Skip to main content
SpringerLink
Log in
Book cover

Molecular Biology of Steroid and Nuclear Hormone Receptors pp 237–260Cite as

Birkhäuser

Regulation of Glucocorticoid and Estrogen Receptor Activity by Phosphorylation

  • Chapter

Part of the book series: Progress in Gene Expression ((PRGE))

Abstract

Protein phosphorylation is a versatile posttranslational modification that can regulate enzymatic activities, cell proliferation, DNA replication, and gene expression (Boulikas 1995, Hofer 1996, Johnson and O’Reilly 1996, Karin 1994, Karin and Hunter 1995, Piwnica-Worms 1996). Steroid receptors, like many transcription factors, are phosphoproteins, and increasing evidence suggests that the activity of steroid receptors is regulated by phosphorylation (Bai and Weigel 1995, Blok et al 1996, Kuiper and Brinkmann 1994, Orti et al 1989, Weigel 1996). Treatment of cells with activators or inhibitors of protein kinases or phosphatases affects the transcriptional activity of steroid receptors (Edwards et al 1993, Edwards 1994, Katzenellenbogen 1996). In some cases, these treatments can activate the receptor in the absence of hormone (O’Malley et al 1995, Power et al 1992). Thus, there appears to be significant communication between signal transduction pathways that affect intracellular kinase and phosphatase activity and steroid receptor function.

This is a preview of subscription content, log in via an institution.

Chapter
USD   29.95
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
eBook
USD   39.99
Price excludes VAT (USA)
  • Available as EPUB and PDF
  • Read on any device
  • Instant download
  • Own it forever
Softcover Book
USD   54.99
Price excludes VAT (USA)
  • Compact, lightweight edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info

Tax calculation will be finalised at checkout

Purchases are for personal use only

Learn about institutional subscriptions

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  • Ali S, Metzger D, Bornert JM, and Chambon, P (1993): Modulation of transcriptional activation by ligand-dependent phosphorylation of the human oestrogen receptor A/B region. EMBO Journal. 12: 1153–60.

    PubMed  CAS  Google Scholar 

  • Almlof T, Wright AP, and Gustafsson JA (1995): Role of acidic and phosphorylated residues in gene activation by the glucocorticoid receptor. Journal of Biological Chemistry 270: 17535–40.

    Article  PubMed  CAS  Google Scholar 

  • Arnold SF, and Notides AC (1995): An antiestrogen: a phosphotyrosyl peptide that blocks dimerization of the human estrogen receptor. Proceedings of the National Academy of Sciences of the United States of America 92: 7475–9.

    Article  PubMed  CAS  Google Scholar 

  • Arnold SF, Obourn JD, Jaffe H, and Notides AC (1994): Serine 167 is the major estradiol-induced phosphorylation site on the human estrogen receptor. Molecular Endocrinology 8: 1208–14.

    Article  PubMed  CAS  Google Scholar 

  • Arnold SF, Obourn JD, Jaffe H, and Notides AC (1995): Phosphorylation of the human estrogen receptor by mitogen-activated protein kinase and casein kinase II: consequence on DNA binding. Journal of Steroid Biochemistry & Molecular Biology 55: 163–72.

    Article  CAS  Google Scholar 

  • Arnold SF, Obourn JD, Jaffe H, and Notides AC (1995): Phosphorylation of the human estrogen receptor on tyrosine 537 in vivo and by src family tyrosine kinases in vitro. Molecular Endocrinology 9: 24–33.

    Article  PubMed  CAS  Google Scholar 

  • Arnold SF, Vorojeikina DP, and Notides AC (1995): Phosphorylation of tyrosine 537 on the human estrogen receptor is required for binding to an estrogen response element. Journal of Biological Chemistry 270: 30205–12.

    Article  PubMed  CAS  Google Scholar 

  • Aronica SM, and Katzenellenbogen BS (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. Molecular Endocrinology 7: 743–52.

    Article  PubMed  CAS  Google Scholar 

  • Aronica SM, Kraus WL, and Katzenellenbogen BS (1994): Estrogen action via the cAMP signaling pathway: stimulation of adenylate cyclase and cAMP-regulated gene transcription. Proceedings of the National Academy of Sciences of the United States of America 91: 8517–21.

    Article  PubMed  CAS  Google Scholar 

  • Auricchio F, Migliaccio A, Castoria G, Di Domenico M, Bilancio A, and Rotondi, A (1996): Protein tyrosine phosphorylation and estradiol action. [Review] [41 refs]. Annals of the New York Academy of Sciences 784: 149–72.

    Article  PubMed  CAS  Google Scholar 

  • Bai W, and Weigel NL (1995): Phosphorylation and steroid hormone action. [Review] [115 refs]. Vitamins & Hormones 51: 289–313.

    Article  CAS  Google Scholar 

  • Bai W, and Weigel NL (1996): Phosphorylation of Ser211 in the chicken progesterone receptor modulates its transcriptional activity. Journal of Biological Chemistry 271: 12801–6.

    Article  PubMed  CAS  Google Scholar 

  • Beato M, Herrlich P, and Schutz, G (1995): Steroid hormone receptors: many actors in search of a plot. [Review] [66 refs]. Cell 83: 851–7.

    Article  PubMed  CAS  Google Scholar 

  • Blok LJ, de Ruiter PE, and Brinkmann AO (1996): Androgen receptor phosphorylation. [Review] [37 refs]. Endocrine Research 22: 197–219.

    Article  PubMed  CAS  Google Scholar 

  • Bodwell JE, Hu JM, Hu LM, and Munck, A (1996): Glucocorticoid receptors: ATP and cell cycle dependence, phosphorylation, and hormone resistance. [Review] [35 refs]. American Journal of Respiratory & Critical Care Medicine. 154: S2–6.

    CAS  Google Scholar 

  • Bodwell JE, Hu JM, Orti E, and Munck, A (1995): Hormone-induced hyperphosphorylation of specific phosphorylated sites in the mouse glucocorticoid receptor. Journal of Steroid Biochemistry & Molecular Biology 52: 135–40.

    Article  CAS  Google Scholar 

  • Bodwell JE, Hu LM, Hu JM, Orti E, and Munck, A (1993): Glucocorticoid receptors: ATP-dependent cycling and hormone-dependent hyperphosphorylation. [Review] [52 refs]. Journal of Steroid Biochemistry & Molecular Biology 47: 31–8.

    Article  CAS  Google Scholar 

  • Bodwell JE, Orti E, Coull JM, Pappin DJ, Smith LI, and Swift, F (1991): Identification of phosphorylated sites in the mouse glucocorticoid receptor. Journal of Biological Chemistry 266: 7549–55.

    PubMed  CAS  Google Scholar 

  • Borror KC, Garabedian MJ, and DeFranco DB (1995): Glucocorticoid receptor phosphorylation in v-mos-transformed cells. Steroids 60: 375–82.

    Article  PubMed  CAS  Google Scholar 

  • Boulikas, T (1995): Phosphorylation of transcription factors and control of the cell cycle. [Review] [524 refs]. Critical Reviews in Eukaryotic Gene Expression 5: 1–77.

    PubMed  CAS  Google Scholar 

  • Bunone G, Briand PA, Miksicek RJ, and Picard, D (1996): Activation of the unliganded estrogen receptor by EGF involves the MAP kinase pathway and direct phosphorylation. EMBO Journal 15: 2174–83.

    PubMed  CAS  Google Scholar 

  • Chauchereau A, Cohen-Solal K, Jolivet A, Bailly A, and Milgrom, E (1994): Phosphorylation sites in ligand-induced and ligand-independent activation of the progesterone receptor. Biochemistry 33: 13295–303.

    Article  PubMed  CAS  Google Scholar 

  • Cho H, and Katzenellenbogen BS (1993): Synergistic activation of estrogen receptor-mediated transcription by estradiol and protein kinase activators. Molecular Endocrinology 7: 441–52.

    Article  PubMed  CAS  Google Scholar 

  • Chrivia JC, Kwok RP, Lamb N, Hagiwara M, Montminy MR, and Goodman RH (1993): Phosphorylated CREB binds specifically to the nuclear protein CBP. Nature 365: 855–9.

    Article  PubMed  CAS  Google Scholar 

  • Cole TJ, Blendy JA, Monaghan AP, Krieglstein K, Schmid W, Aguzzi A, Fantuzzi G, Hummler E, Unsicker K, and Schutz, G (1995): Targeted disruption of the glucocorticoid receptor gene blocks adrenergic chromaffin cell development and severely retards lung maturation. Genes & Development 9: 1608–21.

    Article  CAS  Google Scholar 

  • Dalman FC, Sanchez ER, Lin AL, Perini F, and Pratt WB (1988): Localization of phosphorylation sites with respect to the functional domains of the mouse L cell glucocorticoid receptor. Journal of Biological Chemistry 263: 12259–67.

    PubMed  CAS  Google Scholar 

  • Defranco DB, Madan AP, Tang Y, Chandran UR, Xiao N, and Yang, J (1995): Nucleocytoplasmic shuttling of steroid receptors. [Review] [86 refs]. Vitamins & Hormones 51: 315–38.

    Article  CAS  Google Scholar 

  • DeFranco DB, Qi M, Borror KC, Garabedian MJ, and Brautigan DL (1991): Protein phosphatase types 1 and/or 2A regulate nucleocytoplasmic shuttling of glucocorticoid receptors. Molecular Endocrinology 5: 1215–28.

    Article  PubMed  CAS  Google Scholar 

  • Edwards DP, Weigel NL, Nordeen SK, and Beck CA (1993): Modulators of cellular protein phosphorylation alter the trans-activation function of human progesterone receptor and the biological activity of progesterone antagonists. Breast Cancer Research & Treatment 27: 41–56.

    Article  CAS  Google Scholar 

  • Edwards DR (1994): Cell signalling and the control of gene transcription. [Review] [62 refs]. Trends in Pharmacological Sciences 15: 239–44.

    Article  PubMed  CAS  Google Scholar 

  • Giffin W, Kwast-Welfed J, Rodda DJ, Prefontaine GG, Traykova-Andonova M, Zhang Y, Weigel NL, Lefebvre YA, and Hache RJ, G (1997): Sequence-specific DNA Binding and Transcription Factor Phosphorylation by Ku Autoantigen/ DNA-dependent Protein Kinase. Journal of Biological Chemistry 272: 5647–58.

    Article  PubMed  CAS  Google Scholar 

  • Giffin W, Torrance H, Rodda DJ, Prefontaine GG, Pope L, and Hache RJ (1996): Sequence-specific DNA binding by Ku autoantigen and its effects on transcription. Nature 380: 265–8.

    Article  PubMed  CAS  Google Scholar 

  • Gille H, Kortenjann M, Strahl T, and Shaw PE (1996): Phosphorylation-dependent formation of a quaternary complex at the c-fos SRE. Molecular & Cellular Biology 16: 1094–102.

    CAS  Google Scholar 

  • Gille H, Kortenjann M, Thomae O, Moomaw C, Slaughter C, Cobb MH, and Shaw PE (1995): ERK phosphorylation potentiates Elk-1-mediated ternary complex formation and transactivation. EMBO Journal 14: 951–62.

    PubMed  CAS  Google Scholar 

  • Hoeck W, and Groner, B (1990): Hormone-dependent phosphorylation of the glucocorticoid receptor occurs mainly in the amino-terminal transactivation domain. Journal of Biological Chemistry 265: 5403–8.

    PubMed  CAS  Google Scholar 

  • Hofer HW (1996): Conservation, evolution, and specificity in cellular control by protein phosphorylation. [Review] [27 refs]. Experientia 52: 449–54.

    Article  PubMed  CAS  Google Scholar 

  • Hsu SC, and DeFranco DB (1995): Selectivity of cell cycle regulation of glucocorticoid receptor function. Journal of Biological Chemistry 270: 3359–64.

    Article  PubMed  CAS  Google Scholar 

  • Hsu SC, Qi M, and DeFranco DB (1992): Cell cycle regulation of glucocorticoid receptor function. EMBO Journal 11: 3457–68.

    PubMed  CAS  Google Scholar 

  • Hu JM, Bodwell JE, and Munck, A (1994): Cell cycle-dependent glucocorticoid receptor phosphorylation and activity. Molecular Endocrinology 8: 1709–13.

    Article  PubMed  CAS  Google Scholar 

  • Hutchison KA, Dalman FC, Hoeck W, Groner B, and Pratt WB (1993): Localization of the approximately 12 kDa M(r) discrepancy in gel migration of the mouse glucocorticoid receptor to the major phosphorylated cyanogen bromide fragment in the transactivating domain. Journal of Steroid Biochemistry & Molecular Biology 46: 681–6.

    Article  CAS  Google Scholar 

  • Ignar-Trowbridge DM, Pimentel M, Parker MG, McLachlan JA, and Korach KS (1996): Peptide growth factor cross-talk with the estrogen receptor requires the A/B domain and occurs independently of protein kinase C or estradiol. Endocrinology 137: 1735–44.

    Article  PubMed  CAS  Google Scholar 

  • Ignar-Trowbridge DM, Teng CT, Ross KA, Parker MG, Korach KS, and McLachlan JA (1993): Peptide growth factors elicit estrogen receptor-dependent transcriptional activation of an estrogen-responsive element. Molecular Endocrinology 7: 992–8.

    Article  PubMed  CAS  Google Scholar 

  • Ince BA, Montano MM, and Katzenellenbogen BS (1994): Activation of transcriptionally inactive human estrogen receptors by cyclic adenosine 3’,5’-monophosphate and ligands including antiestrogens. Molecular Endocrinology 8: 1397–406.

    Article  PubMed  CAS  Google Scholar 

  • Iniguez-Lluhi JA, Lou DY, and Yamamoto KR (1997): Three Amino Acid Substitutions Selectively Disrupt the Activation but Not the Repression Function of the Glucocorticoid Receptor N Terminus. Journal of Biological Chemistry 272: 4149–56.

    CAS  Google Scholar 

  • Janknecht R, and Hunter, T (1996a): Transcription. A growing coactivator network [news; comment]. Nature 383: 22–3.

    Article  CAS  Google Scholar 

  • Janknecht R, and Hunter, T (1996b): Versatile molecular glue. Transcriptional control. [Review] [25 refs]. Current Biology 6: 951–4.

    Article  CAS  Google Scholar 

  • Jans DA, and Hubner, S (1996): Regulation of protein transport to the nucleus: central role of phosphorylation. [Review] [400 refs]. Physiological Reviews 76: 651–85.

    PubMed  CAS  Google Scholar 

  • Jans DA, Moll T, Nasmyth K, and Jans, P (1995): Cyclin-dependent kinase site-regulated signal-dependent nuclear localization of the SW15 yeast transcription factor in mammalian cells. Journal of Biological Chemistry 270: 17064–7.

    Article  PubMed  CAS  Google Scholar 

  • Joel PB, Traish AM, and Lannigan DA (1995): Estradiol and phorbol ester cause phosphorylation of serine 118 in the human estrogen receptor. Molecular Endocrinology 9: 1041–52.

    Article  PubMed  CAS  Google Scholar 

  • Johnson LN, and O’Reilly, M (1996): Control by phosphorylation. [Review] [36 refs]. Current Opinion in Structural Biology 6: 762–9.

    Article  PubMed  CAS  Google Scholar 

  • Karin, M (1994): Signal transduction from the cell surface to the nucleus through the phosphorylation of transcription factors. [Review] [76 refs]. Current Opinion in Cell Biology 6: 415–24.

    Article  PubMed  CAS  Google Scholar 

  • Karin M, and Hunter, T (1995): Transcriptional control by protein phosphorylation: signal transmission from the cell surface to the nucleus. [Review] [102 refs]. Current Biology 5: 747–57.

    Article  PubMed  CAS  Google Scholar 

  • Kato S, Endoh H, Masuhiro Y, Kitamoto T, Uchiyama S, Sasaki H, Masushige S, Gotoh Y, Nishida E, Kawashima, H. et al (1995): Activation of the estrogen receptor through phosphorylation by mitogen-activated protein kinase Science 270: 1491–4.

    Article  PubMed  CAS  Google Scholar 

  • Katzenellenbogen BS (1996): Estrogen receptors: bioactivities and interactions with cell signaling pathways. [Review] [74 refs]. Biology of Reproduction 54: 287–93.

    Article  PubMed  CAS  Google Scholar 

  • Korach KS (1994): Insights from the study of animals lacking functional estrogen receptor. [Review] [32 refs]. Science 266: 1524–7.

    Article  PubMed  CAS  Google Scholar 

  • Korach KS, Couse JF, Curtis SW, Washburn TF, Lindzey J, Kimbro KS, Eddy EM, Migliaccio S, Snedeker SM, Lubahn DB, et al (1996): Estrogen receptor gene disruption: molecular characterization and experimental and clinical phenotypes. [Review] [50 refs]. Recent Progress in Hormone Research 51: 159–86.

    PubMed  CAS  Google Scholar 

  • Kralli A, Bohen SP, and Yamamoto KR (1995): LEMI, an ATP-binding-cassette transporter, selectively modulates the biological potency of steroid hormones. Proceedings of the National Academy of Sciences of the United States of America 92: 4701–5.

    Article  PubMed  CAS  Google Scholar 

  • Krstic MK (1995): Functional Anaylsis of Glucocorticoid Receptor Phosphorylation. UCSF. Thesis.

    Google Scholar 

  • Krstic MK, Rogatsky I, Yamamoto KR, and Garabedian MJ (1997): Mitogenactivated and cyclin-dependent protein kinases selectively and differentially modulate transcriptional enhancement by the glucocorticoid receptor. Molecular and Cellular Biology 17: 3947–54.

    PubMed  CAS  Google Scholar 

  • Kuiper GG, and Brinkmann AO (1994): Steroid hormone receptor phosphorylation: is there a physiological role?. [Review] [48 refs]. Molecular & Cellular Endocrinology 100: 103–7.

    Article  CAS  Google Scholar 

  • Lahooti H, White R, Hoare SA, Rahman D, Pappin DJ, and Parker MG (1995): Identification of phosphorylation sites in the mouse oestrogen receptor. Journal of Steroid Biochemistry & Molecular Biology 55: 305–13.

    Article  CAS  Google Scholar 

  • Le Goff P, Montano MM, Schodin DJ, and Katzenellenbogen BS (1994): Phosphorylation of the human estrogen receptor. Identification of hormone-regulated sites and examination of their influence on transcriptional activity. Journal of Biological Chemistry 269: 4458–66.

    PubMed  Google Scholar 

  • Mason SA, and Housley PR (1993): Site-directed mutagenesis of the phosphorylation sites in the mouse glucocorticoid receptor. Journal of Biological Chemistry 268: 21501–4.

    PubMed  CAS  Google Scholar 

  • Moll T, Schwob E, Koch C, Moore A, Auer H, and Nasmyth, K (1993): Transcription factors important for starting the cell cycle in yeast. Philosophical Transactions of the Royal Society of London Series B: Biological Sciences. 340: 351–60.

    Article  PubMed  CAS  Google Scholar 

  • Moll T, Tebb G, Surana U, Robitsch H, and Nasmyth, K (1991): The role of phosphorylation and the CDC28 protein kinase in cell cycle-regulated nuclear import of the S. cerevisiae transcription factor SWI5. Cell 66: 743–58.

    Article  PubMed  CAS  Google Scholar 

  • Moyer ML, Borror KC, Bona BJ, DeFranco DB, and Nordeen SK (1993): Modulation of cell signaling pathways can enhance or impair glucocorticoid-induced gene expression without altering the state of receptor phosphorylation. Journal of Biological Chemistry 268: 22933–40.

    PubMed  CAS  Google Scholar 

  • Nazareth LV, and Weigel NL (1996): Activation of the human androgen receptor through a protein kinase A signaling pathway. Journal of Biological Chemistry 271: 19900–7.

    Article  PubMed  CAS  Google Scholar 

  • O’Malley BW, Schrader WT, Mani S, Smith C, Weigel NL, Conneely OM, and Clark JH (1995): An alternative ligand-independent pathway for activation of steroid receptors. [Review] [45 refs]. Recent Progress in Hormone Research 50: 333–47.

    PubMed  Google Scholar 

  • Orti E, Bodwell JE, and Munck, A (1992): Phosphorylation of steroid hormone receptors. [Review] [232 refs]. Endocrine Reviews 13: 105–28.

    PubMed  CAS  Google Scholar 

  • Orti E Hu, LM, and Munck, A (1993): Kinetics of glucocorticoid receptor phosphorylation in intact cells. Evidence for hormone-induced hyperphosphorylation after activation and recycling of hyperphosphorylated receptors. Journal of Biological Chemistry 268: 7779–84.

    PubMed  CAS  Google Scholar 

  • Orti E, Mendel DB, and Munck, A (1989): Phosphorylation of glucocorticoid receptor-associated and free forms of the approximately 90-kDa heat shock protein before and after receptor activation. Journal of Biological Chemistry 264: 231–7.

    PubMed  CAS  Google Scholar 

  • Papavassiliou AG (1994): The role of regulated phosphorylation in the biological activity of transcription factors SRF and Elk-1/SAP-1. [Review] [31 refs]. Anticancer Research 14: 1923–6.

    PubMed  CAS  Google Scholar 

  • Parker D, Ferreri K, Nakajima T, LaMorte VJ, Evans R, Koerber SC, Hoeger C, and Montminy MR (1996): Phosphorylation of CREB at Ser-133 induces complex formation with CREB-binding protein via a direct mechanism. Molecular & Cellular Biology 16: 694–703.

    CAS  Google Scholar 

  • Pietras RJ, Arboleda J, Reese DM, Wongvipat N, Pegram MD, Ramos L, Gorman CM, Parker MG, Sliwkowski MX, and Slamon DJ (1995): HER-2 tyrosine kinase pathway targets estrogen receptor and promotes hormone-independent growth in human breast cancer cells. Oncogene 10: 2435–46.

    PubMed  CAS  Google Scholar 

  • Piwnica-Worms, H (1996): Reversible phosphorylation and mitotic control. [Review] [34 refs]. Journal of Laboratory & Clinical Medicine 128: 350–4.

    Article  CAS  Google Scholar 

  • Power RF, Conneely OM, and O’Malley BW (1992): New insights into activation of the steroid hormone receptor superfamily. [Review] [41 refs]. Trends in Pharmacological Sciences 13: 318–23.

    Article  PubMed  CAS  Google Scholar 

  • Power RF, Mani SK, Codina J, Conneely OM, and O’Malley BW (1991): Dopaminergic and ligand-independent activation of steroid hormone receptors. Science 254: 1636–9.

    Article  PubMed  CAS  Google Scholar 

  • Smith CL, Conneely OM, and O’Malley BW (1993): Modulation of the ligand-independent activation of the human estrogen receptor by hormone and antihormone. Proceedings of the National Academy of Sciences of the United States of America 90: 6120–4.

    Article  PubMed  CAS  Google Scholar 

  • Tienrungroj W, Sanchez ER, Housley PR, Harrison RW, and Pratt WB (1987): Glucocorticoid receptor phosphorylation, transformation, and DNA binding. Journal of Biological Chemistry 262: 17342–9.

    PubMed  CAS  Google Scholar 

  • Tienrungroj W, Sanchez ER, Housley PR, Harrison RW, and Pratt WB (1987): Glucocorticoid receptor phosphorylation, transformation, and DNA binding. Journal of Biological Chemistry 262: 17342–9.

    PubMed  CAS  Google Scholar 

  • Tzeng DZ, and Klinge CM (1996): Phosphorylation of purified estradiol-liganded estrogen receptor by casein kinase II increases estrogen response element binding but does not alter ligand stability. Biochemical & Biophysical Research Communications 223: 554–60.

    Article  CAS  Google Scholar 

  • Webster JC, Jewell CM, Bodwell JE, Munck A, Sar M, and Cidlowski JA (1997): Mouse Glucocorticoid Receptor Phosphorylation Status Influences Multiple Functions of the Receptor Protein. Journal of Biological Chemistry 272: 9287–9293.

    Article  PubMed  CAS  Google Scholar 

  • Weigel NL (1996): Steroid hormone receptors and their regulation by phosphorylation. [Review] [156 refs]. Biochemical Journal 319: 657–67.

    PubMed  CAS  Google Scholar 

  • White R, Sjoberg M, Kalkhoven E, and Parker MG (1997): Ligand-independent activation of the oestrogen receptor by mutation of a conserved tyrosine. EMBO Journal 16: 1427–35.

    Article  PubMed  CAS  Google Scholar 

  • Zhang Y, Bai W, Allgood VE, and Weigel NL (1994): Multiple signaling pathways activate the chicken progesterone receptor. Molecular Endocrinology 8: 577–84.

    Article  PubMed  CAS  Google Scholar 

  • Zilliacus J, Wright AP, Carlstedt-Duke J, and Gustafsson JA (1995): Structural determinants of DNA-binding specificity by steroid receptors. [Review] [114 refs]. Molecular Endocrinology 9: 389–400.

    Article  PubMed  CAS  Google Scholar 

  • Zwijsen RM, Wientjens E, Klompmaker R, van der Sman J, Bernards R, and Michalides RJAM (1997): CDK-independent activation of estrogen receptor by cyclin D1. Cell 88: 405–15.

    Article  PubMed  CAS  Google Scholar 

Download references

Authors
  1. Michael J. Garabedian
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. Inez Rogatsky
    View author publications

    You can also search for this author in PubMed Google Scholar

  3. Adam Hittelman
    View author publications

    You can also search for this author in PubMed Google Scholar

  4. Roland Knoblauch
    View author publications

    You can also search for this author in PubMed Google Scholar

  5. Janet M. Trowbridge
    View author publications

    You can also search for this author in PubMed Google Scholar

  6. Marija D. Krstic
    View author publications

    You can also search for this author in PubMed Google Scholar

Editor information

Editors and Affiliations

  1. Cell Biology and Genetics, Memorial Sloan-Kettering Cancer Center, 10021, New York, NY, USA

    Leonard P. Freedman

Rights and permissions

Reprints and permissions

Copyright information

© 1998 Springer Science+Business Media New York

About this chapter

Cite this chapter

Garabedian, M.J., Rogatsky, I., Hittelman, A., Knoblauch, R., Trowbridge, J.M., Krstic, M.D. (1998). Regulation of Glucocorticoid and Estrogen Receptor Activity by Phosphorylation. In: Freedman, L.P. (eds) Molecular Biology of Steroid and Nuclear Hormone Receptors. Progress in Gene Expression. Birkhäuser, Boston, MA. https://doi.org/10.1007/978-1-4612-1764-0_9

Download citation

  • DOI: https://doi.org/10.1007/978-1-4612-1764-0_9

  • Publisher Name: Birkhäuser, Boston, MA

  • Print ISBN: 978-1-4612-7271-7

  • Online ISBN: 978-1-4612-1764-0

  • eBook Packages: Springer Book Archive

Publish with us

Policies and ethics

Search

Navigation