Mutation of Serines 104, 106, and 118 Inhibits Dimerization of the Human Estrogen Receptor in Yeast

References

• Evans R. M. The steroid and thyroid hormone receptor superfamily. Science 1988; 240(4854)889–895
   PubMed Web of Science ®Google Scholar
• Kumar V., Green S., Stack G., Berry M., Jin J. R., Chambon P. Functional domains of the human estrogen receptor. Cell 1987; 51(6)941–951
   PubMed Web of Science ®Google Scholar
• Tora L., White J., Brou C., Tasset D., Webster N., Scheer E., Chambon P. The human estrogen receptor has two independent nonacidic transcriptional activation functions. Cell 1989; 59(3)477–487
   PubMed Web of Science ®Google Scholar
• Pham T. A., Hwung Y. P., Santiso‐Mere D., McDonnell D. P., O'Malley B. W. Ligand‐dependent and ‐independent function of the transactivation regions of the human estrogen receptor in yeast. Mol Endocrinol 1992; 6(7)1043–1050
   PubMedGoogle Scholar
• Tzukerman M. T., Esty A., Santiso‐Mere D., Danielian P., Parker M. G., Stein R. B., Pike J. W., McDonnell D. P. Human estrogen receptor transactivational capacity is determined by both cellular and promoter context and mediated by two functionally distinct intramolecular regions. Mol Endocrinol 1994; 8(1)21–30
   PubMedGoogle Scholar
• Graumann K., Jungbauer A. Quantitative assessment of complex formation of nuclear‐receptor accessory proteins. Biochem J 2000; 345(Pt 3)627–636
   PubMedGoogle Scholar
• 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(4)420–434
   PubMedGoogle Scholar
• Pratt W. B., Toft D. O. Steroid receptor interactions with heat shock protein and immunophilin chaperones. Endocr Rev 1997; 18(3)306–360
   PubMed Web of Science ®Google Scholar
• Kumar V., Chambon P. The estrogen receptor binds tightly to its responsive element as a ligand‐induced homodimer. Cell 1988; 55(1)145–156
   PubMed Web of Science ®Google Scholar
• Elliston J. F., Fawell S. E., Klein‐Hitpass L., Tsai S. Y., Tsai M. J., Parker M. G., O'Malley B. W. Mechanism of estrogen receptor‐dependent transcription in a cell‐free system. Mol Cell Biol 1990; 10(12)6607–6612
   PubMedGoogle Scholar
• Ing N. H., Beekman J. M., Tsai S. Y., Tsai M. J., O'Malley B. W. Members of the steroid hormone receptor superfamily interact with TFIIB (S300‐II). J Biol Chem 1992; 267(25)17617–17623
   PubMedGoogle Scholar
• Robyr D., Wolffe A. P., Wahli W. Nuclear hormone receptor coregulators in action: diversity for shared tasks. Mol Endocrinol 2000; 14(3)329–347
   PubMedGoogle Scholar
• Ali S., Metzger D., Bornert J. M., Chambon P. Modulation of transcriptional activation by ligand‐dependent phosphorylation of the human oestrogen receptor A/B region. Embo J 1993; 12(3)1153–1160
   PubMed Web of Science ®Google Scholar
• Le Goff P., Montano M. M., Schodin D. J., Katzenellenbogen B. S. Phosphorylation of the human estrogen receptor. Identification of hormone‐regulated sites and examination of their influence on transcriptional activity. J Biol Chem 1994; 269(6)4458–4466
   PubMed Web of Science ®Google Scholar
• Castano E., Chen C. W., Vorojeikina D. P., Notides A. C. The role of phosphorylation in human estrogen receptor function. J Steroid Biochem Mol Biol 1998; 65(1–6)101–110
   PubMedGoogle Scholar
• Chevray P. M., Nathans D. Protein interaction cloning in yeast: identification of mammalian proteins that react with the leucine zipper of Jun. Proc Natl Acad Sci USA 1992; 89(13)5789–5793
   PubMedGoogle Scholar
• Lyttle C. R., Damian‐Matsumura P., Juul H., Butt T. R. Human estrogen receptor regulation in a yeast model system and studies on receptor agonists and antagonists. J Steroid Biochem Mol Biol 1992; 42(7)677–685
   PubMedGoogle Scholar
• Wang H., Peters G. A., Zeng X., Tang M., Ip W., Khan S. A. Yeast two‐hybrid system demonstrates that estrogen receptor dimerization is ligand‐dependent in vivo. J Biol Chem 1995; 270(40)23322–23329
   PubMedGoogle Scholar
• Sheeler C. Q., Dudley M. W., Khan S. A. Environmental estrogens induce transcriptionally active estrogen receptor dimers in yeast: activity potentiated by the coactivator RIP140. Environ Health Perspect 2000; 108(2)97–103
   PubMedGoogle Scholar
• Lahooti H., White R., Danielian P. S., Parker M. G. Characterization of ligand‐dependent phosphorylation of the estrogen receptor. Mol Endocrinol 1994; 8(2)182–188
   PubMedGoogle Scholar
• Denton R. R., Koszewski N. J., Notides A. C. Estrogen receptor phosphorylation. Hormonal dependence and consequence on specific DNA binding. J Biol Chem 1992; 267(11)7263–7268
   PubMedGoogle Scholar
• Bunone G., Briand P. A., Miksicek R. J., Picard D. Activation of the unliganded estrogen receptor by EGF involves the MAP kinase pathway and direct phosphorylation. Embo J 1996; 15(9)2174–2183
   PubMed Web of Science ®Google Scholar
• Chen D., Pace P. E., Coombes R. C., Ali S. Phosphorylation of human estrogen receptor alpha by protein kinase A regulates dimerization. Mol Cell Biol 1999; 19(2)1002–1015
   PubMedGoogle Scholar
• Arnold S. F., Obourn J. D., Yudt M. R., Carter T. H., Notides A. C. In vivo and in vitro phosphorylation of the human estrogen receptor. J Steroid Biochem Mol Biol 1995; 52(2)159–171
   PubMedGoogle Scholar
• Chen D., Riedl T., Washbrook E., Pace P. E., Coombes R. C., Egly J. M., Ali S. Activation of estrogen receptor alpha by S118 phosphorylation involves a ligand‐dependent interaction with TFIIH and participation of CDK7 [In Process Citation]. Mol Cell 2000; 6(1)127–137
   PubMed Web of Science ®Google Scholar
• Dudley M. W., Sheeler C. Q., Wang H., Khan S. Activation of the human estrogen receptor by the antiestrogens ICI 182,780 and tamoxifen in yeast genetic systems: implications for their mechanism of action. Proc Natl Acad Sci USA 2000; 97(7)3696–3701
   PubMedGoogle Scholar
• Joel P. B., Traish A. M., Lannigan D. A. Estradiol and phorbol ester cause phosphorylation of serine 118 in the human estrogen receptor. Mol Endocrinol 1995; 9(8)1041–1052
   PubMed Web of Science ®Google Scholar
• Joel P. B., Traish A. M., Lannigan D. A. Estradiol‐induced phosphorylation of serine 118 in the estrogen receptor is independent of p42/p44 mitogen‐activated protein kinase. J Biol Chem 1998; 273(21)13317–13323
   PubMed Web of Science ®Google Scholar
• Kato S., Endoh H., Masuhiro Y., Kitamoto T., Uchiyama S., Sasaki H., Masushige S., Gotoh Y., Nishida E., Kawashima H., Metzger D., Chambon P. Activation of the estrogen receptor through phosphorylation by mitogen‐activated protein kinase. Science 1995; 270(5241)1491–1494
   PubMed Web of Science ®Google Scholar
• Bi R., Broutman G., Foy M. R., Thompson R. F., Baudry M. The tyrosine kinase and mitogen‐activated protein kinase pathways mediate multiple effects of estrogen in hippocampus. Proc Natl Acad Sci USA 2000; 97(7)3602–3607
   PubMed Web of Science ®Google Scholar
• Migliaccio A., Di Domenico M., Castoria G., de Falco A., Bontempo P., Nola E., Auricchio F. Tyrosine kinase/p21ras/MAP‐kinase pathway activation by estradiol‐ receptor complex in MCF‐7 cells. Embo J 1996; 15(6)1292–1300
   PubMedGoogle Scholar
• Song R. X., McPherson R. A., Adam L., Bao Y., Shupnik M., Kumar R., Santen R. J. Linkage of rapid estrogen action to MAPK activation by ERalpha‐Shc association and Shc pathway activation. Mol Endocrinol 2002; 16(1)116–127
   PubMedGoogle Scholar
• Wade C. B., Robinson S., Shapiro R. A., Dorsa D. M. Estrogen receptor (ER)alpha and ERbeta exhibit unique pharmacologic properties when coupled to activation of the mitogen‐activated protein kinase pathway. Endocrinology 2001; 142(6)2336–2342
   PubMedGoogle Scholar
• Arnold S. F., Obourn J. D., Jaffe H., Notides A. C. Serine 167 is the major estradiol‐induced phosphorylation site on the human estrogen receptor. Mol Endocrinol 1994; 8(9)1208–1214
   PubMedGoogle Scholar
• Castano E., Vorojeikina D. P., Notides A. C. Phosphorylation of serine‐167 on the human oestrogen receptor is important for oestrogen response element binding and transcriptional activation. Biochem J 1997; 326(Pt 1)149–157
   PubMedGoogle Scholar
• Pocuca N., Ruzdijic S., Demonacos C., Kanazir D., Krstic‐Demonacos M. Using yeast to study glucocorticoid receptor phosphorylation. J Steroid Biochem Mol Biol 1998; 66(5–6)303–318
   PubMedGoogle Scholar
• Poletti A., Conneely O. M., McDonnell D. P., Schrader W. T., O'Malley B. W., Weigel N. L. Chicken progesterone receptor expressed in Saccharomyces cerevisiae is correctly phosphorylated at all four Ser‐Pro phosphorylation sites. Biochemistry 1993; 32(37)9563–9569
   PubMedGoogle Scholar
• Nephew K. P., Sheeler C. Q., Dudley M. D., Gordon S., Nayfield S. G., Khan S. A. Studies of dehydroepiandrosterone (DHEA) with the human estrogen receptor in yeast. Mol Cell Endocrinol 1998; 143(1–2)133–142
   PubMedGoogle Scholar