Estrogen receptor alpha

Estrogen receptor 1
PDB rendering based on 1a52.
Available structures PDB 1A52, 1AKF, 1ERE, 1ERR, 1G50, 1GWQ, 1GWR, 1HCP, 1HCQ, 1L2I, 1PCG, 1QKT, 1QKU, 1R5K, 1SJ0, 1UOM, 1X7E, 1X7R, 1XP1, 1XP6, 1XP9, 1XPC, 1XQC, 1YIM, 1YIN, 1ZKY, 2AYR, 2B1V, 2B1Z, 2B23, 2BJ4, 2FAI, 2G44, 2G5O, 2I0J, 2IOG, 2IOK, 2JF9, 2JFA, 2OCF, 2OUZ, 2P15, 2POG, 2Q6J, 2Q70, 2QA6, 2QA8, 2QAB, 2QE4, 2QGT, 2QGW, 2QH6, 2QR9, 2QSE, 2QXM, 2QXS, 2QZO, 2R6W, 2R6Y, 3CBM, 3CBO, 3CBP, 3DT3, 3ERD, 3ERT, 3HLV, 3HM1, 3OS8, 3OS9, 3OSA
Identifiers
Symbols	ESR1; DKFZp686N23123; ER; ESR; ESRA; Era; NR3A1
External IDs	OMIM: 133430 MGI: 1352467 HomoloGene: 47906 IUPHAR: NR3A1 GeneCards: ESR1 Gene
Gene Ontology Molecular function • sequence-specific DNA binding transcription factor activity • steroid hormone receptor activity • steroid binding • protein binding • beta-catenin binding • transcription factor binding • zinc ion binding • enzyme binding • nitric-oxide synthase regulator activity • estrogen receptor activity • protein complex binding • estrogen response element binding • hormone binding • sequence-specific DNA binding • metal ion binding Cellular component • nucleus • nucleoplasm • cytoplasm • plasma membrane • membrane • chromatin remodeling complex • T-tubule • neuron projection • terminal button • perikaryon Biological process • antral ovarian follicle growth • epithelial cell development • osteoblast development • transcription, DNA-dependent • regulation of transcription, DNA-dependent • signal transduction • androgen metabolic process • male gonad development • gene expression • estrogen receptor signaling pathway • response to estradiol stimulus • regulation of transcription from RNA polymerase II promoter by nuclear hormone receptor • steroid hormone mediated signaling pathway • neuroprotection • response to estrogen stimulus • positive regulation of survival gene product expression • positive regulation of fibroblast proliferation • positive regulation of retinoic acid receptor signaling pathway • uterus development • vagina development • prostate epithelial cord elongation • prostate epithelial cord arborization involved in prostate glandular acinus morphogenesis • regulation of branching involved in prostate gland morphogenesis • mammary gland branching involved in pregnancy • mammary gland alveolus development • epithelial cell proliferation involved in mammary gland duct elongation Sources: Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	2099	13982
Ensembl	ENSG00000091831	ENSMUSG00000019768
UniProt	P03372	P19785
RefSeq (mRNA)	NM_000125.3	NM_007956.4
RefSeq (protein)	NP_000116.2	NP_031982.1
Location (UCSC)	Chr 6: 151.98 – 152.45 Mb	Chr 10: 5.34 – 5.73 Mb
PubMed search	[1]	[2]

Estrogen receptor alpha (ER-α), also known as NR3A1 (nuclear receptor subfamily 3, group A, member 1), is a nuclear receptor that is activated by the sex hormone estrogen. In humans, ER-α is encoded by the gene ESR1 (EStrogen Receptor 1).^[1][2][3]

Structure

The estrogen receptor (ESR) 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][1]

Coactivators

Coactivators of ER-α include:

• SRC-1^[6][7]
• AIB1 – amplified in breast 1^[8]
• BCAS3 – breast carcinoma amplified sequence 3^[9]

Interactions

Estrogen receptor alpha has been shown to interact with:

• AKAP13^[10]
• AHR^[11][12]
• BRCA1^{[13][14][15][16]}
• CAV1^[17]
• CCNC^[18]
• CDC25B^[19]
• CEBPB^[20][21]
• COBRA1^[22]
• COUP-TFI^[23]
• CREBBP^[24][16]
• CRSP3^[18]
• Cyclin D1^[25]
• DDX17^[26]
• DDX5^[27][26]
• DNTTIP2^[28]
• EP300^[29][16][18]
• ESR2^[30][31]
• FOXO1^[32]
• GTF2H1^[33]
• HSP90AA1^[34][35]
• ISL1^[36]
• JARID1A^[37]
• MVP^[38]
• MED1^[39][18]
• MED12^[18]
• MED14^[18]
• MED16^[18]
• MED24^[39][18]
• MED6^[18]
• MGMT^[40]
• MNAT1^[41]
• MTA1^[42][43]
• NCOA6^[44][45]
• NCOA1^{[46][24][47][18][26]}
• NCOA2^{[39][48][26][49][50]}
• NCOA3^[51][52][26]
• NRIP1^[53][54][55]
• PDLIM1^[56]
• POU4F1^[57]
• POU4F2^[57]
• PRDM2^[58]
• PRMT2^[59]
• RBM39^[60]
• RNF12^[56]
• SAFB^[61][62]
• SAFB2^[63]
• SHC1^[64]
• SHP^[65][66]
• SMARCA4^[67][46]
• SMARCE1^[68]
• SRA1^[26]
• Src^{[69][40][70][71]}
• TR2^[72]
• TR4^[73]
• TDG^[74]
• TRIM24^[54][75] and
• XBP1.^[76]

References

1. ^ ^{a b} "Entrez Gene: ESR1 estrogen receptor 1". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2099. 
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. http://www.pnas.org/content/82/23/7889.abstract. 
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. ^ 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. 
6. ^ 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. 
7. ^ 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. 
8. ^ 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. 
9. ^ 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. 
10. ^ 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. 
11. ^ Wormke, Mark; Stoner Matthew, Saville Bradley, Walker Kelcey, Abdelrahim Maen, Burghardt Robert, Safe Stephen (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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=149455. 
12. ^ Klinge, C M; Kaur K, Swanson H I (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. 
13. ^ Zheng, L; Annab L A, Afshari C A, Lee W H, Boyer T G (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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=55496. 
14. ^ Fan, S; Ma Y X, Wang C, Yuan R Q, Meng Q, Wang J A, Erdos M, Goldberg I D, Webb P, Kushner P J, Pestell R G, Rosen E M (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. 
15. ^ Kawai, Hideki; Li Huchun, Chun Philip, Avraham Shalom, Avraham Hava Karsenty (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. 
16. ^ ^{a b c} Fan, Saijun; Ma Yong Xian, Wang Chenguang, Yuan Ren-Qi, Meng Qinghui, Wang Ji-An, Erdos Michael, Goldberg Itzhak D, Webb Paul, Kushner Peter J, Pestell Richard G, Rosen Eliot M (Jan. 2002). "p300 Modulates the BRCA1 inhibition of estrogen receptor activity". Cancer Res. 62 (1): 141–51. PMID 11782371. 
17. ^ Schlegel, A; Wang C, Pestell R G, Lisanti M P (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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1222136. 
18. ^ ^{a b c d e f g h i j} Kang, Yun Kyoung; Guermah Mohamed, Yuan Chao-Xing, Roeder Robert G (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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=122401. 
19. ^ Ma, Z Q; Liu Z, Ngan E S, Tsai S Y (Dec. 2001). "Cdc25B Functions as a Novel Coactivator for the Steroid Receptors". Mol. Cell. Biol. 21 (23): 8056–67. doi:10.1128/MCB.21.23.8056-8067.2001. PMC 99972. PMID 11689696. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=99972. 
20. ^ Boruk, M; Savory J G, Haché R J (Nov. 1998). "AF-2-dependent potentiation of CCAAT enhancer binding protein beta-mediated transcriptional activation by glucocorticoid receptor". Mol. Endocrinol. 12 (11): 1749–63. doi:10.1210/me.12.11.1749. PMID 9817600. 
21. ^ Stein, B; Yang M X (Sep. 1995). "Repression of the interleukin-6 promoter by estrogen receptor is mediated by NF-kappa B and C/EBP beta". Mol. Cell. Biol. 15 (9): 4971–9. PMC 230744. PMID 7651415. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=230744. 
22. ^ Aiyar, Sarah E; Sun Jian-long, Blair Ashley L, Moskaluk Christopher A, Lu Yun-zhe, Ye Qi-Nong, Yamaguchi Yuki, Mukherjee Amitava, Ren Da-ming, Handa Hiroshi, Li Rong (Sep. 2004). "Attenuation of estrogen receptor α-mediated transcription through estrogen-stimulated recruitment of a negative elongation factor". Genes Dev. 18 (17): 2134–46. doi:10.1101/gad.1214104. PMC 515291. PMID 15342491. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=515291. 
23. ^ Métivier, Raphaël; Gay Frédérique A, Hübner Michael R, Flouriot Gilles, Salbert Gilles, Gannon Frank, Kah Olivier, Pakdel Farzad (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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=126093. 
24. ^ ^{a b} Sheppard, H M; Harries J C, Hussain S, Bevan C, Heery D M (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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=86566. 
25. ^ Zwijsen, R M; Wientjens E, Klompmaker R, van der Sman J, Bernards R, Michalides R J (Feb. 1997). "CDK-independent activation of estrogen receptor by cyclin D1". Cell 88 (3): 405–15. doi:10.1016/S0092-8674(00)81879-6. PMID 9039267. 
26. ^ ^{a b c d e f} 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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=145523. 
27. ^ 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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=84379. 
28. ^ Bu, Hengfu; Kashireddy Papreddy, Chang Jeffrey, Zhu Yiwei Tony, Zhang Zhongyi, Zheng Wei, Rao Sambasiva M, Zhu Yi-Jun (Apr. 2004). "ERBP, a novel estrogen receptor binding protein enhancing the activity of estrogen receptor". Biochem. Biophys. Res. Commun. 317 (1): 54–9. doi:10.1016/j.bbrc.2004.02.179. ISSN 0006-291X. PMID 15047147. 
29. ^ Fajas, Lluis; Egler Viviane, Reiter Raphael, Hansen Jacob, Kristiansen Karsten, Debril Marie-Bernard, Miard Stéphanie, Auwerx Johan (Dec. 2002). "The retinoblastoma-histone deacetylase 3 complex inhibits PPARgamma and adipocyte differentiation". Dev. Cell 3 (6): 903–10. doi:10.1016/S1534-5807(02)00360-X. PMID 12479814. 
30. ^ Ogawa, S; Inoue S, Watanabe T, Hiroi H, Orimo A, Hosoi T, Ouchi Y, Muramatsu M (Feb. 1998). "The complete primary structure of human estrogen receptor beta (hER beta) and its heterodimerization with ER alpha in vivo and in vitro". Biochem. Biophys. Res. Commun. 243 (1): 122–6. doi:10.1006/bbrc.1997.7893. ISSN 0006-291X. PMID 9473491. 
31. ^ Poelzl, G; Kasai Y, Mochizuki N, Shaul P W, Brown M, Mendelsohn M E (Mar. 2000). "Specific association of estrogen receptor β with the cell cycle spindle assembly checkpoint protein, MAD2". Proc. Natl. Acad. Sci. U.S.A. 97 (6): 2836–9. doi:10.1073/pnas.050580997. PMC 16016. PMID 10706629. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=16016. 
32. ^ Schuur, E R; Loktev A V, Sharma M, Sun Z, Roth R A, Weigel R J (Sep. 2001). "Ligand-dependent interaction of estrogen receptor-alpha with members of the forkhead transcription factor family". J. Biol. Chem. 276 (36): 33554–60. doi:10.1074/jbc.M105555200. PMID 11435445. 
33. ^ Chen, D; Riedl T, Washbrook E, Pace P E, Coombes R C, Egly J M, Ali S (Jul. 2000). "Activation of estrogen receptor alpha by S118 phosphorylation involves a ligand-dependent interaction with TFIIH and participation of CDK7". Mol. Cell 6 (1): 127–37. doi:10.1016/S1097-2765(00)00014-9. PMID 10949034. 
34. ^ Nair, S C; Toran E J, Rimerman R A, Hjermstad S, Smithgall T E, Smith D F (Dec. 1996). "A pathway of multi-chaperone interactions common to diverse regulatory proteins: estrogen receptor, Fes tyrosine kinase, heat shock transcription factor Hsf1, and the aryl hydrocarbon receptor". Cell Stress Chaperones 1 (4): 237–50. doi:10.1379/1466-1268(1996)001<0237:APOMCI>2.3.CO;2. PMC 376461. PMID 9222609. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=376461. 
35. ^ Lee, Mi Ock; Kim Eun Ok, Kwon Ho Jeong, Kim Young Mi, Kang Hyo Jin, Kang Heonjoong, Lee Jong Eun (Feb. 2002). "Radicicol represses the transcriptional function of the estrogen receptor by suppressing the stabilization of the receptor by heat shock protein 90". Mol. Cell. Endocrinol. 188 (1–2): 47–54. doi:10.1016/S0303-7207(01)00753-5. PMID 11911945. 
36. ^ Gay, F; Anglade I, Gong Z, Salbert G (Oct. 2000). "The LIM/homeodomain protein islet-1 modulates estrogen receptor functions". Mol. Endocrinol. 14 (10): 1627–48. doi:10.1210/me.14.10.1627. PMID 11043578. 
37. ^ Chan, S W; Hong W (Jul. 2001). "Retinoblastoma-binding protein 2 (Rbp2) potentiates nuclear hormone receptor-mediated transcription". J. Biol. Chem. 276 (30): 28402–12. doi:10.1074/jbc.M100313200. PMID 11358960. 
38. ^ Abbondanza, C; Rossi V, Roscigno A, Gallo L, Belsito A, Piluso G, Medici N, Nigro V, Molinari A M, Moncharmont B, Puca G A (Jun. 1998). "Interaction of Vault Particles with Estrogen Receptor in the MCF-7 Breast Cancer Cell". J. Cell Biol. 141 (6): 1301–10. doi:10.1083/jcb.141.6.1301. PMC 2132791. PMID 9628887. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2132791. 
39. ^ ^{a b c} Kitagawa, Hirochika; Fujiki Ryoji, Yoshimura Kimihiro, Mezaki Yoshihiro, Uematsu Yoshikatsu, Matsui Daisuke, Ogawa Satoko, Unno Kiyoe, Okubo Mataichi, Tokita Akifumi, Nakagawa Takeya, Ito Takashi, Ishimi Yukio, Nagasawa Hiromichi, Matsumoto Toshio, Yanagisawa Junn, Kato Shigeaki (Jun. 2003). "The chromatin-remodeling complex WINAC targets a nuclear receptor to promoters and is impaired in Williams syndrome". Cell 113 (7): 905–17. doi:10.1016/S0092-8674(03)00436-7. PMID 12837248. 
40. ^ ^{a b} Teo, A K; Oh H K, Ali R B, Li B F (Oct. 2001). "The Modified Human DNA Repair Enzyme O6-Methylguanine-DNA Methyltransferase Is a Negative Regulator of Estrogen Receptor-Mediated Transcription upon Alkylation DNA Damage". Mol. Cell. Biol. 21 (20): 7105–14. doi:10.1128/MCB.21.20.7105-7114.2001. PMC 99886. PMID 11564893. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=99886. 
41. ^ Talukder, Amjad H; Mishra Sandip K, Mandal Mahitosh, Balasenthil Seetharaman, Mehta Sonal, Sahin Aysegul A, Barnes Christopher J, Kumar Rakesh (Mar. 2003). "MTA1 interacts with MAT1, a cyclin-dependent kinase-activating kinase complex ring finger factor, and regulates estrogen receptor transactivation functions". J. Biol. Chem. 278 (13): 11676–85. doi:10.1074/jbc.M209570200. PMID 12527756. 
42. ^ Kumar, Rakesh; Wang Rui-An, Mazumdar Abhijit, Talukder Amjad H, Mandal Mahitosh, Yang Zhibo, Bagheri-Yarmand Rozita, Sahin Aysegul, Hortobagyi Gabriel, Adam Liana, Barnes Christopher J, Vadlamudi Ratna K (Aug. 2002). "A naturally occurring MTA1 variant sequesters oestrogen receptor-alpha in the cytoplasm". Nature 418 (6898): 654–7. doi:10.1038/nature00889. PMID 12167865. 
43. ^ Mazumdar, A; Wang R A, Mishra S K, Adam L, Bagheri-Yarmand R, Mandal M, Vadlamudi R K, Kumar R (Jan. 2001). "Transcriptional repression of oestrogen receptor by metastasis-associated protein 1 corepressor". Nat. Cell Biol. 3 (1): 30–7. doi:10.1038/35050532. PMID 11146623. 
44. ^ Lee, S K; Anzick S L, Choi J E, Bubendorf L, Guan X Y, Jung Y K, Kallioniemi O P, Kononen J, Trent J M, Azorsa D, Jhun B H, Cheong J H, Lee Y C, Meltzer P S, Lee J W (Nov. 1999). "A nuclear factor, ASC-2, as a cancer-amplified transcriptional coactivator essential for ligand-dependent transactivation by nuclear receptors in vivo". J. Biol. Chem. 274 (48): 34283–93. doi:10.1074/jbc.274.48.34283. PMID 10567404. 
45. ^ Ko, Lan; Cardona Guemalli R, Iwasaki Toshiharu, Bramlett Kelli S, Burris Thomas P, Chin William W (Jan. 2002). "Ser-884 adjacent to the LXXLL motif of coactivator TRBP defines selectivity for ERs and TRs". Mol. Endocrinol. 16 (1): 128–40. doi:10.1210/me.16.1.128. PMID 11773444. 
46. ^ ^{a b} DiRenzo, J; Shang Y, Phelan M, Sif S, Myers M, Kingston R, Brown M (Oct. 2000). "BRG-1 Is Recruited to Estrogen-Responsive Promoters and Cooperates with Factors Involved in Histone Acetylation". Mol. Cell. Biol. 20 (20): 7541–9. doi:10.1128/MCB.20.20.7541-7549.2000. PMC 86306. PMID 11003650. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=86306. 
47. ^ Kalkhoven, E; Valentine J E, Heery D M, Parker M G (Jan. 1998). "Isoforms of steroid receptor co-activator 1 differ in their ability to potentiate transcription by the oestrogen receptor". EMBO J. 17 (1): 232–43. doi:10.1093/emboj/17.1.232. PMC 1170374. PMID 9427757. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1170374. 
48. ^ Wärnmark, Anette; Treuter Eckardt, Gustafsson Jan-Ake, Hubbard Roderick E, Brzozowski Andrzej M, Pike Ashley C W (Jun. 2002). "Interaction of transcriptional intermediary factor 2 nuclear receptor box peptides with the coactivator binding site of estrogen receptor alpha". J. Biol. Chem. 277 (24): 21862–8. doi:10.1074/jbc.M200764200. PMID 11937504. 
49. ^ He, Bin; Wilson Elizabeth M (Mar. 2003). "Electrostatic Modulation in Steroid Receptor Recruitment of LXXLL and FXXLF Motifs". Mol. Cell. Biol. 23 (6): 2135–50. doi:10.1128/MCB.23.6.2135-2150.2003. PMC 149467. PMID 12612084. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=149467. 
50. ^ Fenne, Ingvild S; Hoang Tuyen, Hauglid Marianne, Sagen Jørn Vegard, Lien Ernst A, Mellgren Gunnar (Sep. 2008). "Recruitment of coactivator glucocorticoid receptor interacting protein 1 to an estrogen receptor transcription complex is regulated by the 3',5'-cyclic adenosine 5'-monophosphate-dependent protein kinase". Endocrinology 149 (9): 4336–45. doi:10.1210/en.2008-0037. PMID 18499756. 
51. ^ Wong, C W; Komm B, Cheskis B J (Jun. 2001). "Structure-function evaluation of ER alpha and beta interplay with SRC family coactivators. ER selective ligands". Biochemistry 40 (23): 6756–65. doi:10.1021/bi010379h. PMID 11389589. 
52. ^ Tikkanen, M K; Carter D J, Harris A M, Le H M, Azorsa D O, Meltzer P S, Murdoch F E (Nov. 2000). "Endogenously expressed estrogen receptor and coactivator AIB1 interact in MCF-7 human breast cancer cells". Proc. Natl. Acad. Sci. U.S.A. 97 (23): 12536–40. doi:10.1073/pnas.220427297. PMC 18799. PMID 11050174. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=18799. 
53. ^ Cavaillès, V; Dauvois S, L'Horset F, Lopez G, Hoare S, Kushner P J, Parker M G (Aug. 1995). "Nuclear factor RIP140 modulates transcriptional activation by the estrogen receptor". EMBO J. 14 (15): 3741–51. PMC 394449. PMID 7641693. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=394449. 
54. ^ ^{a b} Thénot, S; Henriquet C, Rochefort H, Cavaillès V (May. 1997). "Differential interaction of nuclear receptors with the putative human transcriptional coactivator hTIF1". J. Biol. Chem. 272 (18): 12062–8. doi:10.1074/jbc.272.18.12062. PMID 9115274. 
55. ^ L'Horset, F; Dauvois S, Heery D M, Cavaillès V, Parker M G (Nov. 1996). "RIP-140 interacts with multiple nuclear receptors by means of two distinct sites". Mol. Cell. Biol. 16 (11): 6029–36. PMC 231605. PMID 8887632. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=231605. 
56. ^ ^{a b} Johnsen, Steven A; Güngör Cenap, Prenzel Tanja, Riethdorf Sabine, Riethdorf Lutz, Taniguchi-Ishigaki Naoko, Rau Thomas, Tursun Baris, Furlow J David, Sauter Guido, Scheffner Martin, Pantel Klaus, Gannon Frank, Bach Ingolf (Jan. 2009). "Regulation of Estrogen-Dependent Transcription by the LIM Cofactors CLIM and RLIM in Breast Cancer". Cancer Res. 69 (1): 128–36. doi:10.1158/0008-5472.CAN-08-1630. PMC 2713826. PMID 19117995. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2713826. 
57. ^ ^{a b} Budhram-Mahadeo, V; Parker M, Latchman D S (Feb. 1998). "POU Transcription Factors Brn-3a and Brn-3b Interact with the Estrogen Receptor and Differentially Regulate Transcriptional Activity via an Estrogen Response Element". Mol. Cell. Biol. 18 (2): 1029–41. PMC 108815. PMID 9448000. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=108815. 
58. ^ Abbondanza, C; Medici N, Nigro V, Rossi V, Gallo L, Piluso G, Belsito A, Roscigno A, Bontempo P, Puca A A, Molinari A M, Moncharmont B, Puca G A (Mar. 2000). "The retinoblastoma-interacting zinc-finger protein RIZ is a downstream effector of estrogen action". Proc. Natl. Acad. Sci. U.S.A. 97 (7): 3130–5. doi:10.1073/pnas.050015697. PMC 16204. PMID 10706618. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=16204. 
59. ^ Qi, Chao; Chang Jeffrey, Zhu Yiwei, Yeldandi Anjana V, Rao Sambasiva M, Zhu Yi-Jun (Aug. 2002). "Identification of protein arginine methyltransferase 2 as a coactivator for estrogen receptor alpha". J. Biol. Chem. 277 (32): 28624–30. doi:10.1074/jbc.M201053200. PMID 12039952. 
60. ^ Jung, Dong-Ju; Na Soon-Young, Na Doe Sun, Lee Jae Woon (Jan. 2002). "Molecular cloning and characterization of CAPER, a novel coactivator of activating protein-1 and estrogen receptors". J. Biol. Chem. 277 (2): 1229–34. doi:10.1074/jbc.M110417200. PMID 11704680. 
61. ^ Townson, Steven M; Kang Kaiyan, Lee Adrian V, Oesterreich Steffi (Jun. 2004). "Structure-function analysis of the estrogen receptor alpha corepressor scaffold attachment factor-B1: identification of a potent transcriptional repression domain". J. Biol. Chem. 279 (25): 26074–81. doi:10.1074/jbc.M313726200. PMID 15066997. 
62. ^ Oesterreich, S; Zhang Q, Hopp T, Fuqua S A, Michaelis M, Zhao H H, Davie J R, Osborne C K, Lee A V (Mar. 2000). "Tamoxifen-bound estrogen receptor (ER) strongly interacts with the nuclear matrix protein HET/SAF-B, a novel inhibitor of ER-mediated transactivation". Mol. Endocrinol. 14 (3): 369–81. doi:10.1210/me.14.3.369. PMID 10707955. 
63. ^ Townson, Steven M; Dobrzycka Klaudia M, Lee Adrian V, Air Mamie, Deng Wanleng, Kang Kaiyan, Jiang Shiming, Kioka Noriyuki, Michaelis Kai, Oesterreich Steffi (May. 2003). "SAFB2, a new scaffold attachment factor homolog and estrogen receptor corepressor". J. Biol. Chem. 278 (22): 20059–68. doi:10.1074/jbc.M212988200. PMID 12660241. 
64. ^ Song, Robert X-D; McPherson Robert A, Adam Liana, Bao Yongde, Shupnik Margaret, Kumar Rakesh, Santen Richard J (Jan. 2002). "Linkage of rapid estrogen action to MAPK activation by ERalpha-Shc association and Shc pathway activation". Mol. Endocrinol. 16 (1): 116–27. doi:10.1210/me.16.1.116. PMID 11773443. 
65. ^ Seol, W; Hanstein B, Brown M, Moore D D (Oct. 1998). "Inhibition of estrogen receptor action by the orphan receptor SHP (short heterodimer partner)". Mol. Endocrinol. 12 (10): 1551–7. doi:10.1210/me.12.10.1551. PMID 9773978. 
66. ^ Klinge, Carolyn M; Jernigan Sarah C, Risinger Kelly E (Mar. 2002). "The agonist activity of tamoxifen is inhibited by the short heterodimer partner orphan nuclear receptor in human endometrial cancer cells". Endocrinology 143 (3): 853–67. doi:10.1210/en.143.3.853. PMID 11861507. 
67. ^ Ichinose, H; Garnier J M, Chambon P, Losson R (Mar. 1997). "Ligand-dependent interaction between the estrogen receptor and the human homologues of SWI2/SNF2". Gene 188 (1): 95–100. doi:10.1016/S0378-1119(96)00785-8. PMID 9099865. 
68. ^ Belandia, Borja; Orford Rob L, Hurst Helen C, Parker Malcolm G (Aug. 2002). "Targeting of SWI/SNF chromatin remodelling complexes to estrogen-responsive genes". EMBO J. 21 (15): 4094–103. doi:10.1093/emboj/cdf412. PMC 126156. PMID 12145209. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=126156. 
69. ^ Migliaccio, A; Castoria G, Di Domenico M, de Falco A, Bilancio A, Lombardi M, Barone M V, Ametrano D, Zannini M S, Abbondanza C, Auricchio F (Oct. 2000). "Steroid-induced androgen receptor–oestradiol receptor β–Src complex triggers prostate cancer cell proliferation". EMBO J. 19 (20): 5406–17. doi:10.1093/emboj/19.20.5406. PMC 314017. PMID 11032808. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=314017. 
70. ^ Kim, H J; Yi J Y, Sung H S, Moore D D, Jhun B H, Lee Y C, Lee J W (Sep. 1999). "Activating Signal Cointegrator 1, a Novel Transcription Coactivator of Nuclear Receptors, and Its Cytosolic Localization under Conditions of Serum Deprivation". Mol. Cell. Biol. 19 (9): 6323–32. PMC 84603. PMID 10454579. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=84603. 
71. ^ Slentz-Kesler, K; Moore J T, Lombard M, Zhang J, Hollingsworth R, Weiner M P (Oct. 2000). "Identification of the human Mnk2 gene (MKNK2) through protein interaction with estrogen receptor beta". Genomics 69 (1): 63–71. doi:10.1006/geno.2000.6299. PMID 11013076. 
72. ^ Hu, Yueh-Chiang; Shyr Chih-Rong, Che Wenyi, Mu Xiao-Min, Kim Eungseok, Chang Chawnshang (Sep. 2002). "Suppression of estrogen receptor-mediated transcription and cell growth by interaction with TR2 orphan receptor". J. Biol. Chem. 277 (37): 33571–9. doi:10.1074/jbc.M203531200. PMID 12093804. 
73. ^ Shyr, Chih-Rong; Hu Yueh-Chiang, Kim Eungseok, Chang Chawnshang (Apr. 2002). "Modulation of estrogen receptor-mediated transactivation by orphan receptor TR4 in MCF-7 cells". J. Biol. Chem. 277 (17): 14622–8. doi:10.1074/jbc.M110051200. PMID 11844790. 
74. ^ Chen, Dongsheng; Lucey Marie J, Phoenix Fladia, Lopez-Garcia Jorge, Hart Stephen M, Losson Régine, Buluwela Lakjaya, Coombes R Charles, Chambon Pierre, Schär Primo, Ali Simak (Oct. 2003). "T:G mismatch-specific thymine-DNA glycosylase potentiates transcription of estrogen-regulated genes through direct interaction with estrogen receptor alpha". J. Biol. Chem. 278 (40): 38586–92. doi:10.1074/jbc.M304286200. PMID 12874288. 
75. ^ Thénot, S; Bonnet S, Boulahtouf A, Margeat E, Royer C A, Borgna J L, Cavaillès V (Dec. 1999). "Effect of ligand and DNA binding on the interaction between human transcription intermediary factor 1alpha and estrogen receptors". Mol. Endocrinol. 13 (12): 2137–50. doi:10.1210/me.13.12.2137. PMID 10598587. 
76. ^ Ding, Lihua; Yan Jinghua, Zhu Jianhua, Zhong Hongjun, Lu Qiujun, Wang Zonghua, Huang Cuifen, Ye Qinong (Sep. 2003). "Ligand-independent activation of estrogen receptor α by XBP-1". Nucleic Acids Res. 31 (18): 5266–74. doi:10.1093/nar/gkg731. PMC 203316. PMID 12954762. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=203316. 

Further reading

• McDonnell DP, Norris JD (2002). "Connections and regulation of the human estrogen receptor". Science 296 (5573): 1642–4. doi:10.1126/science.1071884. PMID 12040178. 
• Simoncini T, Fornari L, Mannella P et al. (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, David M. (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 et al. (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 et al. (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 et al. (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 et al. (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 et al. (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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=401066. 
• 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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=454836. 
• Greene GL, Gilna P, Waterfield M et al. (1986). "Sequence and expression of human estrogen receptor complementary DNA". Science 231 (4742): 1150–4. doi:10.1126/science.3753802. PMID 3753802. 

External links

• FactorBook ERalpha_a

This article incorporates text from the United States National Library of Medicine, which is in the public domain.