormone receptor superfamily”. Science 1995; 270: 1354–1357
  • O'Shannessy D. J., Winzor D. J. “Interpretation of deviations from pseudo-first-order kinetic behavior in the characterization of ligand binding by biosensor technology”. Anal. Biochem 1996; 236: 275–283
  • O'Shannessy D. J., Brigham-Burke M., Soneson K. K., Hensley P., Brooks I. “Determination of rate and equilibrium binding constants for macromolecular interactions using surface plasmon resonance: use of nonlinear least squares analysis methods”. Anal. Biochem. 1993; 212: 457–468
  • O'Shannessy D. J., Brigham-Burke M., Soneson K. K., Hensley P., Brooks I. “Determination of rate and equilibrium binding constants for macromolecular interactions by surface plasmon resonance”. Meth. Enzymol 1994; 240: 323–349
  • Prapapanich V., Chen S., Nair S. C., Rimerman R. A., Smith D. F. “Molecular cloning of human p48, a transient component of progesterone receptor complexes and an Hsp70-binding protein”. Mol Endocrinol 1996; 10: 420–431
  • Pratt W. B. “The hsp90-based chaperone system: involvement in signal transduction from a variety of hormone and growth factor receptors”. Proc. Soc. Exp. Biol. Med 1998; 217: 420–434
  • Pratt W. B., Toft D. O. “Steroid receptor interactions with heat shock protein and immunophilin chaperones”. Endocr. Rev 1997; 18: 306–360
  • Pratt W. B., Gehring U., Toft D. O. “Molecular chaperoning of steroid hormone receptors”. EXS 1996; 77: 79–95
  • Pratt W. B., Silverstein A. M., Galigniana M. D. “A model for the cytoplasmic trafficking of signalling proteins involving the hsp90-binding immunophilins and p50cdc37”. Cell Signal 1999; 11: 839–851
  • Roos H., Karlsson R., Nilshans H., Persson A. “Thermodynamic analysis of protein interactions with biosensor tehnology”. J. Mol. Recogn 1998; 11: 204–210
  • Rutherford S. L., Zuker C. S. “Protein folding and the regulation of signaling pathways”. Cell 1994; 19: 1129–1132
  • Segnitz B., Gehring U. “Subunit structure of the nonactivated human estrogen receptor”. Proc. Nad. Acad. Sci. USA 1995; 92: 2179–2183
  • Silin V., Plant A. “Biotechnological applications of surface plasmon resonance”. Tibtech 1997; 15: 353–359
  • Smith C. L., Onate S. A., Tsai M. J., O'Malley B. W. “CREB binding protein acts synergistically with steroid receptor coactivator-1 to enhance steroid receptor-dependent transcription”. Proc. Narl. Acad. Sci. USA 1996; 93: 8884–8888
  • Thénot S., Henriquet C, Rochefort H., Cavaillés V. “Differential interaction of nuclear receptors with the putative human transcriptional coactivator hTIFl”. J. Biol. Chem 1997; 272: 12062–12068
  • Tora L., White J., Brou Tasset C. D., Webster N., Scheer E., Chambon P. “The human estrogen receptor has two independent nonacidic transcriptional activation functions”. Cell 1989; 59: 477–487
  • Torehia J., Rose D. W., Inostroza J., Kamei Y., Westin S., Glass C. K., Rosenfeld M. G. “The transcriptional co-activator p/CIP binds CBP and mediates nuclear- receptor function”. Nature 1997; 387: 677–684
  • Tremblay G. B., Tremblay A., Copeland N. G., Gilbert D. J., Jenkins N. A., Labrie F., Giguére V. “Cloning, chromosomal localization, and functional analysis of the murine estrogen receptor beta”. Mol. Endocrinol 1997; 11: 353–365
  • Tremblay A., Tremblay G. B., Labrie F., Giguere V. “Ligand-independent recruitment of SRC-1 to estrogen receptor beta through phosphorylation of activation function AF-1”. Mol. Cell 1999; 3: 513–519
  • Voegel J. J., Heine M. J., Zechel Chambon C. P., Gronemeyer H. “TIF2, a 160kDa transcriptional mediator for the ligand-dependent activation function AF-2 of nuclear receptors”. Embo. J 1996; 15: 3667–3675
  • Webb P., Nguyen P., Shinsako J., Anderson Feng C. W., Nguyen M. P., Chen D., Huang S. M., Subramanian S., McKinemey E., Katzenellenbogen B. S., Stallcup M. R., Kushner P. J. “Estrogen receptor activation function 1 works by binding p160 coactivator proteins”. Mol. Endocrinol 1998; 12: 1605–1618
  • Webster N. J., Green S., Jin J. R., Chambon P. “The hormone-binding domains of the estrogen and glucocorticoid receptors contain an inducible transcription activation function”. Cell 1988; 54: 199–207

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.