Estrogen receptor alpha

Estrogen receptor 1

PDB rendering based on 1a52.
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
Symbols ESR1 ; ER; ESR; ESRA; ESTRR; Era; NR3A1
External IDs OMIM: 133430 MGI: 1352467 HomoloGene: 47906 IUPHAR: 620 ChEMBL: 206 GeneCards: ESR1 Gene
Orthologs
Species Human Mouse
Entrez 2099 13982
Ensembl ENSG00000091831 ENSMUSG00000019768
UniProt P03372 P19785
RefSeq (mRNA) NM_000125 NM_001302531
RefSeq (protein) NP_000116 NP_001289460
Location (UCSC) Chr 6:
151.66 – 152.13 Mb		 Chr 10:
4.61 – 5.01 Mb
PubMed search

Estrogen receptor alpha (ERα), also known as NR3A1 (nuclear receptor subfamily 3, group A, member 1), is one of two main types of estrogen receptor, a nuclear receptor that is activated by the sex hormone estrogen. In humans, ERα is encoded by the gene ESR1 (EStrogen Receptor 1).[1][2][3]

Structure

The estrogen receptor (ER) is a ligand-activated transcription factor composed of several domains important for hormone binding, DNA binding, and activation of transcription.[4] Alternative splicing results in several ESR1 mRNA transcripts, which differ primarily in their 5-prime untranslated regions. The translated receptors show less variability.[5][6]

Ligands

Agonists

Agonists of ERα selective over ERβ include:

Antagonists

Antagonists of ERα selective over ERβ include:

Clinical significance

Estrogen insensitivity syndrome is a very rare condition characterized by a defective ERα that is insensitive to estrogens.[7][8][9][10] The clinical presentation of a female was observed to include absence of breast development and other female secondary sexual characteristics at puberty, hypoplastic uterus, primary amenorrhea, enlarged multicystic ovaries and associated lower abdominal pain, mild hyperandrogenism (manifested as cystic acne), and delayed bone maturation as well as an increased rate of bone turnover.[10] The clinical presentation in a male was reported to include lack of epiphyseal closure, tall stature, osteoporosis, and poor sperm viability.[9] Both individuals were completely insensitive to exogenous estrogen treatment, even with high doses.[10][9]

Coactivators

Coactivators of ER-α include:

Interactions

Estrogen receptor alpha has been shown to interact with:

References

  1. ↑ "Entrez Gene: ESR1 estrogen receptor 1".
  2. ↑ Walter P, Green S, Greene G, Krust A, Bornert JM, Jeltsch JM, Staub A, Jensen E, Scrace G, Waterfield M (December 1985). "Cloning of the human estrogen receptor cDNA". Proc. Natl. Acad. Sci. U.S.A. 82 (23): 7889–93. doi:10.1073/pnas.82.23.7889. PMC 390875. PMID 3865204.
  3. ↑ Greene GL, Gilna P, Waterfield M, Baker A, Hort Y, Shine J (March 1986). "Sequence and expression of human estrogen receptor complementary DNA". Science 231 (4742): 1150–4. doi:10.1126/science.3753802. PMID 3753802.
  4. ↑ Dahlman-Wright K, Cavailles V, Fuqua SA, Jordan VC, Katzenellenbogen JA, Korach KS, Maggi A, Muramatsu M, Parker MG, Gustafsson JA (December 2006). "International Union of Pharmacology. LXIV. Estrogen receptors". Pharmacol. Rev. 58 (4): 773–81. doi:10.1124/pr.58.4.8. PMID 17132854.
  5. ↑ "Entrez Gene: DBI diazepam binding inhibitor (GABA receptor modulator, acyl-Coenzyme A binding protein)".
  6. ↑ Kos M, Reid G, Denger S, Gannon F (December 2001). "Minireview: genomic organization of the human ERalpha gene promoter region". Mol. Endocrinol. 15 (12): 2057–63. doi:10.1210/me.15.12.2057. PMID 11731608.
  7. ↑ J. Larry Jameson; Leslie J. De Groot (25 February 2015). Endocrinology: Adult and Pediatric. Elsevier Health Sciences. pp. 238–. ISBN 978-0-323-32195-2.
  8. ↑ Korach KS, Couse JF, Curtis SW, Washburn TF, Lindzey J, Kimbro KS, Eddy EM, Migliaccio S, Snedeker SM, Lubahn DB, Schomberg DW, Smith EP (1996). "Estrogen receptor gene disruption: molecular characterization and experimental and clinical phenotypes". Recent Progress in Hormone Research 51: 159–86; discussion 186–8. PMID 8701078.
  9. 1 2 3 Smith EP, Boyd J, Frank GR, Takahashi H, Cohen RM, Specker B, Williams TC, Lubahn DB, Korach KS (Oct 1994). "Estrogen resistance caused by a mutation in the estrogen-receptor gene in a man". The New England Journal of Medicine 331 (16): 1056–61. doi:10.1056/NEJM199410203311604. PMID 8090165.
  10. 1 2 3 Quaynor SD, Stradtman EW, Kim HG, Shen Y, Chorich LP, Schreihofer DA, Layman LC (Jul 2013). "Delayed puberty and estrogen resistance in a woman with estrogen receptor α variant". The New England Journal of Medicine 369 (2): 164–71. doi:10.1056/NEJMoa1303611. PMID 23841731.
  11. ↑ Shang Y, Brown M (2002). "Molecular determinants for the tissue specificity of SERMs". Science 295 (5564): 2465–8. doi:10.1126/science.1068537. PMID 11923541.
  12. ↑ Smith CL, O'Malley BW (2004). "Coregulator function: a key to understanding tissue specificity of selective receptor modulators". Endocr Rev 25 (1): 45–71. doi:10.1210/er.2003-0023. PMID 14769827.
  13. ↑ Anzick SL, Kononen J, Walker RL, Azorsa DO, Tanner MM, Guan XY, Sauter G, Kallioniemi OP, Trent JM, Meltzer PS (1997). "AIB1, a steroid receptor coactivator amplified in breast and ovarian cancer". Science 277 (5328): 965–8. doi:10.1126/science.277.5328.965. PMID 9252329.
  14. ↑ Gururaj AE, Peng S, Vadlamudi RK, Kumar R (August 2007). "Estrogen induces expression of BCAS3, a novel estrogen receptor-alpha coactivator, through proline-, glutamic acid-, and leucine-rich protein-1 (PELP1)". Mol. Endocrinol. 21 (8): 1847–60. doi:10.1210/me.2006-0514. PMID 17505058.
  15. ↑ Vadlamudi RK, Wang RA, Mazumdar A, Kim Y, Shin J, Sahin A, Kumar R (2001). "Molecular cloning and characterization of PELP1, a novel human coregulator of estrogen receptor alpha". J. Biol. Chem. 276 (41): 38272–9. doi:10.1074/jbc.M103783200. PMID 11481323.
  16. ↑ Rubino D, Driggers P, Arbit D, Kemp L, Miller B, Coso O, Pagliai K, Gray K, Gutkind S, Segars J (May 1998). "Characterization of Brx, a novel Dbl family member that modulates estrogen receptor action". Oncogene 16 (19): 2513–26. doi:10.1038/sj.onc.1201783. PMID 9627117.
  17. ↑ Wormke M, Stoner M, Saville B, Walker K, Abdelrahim M, Burghardt R, Safe S (Mar 2003). "The Aryl Hydrocarbon Receptor Mediates Degradation of Estrogen Receptor α through Activation of Proteasomes". Mol. Cell. Biol. 23 (6): 1843–55. doi:10.1128/MCB.23.6.1843-1855.2003. PMC 149455. PMID 12612060.
  18. ↑ Klinge CM, Kaur K, Swanson HI (Jan 2000). "The aryl hydrocarbon receptor interacts with estrogen receptor alpha and orphan receptors COUP-TFI and ERRalpha1". Arch. Biochem. Biophys. 373 (1): 163–74. doi:10.1006/abbi.1999.1552. PMID 10620335.
  19. ↑ Zheng L, Annab LA, Afshari CA, Lee WH, Boyer TG (Aug 2001). "BRCA1 mediates ligand-independent transcriptional repression of the estrogen receptor". Proc. Natl. Acad. Sci. U.S.A. 98 (17): 9587–92. doi:10.1073/pnas.171174298. PMC 55496. PMID 11493692.
  20. ↑ Fan S, Ma YX, Wang C, Yuan RQ, Meng Q, Wang JA, Erdos M, Goldberg ID, Webb P, Kushner PJ, Pestell RG, Rosen EM (Jan 2001). "Role of direct interaction in BRCA1 inhibition of estrogen receptor activity". Oncogene 20 (1): 77–87. doi:10.1038/sj.onc.1204073. PMID 11244506.
  21. ↑ Kawai H, Li H, Chun P, Avraham S, Avraham HK (Oct 2002). "Direct interaction between BRCA1 and the estrogen receptor regulates vascular endothelial growth factor (VEGF) transcription and secretion in breast cancer cells". Oncogene 21 (50): 7730–9. doi:10.1038/sj.onc.1205971. PMID 12400015.
  22. 1 2 3 Fan S, Ma YX, Wang C, Yuan RQ, Meng Q, Wang JA, Erdos M, Goldberg ID, Webb P, Kushner PJ, Pestell RG, Rosen EM (Jan 2002). "p300 Modulates the BRCA1 inhibition of estrogen receptor activity". Cancer Res. 62 (1): 141–51. PMID 11782371.
  23. ↑ Schlegel A, Wang C, Pestell RG, Lisanti MP (Oct 2001). "Ligand-independent activation of oestrogen receptor alpha by caveolin-1". Biochem. J. 359 (Pt 1): 203–10. doi:10.1042/0264-6021:3590203. PMC 1222136. PMID 11563984.
  24. 1 2 3 4 5 6 7 8 9 10 Kang YK, Guermah M, Yuan CX, Roeder RG (Mar 2002). "The TRAP/Mediator coactivator complex interacts directly with estrogen receptors α and β through the TRAP220 subunit and directly enhances estrogen receptor function in vitro". Proc. Natl. Acad. Sci. U.S.A. 99 (5): 2642–7. doi:10.1073/pnas.261715899. PMC 122401. PMID 11867769.
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  29. ↑ Métivier R, Gay FA, Hübner MR, Flouriot G, Salbert G, Gannon F, Kah O, Pakdel F (Jul 2002). "Formation of an hERα–COUP-TFI complex enhances hERα AF-1 through Ser118 phosphorylation by MAPK". EMBO J. 21 (13): 3443–53. doi:10.1093/emboj/cdf344. PMC 126093. PMID 12093745.
  30. 1 2 Sheppard HM, Harries JC, Hussain S, Bevan C, Heery DM (Jan 2001). "Analysis of the Steroid Receptor Coactivator 1 (SRC1)-CREB Binding Protein Interaction Interface and Its Importance for the Function of SRC1". Mol. Cell. Biol. 21 (1): 39–50. doi:10.1128/MCB.21.1.39-50.2001. PMC 86566. PMID 11113179.
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  32. 1 2 3 4 5 6 Watanabe M, Yanagisawa J, Kitagawa H, Takeyama K, Ogawa S, Arao Y, Suzawa M, Kobayashi Y, Yano T, Yoshikawa H, Masuhiro Y, Kato S (Mar 2001). "A subfamily of RNA-binding DEAD-box proteins acts as an estrogen receptor α coactivator through the N-terminal activation domain (AF-1) with an RNA coactivator, SRA". EMBO J. 20 (6): 1341–52. doi:10.1093/emboj/20.6.1341. PMC 145523. PMID 11250900.
  33. ↑ Endoh H, Maruyama K, Masuhiro Y, Kobayashi Y, Goto M, Tai H, Yanagisawa J, Metzger D, Hashimoto S, Kato S (Aug 1999). "Purification and Identification of p68 RNA Helicase Acting as a Transcriptional Coactivator Specific for the Activation Function 1 of Human Estrogen Receptor α". Mol. Cell. Biol. 19 (8): 5363–72. PMC 84379. PMID 10409727.
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Further reading

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  • Simoncini T, Fornari L, Mannella P, Varone G, Caruso A, Liao JK, Genazzani AR (2003). "Novel non-transcriptional mechanisms for estrogen receptor signaling in the cardiovascular system. Interaction of estrogen receptor alpha with phosphatidylinositol 3-OH kinase". Steroids 67 (12): 935–9. doi:10.1016/S0039-128X(02)00040-5. PMID 12398989. 
  • Lannigan DA (2003). "Estrogen receptor phosphorylation". Steroids 68 (1): 1–9. doi:10.1016/S0039-128X(02)00110-1. PMID 12475718. 
  • Herrington DM (2003). "Role of estrogen receptor-alpha in pharmacogenetics of estrogen action". Curr. Opin. Lipidol. 14 (2): 145–50. doi:10.1097/00041433-200304000-00005. PMID 12642782. 
  • Tanaka Y, Sasaki M, Kaneuchi M, Fujimoto S, Dahiya R (2004). "Estrogen receptor alpha polymorphisms and renal cell carcinoma--a possible risk". Mol. Cell. Endocrinol. 202 (1–2): 109–16. doi:10.1016/S0303-7207(03)00071-6. PMID 12770739. 
  • Ali S, Coombes RC (2004). "Estrogen receptor alpha in human breast cancer: occurrence and significance". Journal of Mammary Gland Biology and Neoplasia 5 (3): 271–81. doi:10.1023/A:1009594727358. PMID 14973389. 
  • Olsson H (2004). "Estrogen receptor content in malignant breast tumors in men--a review". Journal of Mammary Gland Biology and Neoplasia 5 (3): 283–7. doi:10.1023/A:1009546811429. PMID 14973390. 
  • Surmacz E, Bartucci M (2005). "Role of estrogen receptor alpha in modulating IGF-I receptor signaling and function in breast cancer". J. Exp. Clin. Cancer Res. 23 (3): 385–94. PMID 15595626. 
  • Evinger AJ, Levin ER (2005). "Requirements for estrogen receptor alpha membrane localization and function". Steroids 70 (5–7): 361–3. doi:10.1016/j.steroids.2005.02.015. PMID 15862818. 
  • Wang CL, Tang XY, Chen WQ, Su YX, Zhang CX, Chen YM (2007). "Association of estrogen receptor alpha gene polymorphisms with bone mineral density in Chinese women: a meta-analysis". Osteoporosis international : a journal established as result of cooperation between the European Foundation for Osteoporosis and the National Osteoporosis Foundation of the USA 18 (3): 295–305. doi:10.1007/s00198-006-0239-2. PMID 17089081. 
  • Keaveney M, Klug J, Gannon F (1992). "Sequence analysis of the 5' flanking region of the human estrogen receptor gene". DNA Seq. 2 (6): 347–58. doi:10.3109/10425179209020816. PMID 1476547. 
  • Piva R, Gambari R, Zorzato F, Kumar L, del Senno L (1992). "Analysis of upstream sequences of the human estrogen receptor gene". Biochem. Biophys. Res. Commun. 183 (3): 996–1002. doi:10.1016/S0006-291X(05)80289-X. PMID 1567414. 
  • Reese JC, Katzenellenbogen BS (1992). "Characterization of a temperature-sensitive mutation in the hormone binding domain of the human estrogen receptor. Studies in cell extracts and intact cells and their implications for hormone-dependent transcriptional activation". J. Biol. Chem. 267 (14): 9868–73. PMID 1577818. 
  • Dotzlaw H, Alkhalaf M, Murphy LC (1992). "Characterization of estrogen receptor variant mRNAs from human breast cancers". Mol. Endocrinol. 6 (5): 773–85. doi:10.1210/me.6.5.773. PMID 1603086. 
  • Keaveney M, Klug J, Dawson MT, Nestor PV, Neilan JG, Forde RC, Gannon F (1991). "Evidence for a previously unidentified upstream exon in the human oestrogen receptor gene". J. Mol. Endocrinol. 6 (1): 111–5. doi:10.1677/jme.0.0060111. PMID 2015052. 
  • Reese JC, Katzenellenbogen BS (1991). "Mutagenesis of cysteines in the hormone binding domain of the human estrogen receptor. Alterations in binding and transcriptional activation by covalently and reversibly attaching ligands". J. Biol. Chem. 266 (17): 10880–7. PMID 2040605. 
  • Schwabe JW, Neuhaus D, Rhodes D (1991). "Solution structure of the DNA-binding domain of the oestrogen receptor". Nature 348 (6300): 458–61. doi:10.1038/348458a0. PMID 2247153. 
  • Tora L, Mullick A, Metzger D, Ponglikitmongkol M, Park I, Chambon P (1989). "The cloned human oestrogen receptor contains a mutation which alters its hormone binding properties". EMBO J. 8 (7): 1981–6. PMC 401066. PMID 2792078. 
  • Ponglikitmongkol M, Green S, Chambon P (1989). "Genomic organization of the human oestrogen receptor gene". EMBO J. 7 (11): 3385–8. PMC 454836. PMID 3145193. 
  • Greene GL, Gilna P, Waterfield M, Baker A, Hort Y, Shine J (1986). "Sequence and expression of human estrogen receptor complementary DNA". Science 231 (4742): 1150–4. doi:10.1126/science.3753802. PMID 3753802. 

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