E1A-mediated repression of progesterone receptor-dependent transactivation involves inhibition of the assembly of a multisubunit coactivation complex

Molecular and Cellular Biology

Volumn 20, Issue 6, 2000, Pages 2138-2146

  Xu, Yue ^a   Klein Hitpass, Ludger ^b   Bagchi, Milan K ^a  

^a ROCKEFELLER UNIVERSITY   (United States)

^b UNIVERSITY HOSPITAL ESSEN   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

CYCLIC AMP RESPONSIVE ELEMENT BINDING PROTEIN; HISTONE ACETYLTRANSFERASE; PROGESTERONE; PROGESTERONE RECEPTOR; STEROID RECEPTOR COACTIVATOR 1;

ARTICLE; CHROMATIN STRUCTURE; DNA SEQUENCE; DNA TEMPLATE; GENE ACTIVATION; HUMAN; HUMAN CELL; NUCLEOSOME; PRIORITY JOURNAL; PROMOTER REGION; PROTEIN ASSEMBLY; RNA SYNTHESIS; TRANSACTIVATION; TRANSCRIPTION INITIATION; TRANSCRIPTION REGULATION;

ADENOVIRUS E1A PROTEINS; HISTONE ACETYLTRANSFERASES; HUMANS; PROGESTERONE; PROTEIN BINDING; RECEPTORS, PROGESTERONE; SIGNAL TRANSDUCTION; TRANS-ACTIVATION (GENETICS); TRANSCRIPTION FACTORS; TUMOR CELLS, CULTURED;

EID: 0033999611     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.20.6.2138-2146.2000     Document Type: Article

References (63)

1. 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 P. S. Meltzer. 1997. AIB1, a steroid receptor coactivator amplified in breast and ovarian cancer. Science 277:965-968.
2. Arany, Z., D. Newsome, E. Oldread, D. M. Livingston, and R. Eckner. 1995. A family of transcriptional adaptor proteins targeted by the E1A oncoprotein. Nature 374:81-84.
3. Bagchi, M. K., S. Y. Tsai, M.-J. Tsai, and B. W. O'Malley. 1990. Identification of a functional intermediate in receptor activation in progesterone-dependent cell-free transcription. Nature 345:547-550.
4. Bagchi, M. K., S. Y. Tsai, N. L. Weigel, M.-J. Tsai, and B. W. O'Malley. 1990. Regulation of in vitro transcription by progesterone receptor: characterization and kinetic studies. J. Biol. Chem. 265:5129-5134.
5. Bannister, A. J., and T. Kouzarides. 1996. The CBP coactivator is a histoneacetyl transferase. Nature 384:641-643.
6. Baulieu, E. E. 1989. Contragestion and other clinical applications of RU486, an antiprogesterone at the receptor. Science 245:1351-1357.
7. Beato, M., P. Herrlich, and G. Schutz. 1995. Steroid hormone receptors: many actors in search of a plot. Cell 83:851-857.
8. Blanco, J., S. Minucci, J. Lu, X.-J. Yang, K. K. Walker, H. Chen, R. M. Evans, Y. Nakatani, and K. Ozato. 1998. The histone acetylase PCAF is a nuclear receptor coactivator. Genes Dev. 12:1638-1651.
9. Bocquel, M. T., V. Kumar, C. Stricker, P. Chambon, and H. Gronemeyer. 1989. The contribution of N- and C-terminal regions of steroid receptors to activation of transcription is both receptor and cell-specific. Nucleic Acids Res. 17:2581-2595.
10. Chakravarti, D., V.J. LaMorte, M. C. Nelson, T. Nakajima, I. G. Schulman, H. Juguilon, M. Montminy, and R. M. Evans. 1996. Role of CBP/P300 in nuclear receptor signalling. Nature 383:99-103.
11. Chakravarti, U., V. Ogryzko, H.-Y. Kao, A. Nash, H. Chen, Y. Nakatani, and R. M. Evans. 1999. A viral mechanism for inhibition of p300 and PCAF acetyl transferase activity. Cell 96:393-404.
12. Chen, H., R. J. Lin, R. L. Schultz, D. Chakravarty, A. Nash, L. Nagy, M. L. Privalsky, Y. Nakatani, and R. M. 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.
13. Clarke, C. L., and R. L. Sutherland. 1990. Progestin regulation of cellular proliferation. Endocrine Rev. 11:266-300.
14. Danielian, P. S., R. White, J. A. Lees, and M. G. Parker. 1992. Identification of a conserved region required for hormone dependent transcriptional activation by steroid hormone receptors. EMBO J. 11:1025-1033.
15. Darimont, B. D., R. L. Wagner, J. W. Apriletti, M. R. Stallcup, P. J. Kushner, J. D. Baxter, R. J. Fletterick, and K. R. Yamamoto. 1998. Structure and specificity of nuclear receptor-coactivator interactions. Genes Dev. 12:3343-3356.
16. Denner, L. A., N. L. Weigel, B. L. Maxwell, W. T. Schrader, and B. W. O'Malley. 1990. Regulation of progesterone receptor-mediated transcription by phosphorylation. Science 250:1740-1743.
17. Dyson, N., and E. Harlow. 1992. Adenovirus E1A targets key regulators of cell proliferation. Cancer Surv. 12:161-195.
18. Eckner, R., M. E. Ewen, D. Newsome, M. Gerdes, J. A. DeCaprio, J. B. Lawrence, and D. M. Livingston. 1994. Molecular cloning and functional analysis of the adenovirus E1A-associated 300-kD protein (p300) reveals a protein with properties of a transcriptional adaptor. Genes Dev. 8:869-884.
19. Fondell, J. D., H. Ge, and R. G. Roeder. 1996. Ligand induction of a transcriptionally active thyroid hormone receptor coactivator complex. Proc. Natl. Acad. Sci. USA 93:8323-8333.
20. Freedman, L. P. 1999. Increasing the complexity of coactivation in nuclear receptor signaling. Cell 97:5-8.
21. Heery, D. M., E. Kalkhoven, S. Hoare, and M. G. Parker. 1997. A signature motif in transcriptional coactivators mediates binding to nuclear receptors. Nature 387:733-736.
22. Hong, H., K. Kohli, A. Trivedi, D. L. Johnson, and M. R. Stallcup. 1996. GRIP1. A novel mouse protein that serves as a transcriptional coactivator in yeast for the hormone binding domains of steroid receptors. Proc. Natl. Acad. Sci. USA 93:4948-4952.
23. Horwitz, K. B., and P. S. Alexander. 1983. In situ photolinked nuclear progesterone receptors of human breast cancer cells: subunit molecular weights after transformation and translocation. Endocrinology 113:2195-2201.
24. Horwitz, K. B., T. A. Jackson, D. L. Bain, J. K. Richer, G. S. Takimoto, and L. Tung. 1996. Nuclear receptor coactivators and corepressors. Mol. Endocrinol. 10:1167-1177.
25. Imhof, A., X.-J. Yang, V. Ogryzko, Y. Nakatani, A. P. Wolff, and H. Ge. 1997. Acetylation of general transcription factors by histone acetyltransferases. Curr. Biol. 7:689-692.
26. 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 M. G. Rosenfeld. 1996. A CBP integrator complex mediates transcriptional activation and AP-1 inhibition by nuclear receptors. Cell 85:403-414.
27. Klein-Hitpass, L., S. Y. Tsai, N. L. Weigel, G. A. Allan, D. Riley, R. Rodriguez, W. T. Schrader, M.-J. Tsai, and B. W. O'Malley. 1990. The progesterone receptor stimulates cell-free transcription by enhancing the formation of a stable pre-initiation complex. Cell 60:247-257.
28. Klotzbucher, M., C. Schwerk, B. Holewa, and L. Klein-Hitpass. 1997. Activation of transcription by progesterone receptor involves derepression of activation functions by a cofactor. Mol. Endocrinol. 11:768-778.
29. Korzus, E., J. Torchia, D. W. Rose, L. Xu, R. Kurokawa, E. M. McInerney, T.-M. Mullen, C. K. Glass, and M. G. Rosenfeld. 1998. Transcription factor-specific requirements for coactivators and their acetyltransferase functions. Science 279:703-707.
30. Kraus, W. L., and J. T. Kadonaga. 1998. p300 and estrogen receptor cooperatively activate transcription via differential enhancement of initiation and reinitiation. Genes Dev. 12:331-342.
31. Kurokawa, R., D. Kalafus, M.-H. Ogliastro, C. Kioussi, L. Xu, J. Torchia, M. G. Rosenfeld, and C. K. Glass. 1998. Differential use of CREB binding protein-coactivator complexes. Science 279:700-703.
32. Kwok, R. P. S., J. R. Lundland, J. C. Chrivia, J. P. Richards, H. P. Bachinger, R. G. Brennan, S. G. E. Roberts, M. R. Green, and R. H. Goodman. 1994. Nuclear protein CBP is a coactivator for the transcription factor CREB. Nature 370:223-226.
33. Li, H., P. J. Gomes, and J. D. Chen. 1997. RAC3, a steroid/nuclear receptor-associated coactivator that is related to SRC-1 and TIF2. Proc. Natl. Acad. Sci. USA 94:8479-8484.
34. Liu, Z., J. Wong, S. Y. Tsai, M.-J. Tsai, and B. W. O'Malley. 1999. Steroid receptor coactivator-1 (SRC-1) enhances ligand-dependent and receptor-dependent cell-free transcription of chromatin. Proc. Natl. Acad. Sci. USA 96:9485-9490.
35. Lydon, J. P., F. J. DeMayo, C. R. Funk, S. K. Mani, A. R. Hughes, C. A. Montgomery, G. Shyamala, O. M. Conneely, and B. W. O'Malley. 1995. Mice lacking progesterone receptor exhibit pleiotropic reproductive abnormalities. Genes Dev. 9:2266-2278.
36. McInerney, E. M., D. W. Rose, S. E. Flynn, S. Westin, T.-M. Mullen, A. Krones, J. Inostroza, R. T. Nolte, N. Assa-Munt, M. V. Milburn, C. K. Glass, and M. G. Rosenfeld. 1998. Determinants of coactivator LXXLL motif specificity in nuclear receptor transcriptional activation. Genes Dev. 12: 3357-3368.
37. McKenna, N. J., Z. Nawaz, S. Y. Tsai, M.-J. Tsai, and B. W. O'Malley. 1998. Distinct steady-state nuclear receptor coregulator complexes exist in vivo. Proc. Natl. Acad. Sci. USA 95:11697-11702.
38. Meyer, M. E., A. Pornon, J. Ji, M. T. Bocquel, P. Chambon, and H. Gronemeyer. 1990. Agonistic and antagonistic activities of RU486 on the functions of the human progesterone receptor. EMBO J. 9:3923-3932.
39. Moran, E. 1993. DNA tumor virus transforming proteins and the cell cycle. Curr. Opin. Genet. Dev. 3:63-70.
40. Nakajima, T., C. Uchida, S. F. Anderson, C.-G. Lee, J. Hurwitz, J. D. Parvin, and M. Montminy. 1997. RNA helicase A mediates association of CBP with RNA polymerase II. Cell 90:1107-1112.
41. Nakajima, T., C. Uchida, S. F. Anderson, J. D. Parvin, and M. Montminy. 1997. Analysis of a cAMP-responsive activator reveals a two component mechanism for transcriptional induction via signal dependent factors. Genes Dev. 11:738-743.
42. Ogryzko, V. V., T. Kotani, X. Zhang, R. L. Schlitz, T. Howard, X.-J. Yang, B. H. Howard, J. Qin, and Y. Nakatani. 1998. Histone-like TAFs within the PCAF histone acetyl transferase complex. Cell 94:35-44.
43. Ogryzko, V. V., R. L. Schlitz, V. Russanova, B. H. Howard, and Y. Nakatani. 1996. The transcription coactivators p300 and CBP are histone acetyltransferase. Cell 87:953-959.
44. Onate, S. A., S. Y. Tsai, M.-J. Tsai, and B. W. O'Malley. 1995. Sequence and characterization of a coactivator for the steroid hormone receptor superfamily. Science 270:1354-1357.
45. Rachez, C., B. D. Lemon, Z. Suldan, V. Bromleigh, M. Gamble, A. M. Naar, H. Erdjument-Bromage, P. Tempst, and L. P. Freedman. 1999. Ligand-dependent transactivation by nuclear receptors requires the DRIP complex. Nature 398:824-828.
46. Sartorius, C. A., M. Y. Melville, A. R. Hovland, L. Tung, G. S. Takimoto, and K. B. Horwitz. 1994. A third transactivation function (AF3) of human progesterone receptors located in the unique N-terminal segment of the B isoform. Mol. Endocrinol. 8:1347-1360.
47. Smith, C. L., Z. Nawaz, and B. W. O'Malley. 1997. Coactivator and corepressor regulation of the agonist/antagonist activity of the mixed antiestrogen, 4-hydroxytamoxifen. Mol. Endocrinol. 11:657-666.
48. 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 B. W. O'Malley. 1997. Steroid receptor coactivator-1 is a histone acetyltransferase. Nature 389:194-198.
49. Strauss, J. F., and E. Gurpide. 1991. The endometrium: regulation and dysfunction, p. 309-357. In S. S. C. Yen and R. B. Jaffe (ed.), Reproductive endocrinology: physiology, pathophysiology, and clinical management. W. B. Saunders Co., Philadelphia, Pa.
50. Struhl, K. 1998. Histone acetylation and transcriptional regulatory mechanisms. Genes Dev. 12:599-606.
51. Tong, G.-X., M. Jeyakumar, M. R. Tanen, and M. K. Bagchi. 1996. Transcriptional silencing by unliganded thyroid hormone receptor β requires a soluble corepressor that interacts with the ligand-binding domain of the receptor. Mol. Cell. Biol. 16:1909-1920.
52. Torchia, J., D. W. Rose, J. Inostroza, Y. Kamei, S. Westin, C. K. Glass, and M. G. Rosenfeld. 1997. The transcriptional coactivator p/CIP binds CBP and mediates nuclear receptor function. Nature 387:677-684.
53. Tremblay, A., G. B. Tremblay, F. Labrie, and V. Giguere. 1999. Ligand-independent recruitment of SRC-1 to estrogen receptor β through phosphorylation of activation function AF-1. Cell 3:513-520.
54. Tsai, M.-J., and B. W. O'Malley. 1994. Molecular mechanisms of action of steroid/thyroid receptor superfamily members. Annu. Rev. Biochem. 63: 451-486.
55. Tzukerman, M. T., A. Esty, D. Santiso-Mere, P. Danielian, M. G. Parker, R. B. Stein, J. W. Pike, and D. P. McDonnell. 1994 Human estrogen receptor transactivational capacity is determined by both cellular and promoter context and mediated by two functionally distinct intramolecular regions. Mol. Endocrinol. 8:21-29.
56. Vegeto, E., M. M. Shahbaz, D. X. Wen, M. E. Goldman, B. W. O'Malley, and D. P. McDonnell. 1993. Human progesterone receptor A form is a cell- and promoter-specific repressor of human progesterone receptor B function. Mol. Endocrinol. 7:1244-1255.
57. Vidal, M., and R. F. Gaber. 1991. RPD3 encodes a second factor required to achieve maximum positive and negative transcriptional states in Saccharomyces cerevisiae. Mol. Cell. Biol. 11:6317-6327.
58. Voegel, J. J., M. J. S. Heine, C. Zechel, P. Chambon, and H. Gronemeyer. 1996. TIF2, a 160kDa transcriptional mediator for the ligand-dependent activation function AF-2 of nuclear receptors. EMBO J. 15:3667-3675.
59. 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 P. J. Kushner. 1998. Estrogen receptor activation function 1 works by binding p 160 coactivator proteins. Mol. Endocrinol. 12:1605-1618.
60. Xu, J., Y. Qiu, F. J. DeMayo, S. Y. Tsai, M.-J. Tsai, and B. W. O'Malley. 1998. Partial hormone resistance in mice with disruption of the steroid receptor coactivator-1 gene. Science 279:1922-1925.
61. Yang, X.-J., V. V. Ogryzko, J. Nishikawa, B. H. Howard, and Y. A. Nakatani. 1996. p300/CBP-associated factor that competes with the adenoviral oncoprotein E1A. Nature 382:319-324.
62. Yao, T.-P., G. Ku, N. Zhou, R. Scully, and D. M. Livingston. 1996. The nuclear hormone receptor coactivator SRC-1 is a specific target of p300. Proc. Natl. Acad. Sci. USA 93:10626-10631.
63. Zhang, X., M. Jeyakumar, and M. K. Bagchi. 1996. Ligand-dependent cross-talk between steroid and thyroid hormone receptors. J. Biol. Chem. 271: 14825-14833.