8-Bromo-Cyclic AMP Induces Phosphorylation of Two Sites in SRC-1 That Facilitate Ligand-Independent Activation of the Chicken Progesterone Receptor and Are Critical for Functional Cooperation between SRC-1 and CREB Binding Protein

REFERENCES

• Abreu-Martin, M. T., Chari, A., Palladino, A. A., Craft, N. A., and Sawyers, C. L.. 1999. Mitogen-activated protein kinase kinase kinase 1 activates androgen receptor-dependent transcription and apoptosis in prostate cancer. Mol. Cell. Biol. 19:5143–5154
   PubMed Web of Science ®Google Scholar
• Ait, S. A., Carlisi, D., Ramirez, S., Upegui-Gonzalez, L. C., Duquet, A., Robin, P., Rudkin, B., Harel-Bellan, A., and Trouche, D.. 1999. Phosphorylation by p44 MAP kinase/ERK1 stimulates CBP histone acetyl transferase activity in vitro. Biochem. Biophys. Res. Commun. 262:157–162
   PubMedGoogle Scholar
• Ait, S. A., Ramirez, S., Barre, F. X., Dkhissi, F., Magnaghi-Jaulin, L., Girault, J. A., Robin, P., Knibiehler, M., Pritchard, L. L., Ducommun, B., Trouche, D., and Harel-Bellan, A.. 1998. Histone acetyltransferase activity of CBP is controlled by cycle-dependent kinases and oncoprotein E1A. Nature 396:184–186
   PubMedGoogle Scholar
• Allgood, V. E., Zhang, Y., O'Malley, B. W., and Weigel, N. L.. 1997. Analysis of chicken progesterone receptor function and phosphorylation using an adenovirus-mediated procedure for high-efficiency DNA transfer. Biochemistry 36:224–232
   PubMedGoogle Scholar
• Alnemri, E. S., Maksymowych, A. B., Robertson, N. M., and Litwack, G.. 1991. Characterization and purification of a functional rat glucocorticoid receptor overexpressed in a baculovirus system. J. Biol. Chem. 266:3925–3936
   PubMed Web of Science ®Google Scholar
• Ambrosini, A., Tininini, S., Barassi, A., Racagni, G., Sturani, E., and Zippel, R.. 2000. cAMP cascade leads to Ras activation in cortical neurons. Brain Res. Mol. Brain Res. 75:54–60
   PubMedGoogle Scholar
• Arnold, S. F., Obourn, J. D., Jaffe, H., and Notides, A. C.. 1995. Phosphorylation of the human estrogen receptor on tyrosine 537 in vivo and by src family tyrosine kinases in vitro. Mol. Endocrinol. 9:24–33
   PubMedGoogle Scholar
• Aronica, S. M., and Katzenellenbogen, B. S.. 1993. Stimulation of estrogen receptor-mediated transcription and alteration in the phosphorylation state of the rat uterine estrogen receptor by estrogen, cyclic adenosine monophosphate, and insulin-like growth factor-I. Mol. Endocrinol. 7:743–752
   PubMed Web of Science ®Google Scholar
• Bai, W., Rowan, B. G., Allgood, V. E., O'Malley, B. W., and Weigel, N. L.. 1997. Differential phosphorylation of chicken progesterone receptor in hormone-dependent and ligand-independent activation. J. Biol. Chem. 272:10457–10463
   PubMedGoogle Scholar
• Bai, W., Tullos, S., and Weigel, N. L.. 1994. Phosphorylation of Ser530 facilitates hormone-dependent transcriptional activation of the chicken progesterone receptor. Mol. Endocrinol. 8:1465–1473
   PubMedGoogle Scholar
• Bai, W., and Weigel, N. L.. 1996. Phosphorylation of Ser211 in the chicken progesterone receptor modulates its transcriptional activity. J. Biol. Chem. 271:12801–12806
   PubMedGoogle Scholar
• Barge, R. M., Falkenburg, J. H., Willemze, R., and Maassen, J. A.. 1997. 8-Bromo-cAMP induces a proliferative response in an IL-3 dependent leukemic cell line and activates Erk 1,2 via a Shc-independent pathway. Biochim. Biophys. Acta 1355:141–146
   PubMedGoogle Scholar
• Beck, C. A., Weigel, N. L., and Edwards, D. P.. 1992. Effects of hormone and cellular modulators of protein phosphorylation on transcriptional activity, DNA binding, and phosphorylation of human progesterone receptors. Mol. Endocrinol. 6:607–620
   PubMedGoogle Scholar
• Boonyaratanakornkit, V., Melvin, V., Prendergast, P., Altmann, M., Ronfani, L., Bianchi, M. E., Taraseviciene, L., Nordeen, S. K., Allegretto, E. A., and Edwards, D. P.. 1998. High-mobility group chromatin proteins 1 and 2 functionally interact with steroid hormone receptors to enhance their DNA binding in vitro and transcriptional activity in mammalian cells. Mol. Cell. Biol. 18:4471–4487
   PubMed Web of Science ®Google Scholar
• Bunone, G., Briand, P. A., Miksicek, R. J., and Picard, D.. 1996. Activation of the unliganded estrogen receptor by EGF involves the MAP kinase pathway and direct phosphorylation. EMBO J. 15:2174–2183
   PubMed Web of Science ®Google Scholar
• Castoria, G., Migliaccio, A., Green, S., Di Domenico, M., Chambon, P., and Auricchio, F.. 1993. Properties of a purified estradiol-dependent calf uterus tyrosine kinase. Biochemistry 32:1740–1750
   PubMed Web of Science ®Google Scholar
• Chawla, S., Hardingham, G. E., Quinn, D. R., and Bading, H.. 1998. CBP: a signal-regulated transcriptional coactivator controlled by nuclear calcium and CaM kinase IV. Science 281:1505–1509
   PubMedGoogle Scholar
• Cook, S. J., and McCormick, F.. 1993. Inhibition by cAMP of Ras-dependent activation of Raf. Science 262:1069–1072
   PubMed Web of Science ®Google Scholar
• Culig, Z., Hobisch, A., Hittmair, A., Cronauer, M. V., Radmayr, C., Zhang, J., Bartsch, G., and Klocker, H.. 1997. Synergistic activation of androgen receptor by androgen and luteinizing hormone-releasing hormone in prostatic carcinoma cells. Prostate 32:106–114
   PubMed Web of Science ®Google Scholar
• Dayani, N., McNaught, R. W., Shenolikar, S., and Smith, R. G.. 1990. Receptor interconversion model of hormone action. 2. Requirement of both kinase and phosphatase activities for conferring estrogen binding activity to the estrogen receptor. Biochemistry 29:2691–2698
   PubMed Web of Science ®Google Scholar
• Denner, L. A., Schrader, W. T., O'Malley, B. W., and Weigel, N. L.. 1990. Hormonal regulation and identification of chicken progesterone receptor phosphorylation sites. J. Biol. Chem. 265:16548–16555
   PubMedGoogle Scholar
• Denner, L. A., Weigel, N. L., Maxwell, B. L., Schrader, W. T., and O'Malley, B. W.. 1990. Regulation of progesterone receptor-mediated transcription by phosphorylation. Science 250:1740–1743
   PubMedGoogle Scholar
• Denton, R. R., Koszewski, N. J., and Notides, A. C.. 1992. Estrogen receptor phosphorylation. Hormonal dependence and consequence on specific DNA binding. J. Biol. Chem. 267:7263–7268
   PubMedGoogle Scholar
• Font de Mora, J., and Brown, M.. 2000. AIB1 is a conduit for kinase-mediated growth factor signaling to the estrogen receptor. Mol. Cell. Biol. 20:5041–5047
   PubMedGoogle Scholar
• Gao, Z., Chen, T., Weber, M. J., and Linden, J.. 1999. A2B adenosine and P2Y2 receptors stimulate mitogen-activated protein kinase in human embryonic kidney-293 cells. Cross-talk between cyclic AMP and protein kinase C pathways. J. Biol. Chem. 274:5972–5980
   PubMed Web of Science ®Google Scholar
• Han, X. B., and Conn, P. M.. 1999. The role of protein kinases A and C pathways in the regulation of mitogen-activated protein kinase activation in response to gonadotropin-releasing hormone receptor activation. Endocrinology 140:2241–2251
   PubMed Web of Science ®Google Scholar
• Heery, D. M., Kalkhoven, E., Hoare, S., and Parker, M. G.. 1997. A signature motif in transcriptional co-activators mediates binding to nuclear receptors. Nature 387:733–736
   PubMed Web of Science ®Google Scholar
• Hong, S. H., Wong, C. W., and Privalsky, M. L.. 1998. Signaling by tyrosine kinases negatively regulates the interaction between transcription factors and SMRT (Silencing Mediator of Retinoic acid and Thyroid hormone receptor) corepressor. Mol. Endocrinol. 12:1161–1171
   PubMedGoogle Scholar
• Hu, J. M., Bodwell, J. E., and Munck, A.. 1997. Control by basal phosphorylation of cell cycle-dependent, hormone-induced glucocorticoid receptor hyperphosphorylation. Mol. Endocrinol. 11:305–311
   PubMedGoogle Scholar
• Ikonen, T., Palvimo, J. J., Kallio, P. J., Reinikainen, P., and Janne, O. A.. 1994. Stimulation of androgen-regulated transactivation by modulators of protein phosphorylation. Endocrinology 135:1359–1366
   PubMed Web of Science ®Google Scholar
• Janknecht, R., and Nordheim, A.. 1996. MAP kinase-dependent transcriptional coactivation by Elk-1 and its cofactor CBP. Biochem. Biophys. Res. Commun. 228:831–837
   PubMed Web of Science ®Google Scholar
• Janknecht, R., and Nordheim, A.. 1996. Regulation of the c-fos promoter by the ternary complex factor Sap-1a and its coactivator CBP. Oncogene 12:1961–1969
   PubMed Web of Science ®Google Scholar
• Jenster, G., Spencer, T. E., Burcin, M. M., Tsai, S. Y., Tsai, M. J., and O'Malley, B. W.. 1997. Steroid receptor induction of gene transcription—a two step model. Proc. Natl. Acad. Sci. USA 94:7879–7884
   PubMedGoogle Scholar
• Kato, S., Endoh, H., Masuhiro, Y., Kitamoto, T., Uchiyama, S., Sasaki, H., Masushige, S., Gotoh, Y., Nishida, E., Kawashima, H., Metzger, D., and Chambon, P.. 1995. Activation of the estrogen receptor through phosphorylation by mitogen-activated protein kinase. Science 270:1491–1494
   PubMed Web of Science ®Google Scholar
• Kazmi, S. M., Visconti, V., Plante, R. K., Ishaque, A., and Lau, C.. 1993. Differential regulation of human progesterone receptor A and B form-mediated trans-activation by phosphorylation. Endocrinology 133:1230–1238
   PubMedGoogle Scholar
• Krstic, M. D., Rogatsky, I., Yamamoto, K. R., and Garabedian, M. J.. 1997. Mitogen-activated and cyclin-dependent protein kinases selectively and differentially modulate transcriptional enhancement by the glucocorticoid receptor. Mol. Cell. Biol. 17:3947–3954
   PubMed Web of Science ®Google Scholar
• Lange-Carter, C. A., and Johnson, G. L.. 1994. Ras-dependent growth factor regulation of MEK kinase in PC12 cells. Science 265:1458–1461
   PubMed Web of Science ®Google Scholar
• Lavinsky, R. M., Jepsen, K., Heinzel, T., Torchia, J., Mullen, T. M., Schiff, R., Delrio, A. L., Ricote, M., Ngo, S., Gemsch, J., Hilsenbeck, S. G., Osborne, C. K., Glass, C. K., Rosenfeld, M. G., and Rose, D. W.. 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
• Liu, Y. Z., Chrivia, J. C., and Latchman, D. S.. 1998. Nerve growth factor up-regulates the transcriptional activity of CBP through activation of the p42/p44(MAPK) cascade. J. Biol. Chem. 273:32400–32407
   PubMedGoogle Scholar
• Liu, Y. Z., Thomas, N. S., and Latchman, D. S.. 1999. CBP associates with the p42/p44 MAPK enzymes and is phosphorylated following NGF treatment. Neuroreport 10:1239–1243
   PubMedGoogle Scholar
• Massaad, C., Houard, N., Lombes, M., and Barouki, R.. 1999. Modulation of human mineralocorticoid receptor function by protein kinase A. Mol. Endocrinol. 13:57–65
   PubMedGoogle Scholar
• McKenna, N. J., Lanz, R. B., and O'Malley, B. W.. 1999. Nuclear receptor coregulators: cellular and molecular biology. Endocr. Rev. 20:321–344
   PubMed Web of Science ®Google Scholar
• McKenna, N. J., Nawaz, Z., Tsai, S. Y., Tsai, M. J., and O'Malley, B. W.. 1998. Distinct steady-state nuclear receptor coregulator complexes exist in vivo. Proc. Natl. Acad. Sci. USA 95:11697–11702
   PubMed Web of Science ®Google Scholar
• Nazareth, L. V., and Weigel, N. L.. 1996. Activation of the human androgen receptor through a protein kinase A signaling pathway. J. Biol. Chem. 271:19900–19907
   PubMed Web of Science ®Google Scholar
• Nordeen, S. K., Moyer, M. L., and Bona, B. J.. 1994. The coupling of multiple signal transduction pathways with steroid response mechanisms. Endocrinology 134:1723–1732
   PubMed Web of Science ®Google Scholar
• Onate, S. A., Boonyaratanakornkit, V., Spencer, T. E., Tsai, S. Y., Tsai, M. J., Edwards, D. P., and O'Malley, B. W.. 1998. The steroid receptor coactivator-1 contains multiple receptor interacting and activation 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
• Onate, S. A., Tsai, S. Y., Tsai, M. J., and O'Malley, B. W.. 1995. Sequence and characterization of a coactivator for the steroid hormone receptor superfamily. Science 270:1354–1357
   PubMed Web of Science ®Google Scholar
• Parameswaran, N., Disa, J., Spielman, W. S., Brooks, D. P., Nambi, P., and Aiyar, N.. 2000. Activation of multiple mitogen-activated protein kinases by recombinant calcitonin gene-related peptide receptor. Eur. J. Pharmacol. 389:125–130
   PubMedGoogle Scholar
• Poletti, A., and Weigel, N. L.. 1993. Identification of a hormone-dependent phosphorylation site adjacent to the DNA-binding domain of the chicken progesterone receptor. Mol. Endocrinol. 7:241–246
   PubMedGoogle Scholar
• Rowan, B. G., Weigel, N. L., and O'Malley, B. W.. 2000. Phosphorylation of steroid receptor coactivator-1. Identification of the phosphorylation sites and phosphorylation through the mitogen-activated protein kinase pathway. J. Biol. Chem. 275:4475–4483
   PubMed Web of Science ®Google Scholar
• Smith, C. L., Onate, S. A., Tsai, M. J., and O'Malley, B. W.. 1996. CREB binding protein acts synergistically with steroid receptor coactivator-1 to enhance steroid receptor-dependent transcription. Proc. Natl. Acad. Sci. USA 93:8884–8888
   PubMed Web of Science ®Google Scholar
• Spencer, T. E., Jenster, G., Burcin, M. M., Allis, C. D., Zhou, J. X., Mizzen, C. A., McKenna, N. J., Onate, S. A., Tsai, S. Y., Tsai, M. J., and O'Malley, B. W.. 1997. Steroid receptor coactivator-1 is a histone acetyltransferase. Nature 389:194–198
   PubMed Web of Science ®Google Scholar
• Torchia, J., Rose, D. W., Inostroza, J., Kamei, Y., Westin, S., Glass, C. K., and Rosenfeld, M. G.. 1997. The transcriptional co-activator p/CIP binds CBP and mediates nuclear-receptor function. Nature 387:677–684
   PubMed Web of Science ®Google Scholar
• Wagner, B. L., Norris, J. D., Knotts, T. A., Weigel, N. L., and McDonnell, D. P.. 1998. The nuclear corepressors NCoR and SMRT are key regulators of both ligand- and 8-bromo-cyclic AMP-dependent transcriptional activity of the human progesterone receptor. Mol. Cell. Biol. 18:1369–1378
   PubMed Web of Science ®Google Scholar
• Webster, J., Prager, D., and Melmed, S.. 1994. Insulin-like growth factor-1 activation of extracellular signal-related kinase-1 and -2 in growth hormone-secreting cells. Mol. Endocrinol. 8:539–544
   PubMedGoogle Scholar
• Webster, J. C., Jewell, C. M., Bodwell, J. E., Munck, A., Sar, M., and Cidlowski, J. A.. 1997. Mouse glucocorticoid receptor phosphorylation status influences multiple functions of the receptor protein. J. Biol. Chem. 272:9287–9293
   PubMed Web of Science ®Google Scholar
• Weigel, N. L.. 1996. Steroid hormone receptors and their regulation by phosphorylation. Biochem. J. 319:657–667
   PubMed Web of Science ®Google Scholar
• West, M. H. P., Wu, R. S., and Bonner, W. M.. 1984. Polyacrylamide gel electrophoresis of small peptides. Electrophoresis 5:133–138
   Google Scholar
• Xu, L., Lavinsky, R. M., Dasen, J. S., Flynn, S. E., McInerney, E. M., Mullen, T. M., Heinzel, T., Szeto, D., Korzus, E., Kurokawa, R., Aggarwal, A. K., Rose, D. W., Glass, C. K., and Rosenfeld, M. G.. 1998. Signal-specific co-activator domain requirements for Pit-1 activation. Nature 395:301–306
   PubMedGoogle Scholar
• Yeh, S., Lin, H. K., Kang, H. Y., Thin, T. H., Lin, M. F., and Chang, C.. 1999. From HER2/Neu signal cascade to androgen receptor and its coactivators: a novel pathway by induction of androgen target genes through MAP kinase in prostate cancer cells. Proc. Natl. Acad. Sci. USA 96:5458–5463
   PubMed Web of Science ®Google Scholar
• Zanger, K., Cohen, L. E., Hashimoto, K., Radovick, S., and Wondisford, F. E.. 1999. A novel mechanism for cyclic adenosine 3′,5′-monophosphate regulation of gene expression by CREB-binding protein. Mol. Endocrinol. 13:268–275
   PubMedGoogle Scholar
• 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
   PubMedGoogle Scholar