Estrogen receptor alpha: Difference between revisions

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{{Infobox_gene}}
{{PBB_Controls
'''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).<ref name="entrez">{{cite web | title = Entrez Gene: ESR1 estrogen receptor 1| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2099| accessdate = }}</ref><ref name="pmid3865204">{{cite journal | vauthors = Walter P, Green S, Greene G, Krust A, Bornert JM, Jeltsch JM, Staub A, Jensen E, Scrace G, Waterfield M | title = Cloning of the human estrogen receptor cDNA | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 82 | issue = 23 | pages = 7889–93 | date = December 1985 | pmid = 3865204 | pmc = 390875 | doi = 10.1073/pnas.82.23.7889 }}</ref><ref name="pmid3753802">{{cite journal | vauthors = Greene GL, Gilna P, Waterfield M, Baker A, Hort Y, Shine J | title = Sequence and expression of human estrogen receptor complementary DNA | journal = Science | volume = 231 | issue = 4742 | pages = 1150–4 | date = March 1986 | pmid = 3753802 | doi = 10.1126/science.3753802 }}</ref>
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
==Structure==
{{GNF_Protein_box
The estrogen receptor (ER) is a [[ligand (biochemistry)|ligand]]-activated [[transcription factor]] composed of several [[protein domain|domains]] important for hormone binding, [[DNA-binding domain|DNA binding]], and [[activator (genetics)|activation]] of [[transcription (genetics)|transcription]].<ref name="pmid17132854">{{cite journal | vauthors = Dahlman-Wright K, Cavailles V, Fuqua SA, Jordan VC, Katzenellenbogen JA, Korach KS, Maggi A, Muramatsu M, Parker MG, Gustafsson JA | title = International Union of Pharmacology. LXIV. Estrogen receptors | journal = Pharmacol. Rev. | volume = 58 | issue = 4 | pages = 773–81 | date = December 2006 | pmid = 17132854 | doi = 10.1124/pr.58.4.8 }}</ref> [[Alternative splicing]] results in several ESR1 [[messenger RNA|mRNA]] transcripts, which differ primarily in their [[five prime untranslated region|5-prime untranslated regions]]. The translated receptors show less variability.<ref name="entrez2">{{cite web | title = Entrez Gene: DBI diazepam binding inhibitor (GABA receptor modulator, acyl-Coenzyme A binding protein)| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1622| accessdate = }}</ref><ref name="pmid11731608">{{cite journal | vauthors = Kos M, Reid G, Denger S, Gannon F | title = Minireview: genomic organization of the human ERalpha gene promoter region | journal = Mol. Endocrinol. | volume = 15 | issue = 12 | pages = 2057–63 | date = December 2001 | pmid = 11731608 | doi = 10.1210/me.15.12.2057 }}</ref>
| image = PBB_Protein_ESR1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1a52.
| PDB = {{PDB2|1a52}}, {{PDB2|1ere}}, {{PDB2|1err}}, {{PDB2|1g50}}, {{PDB2|1gwq}}, {{PDB2|1gwr}}, {{PDB2|1hcp}}, {{PDB2|1hcq}}, {{PDB2|1l2i}}, {{PDB2|1pcg}}, {{PDB2|1qkt}}, {{PDB2|1qku}}, {{PDB2|1r5k}}, {{PDB2|1sj0}}, {{PDB2|1uom}}, {{PDB2|1x7e}}, {{PDB2|1x7r}}, {{PDB2|1xp1}}, {{PDB2|1xp6}}, {{PDB2|1xp9}}, {{PDB2|1xpc}}, {{PDB2|1xqc}}, {{PDB2|1yim}}, {{PDB2|1yin}}, {{PDB2|1zky}}, {{PDB2|2ayr}}, {{PDB2|2b1v}}, {{PDB2|2b1z}}, {{PDB2|2b23}}, {{PDB2|2bj4}}, {{PDB2|2fai}}, {{PDB2|2g44}}, {{PDB2|2g5o}}, {{PDB2|2i0j}}, {{PDB2|2jf9}}, {{PDB2|2jfa}}, {{PDB2|2ouz}}, {{PDB2|2p15}}, {{PDB2|3erd}}, {{PDB2|3ert}}
| Name = Estrogen receptor 1
| HGNCid = 3467
| Symbol = ESR1
| AltSymbols =; ER; DKFZp686N23123; ESR; ESRA; Era; NR3A1
| OMIM = 133430
| ECnumber = 
| Homologene = 47906
| MGIid = 1352467
| Function = {{GNF_GO|id=GO:0003677 |text = DNA binding}} {{GNF_GO|id=GO:0003700 |text = transcription factor activity}} {{GNF_GO|id=GO:0003707 |text = steroid hormone receptor activity}} {{GNF_GO|id=GO:0004872 |text = receptor activity}} {{GNF_GO|id=GO:0005496 |text = steroid binding}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0008289 |text = lipid binding}} {{GNF_GO|id=GO:0030235 |text = nitric-oxide synthase regulator activity}} {{GNF_GO|id=GO:0030284 |text = estrogen receptor activity}} {{GNF_GO|id=GO:0043565 |text = sequence-specific DNA binding}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016585 |text = chromatin remodeling complex}}
| Process = {{GNF_GO|id=GO:0006355 |text = regulation of transcription, DNA-dependent}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0016049 |text = cell growth}} {{GNF_GO|id=GO:0030520 |text = estrogen receptor signaling pathway}} {{GNF_GO|id=GO:0045839 |text = negative regulation of mitosis}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 2099
    | Hs_Ensembl = ENSG00000091831
    | Hs_RefseqProtein = NP_000116
    | Hs_RefseqmRNA = NM_000125
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 6
    | Hs_GenLoc_start = 152170379
    | Hs_GenLoc_end = 152466099
    | Hs_Uniprot = P03372
    | Mm_EntrezGene = 13982
    | Mm_Ensembl = ENSMUSG00000019768
    | Mm_RefseqmRNA = XM_985634
    | Mm_RefseqProtein = XP_990728
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 10
    | Mm_GenLoc_start = 5342780
    | Mm_GenLoc_end = 5734495
    | Mm_Uniprot = Q3UT58
  }}
}}
'''Estrogen receptor alpha''' ('''ER-alpha'''), also known as '''NR3A1''' (nuclear receptor subfamily 3, group A, member 1), is a [[nuclear receptor]] which is activated by the sex hormone [[estrogen]]. ER-alpha is encoded by the human gene {{gene|ESR1}} (EStrogen Receptor 1).<ref name="entrez">{{cite web | title = Entrez Gene: ESR1 estrogen receptor 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2099| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
==Ligands==
{{PBB_Summary
 
| section_title =  
===Agonists===
| summary_text = The estrogen receptor (ESR) is a ligand-activated transcription factor composed of several domains important for hormone binding, DNA binding, and activation of transcription. Alternative splicing results in several ESR1 mRNA transcripts, which differ primarily in their 5-prime untranslated regions. The translated receptors show less variability.[supplied by OMIM]<ref name="entrez">{{cite web | title = Entrez Gene: ESR1 estrogen receptor 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2099| accessdate = }}</ref>
 
}}
====Non-selective====
* [[Endogenous]] [[estrogen]]s (e.g., [[estradiol]], [[estrone]], [[estriol]], [[estetrol]])
* [[Natural product|Natural]] [[estrogen]]s (e.g., [[conjugated equine estrogen]]s)
* [[Synthetic compound|Synthetic]] [[estrogen]]s (e.g., [[ethinylestradiol]], [[diethylstilbestrol]])
 
====Selective====
Agonists of ERα selective over [[ERβ]] include:
 
* [[Propylpyrazoletriol]] (PPT)
* [[16α-LE2|16α-LE<sub>2</sub>]] (Cpd1471)
* [[16α-Iodo-E2|16α-IE<sub>2</sub>]]
* [[ERA-63]] (ORG-37663)
* [[SKF-82,958]] – also a [[D1-like receptor|D<sub>1</sub>-like receptor]] [[full agonist]]
* [[(R,R)-Tetrahydrochrysene]] ((R,R)-THC) – actually not selective over ERβ, but rather an antagonist instead of an agonist of ERβ
 
===Mixed===
* [[Phytoestrogen]]s (e.g., [[coumestrol]], [[daidzein]], [[genistein]], [[miroestrol]])
* [[Selective estrogen receptor modulator]]s (e.g., [[tamoxifen]], [[clomifene]], [[raloxifene]])
 
===Antagonists===
 
====Non-selective====
* [[Antiestrogen]]s (e.g., [[fulvestrant]], [[ICI-164384]], [[ethamoxytriphetol]])
 
====Selective====
Antagonists of ERα selective over ERβ include:
 
* [[Methylpiperidinopyrazole]] (MPP)
 
== Tissue distribution and function ==
ERα plays a role in the physiological development and function of a variety of [[organ systems]] to varying degrees, including the [[Reproductive system|reproductive]], [[Central nervous system|central nervous]], [[Skeleton|skeletal]], and [[Circulatory system|cardiovascular systems]].<ref name="Bondesson_2015">{{cite journal | vauthors = Bondesson M, Hao R, Lin CY, Williams C, Gustafsson JÅ | title = Estrogen receptor signaling during vertebrate development | journal = Biochimica et Biophysica Acta | volume = 1849 | issue = 2 | pages = 142–51 | date = February 2015 | pmid = 24954179 | pmc = 4269570 | doi = 10.1016/j.bbagrm.2014.06.005 }}</ref> Accordingly, ERα is widely expressed throughout the body, including the [[uterus]] and [[ovary]], [[Male reproductive system|male reproductive organs]], [[mammary gland]], [[Bone|bone,]] [[heart]], [[hypothalamus]], [[pituitary gland]], [[liver]], [[lung]], [[kidney]], [[spleen]], and [[Adipose tissue|adipose]] tissue.<ref name="Bondesson_2015" /><ref name="Curtis_Hewitt_2000">{{cite journal | vauthors = Curtis Hewitt S, Couse JF, Korach KS | title = Estrogen receptor transcription and transactivation: Estrogen receptor knockout mice: what their phenotypes reveal about mechanisms of estrogen action | journal = Breast Cancer Research | volume = 2 | issue = 5 | pages = 345–52 | date = 2000 | pmid = 11250727 | doi = 10.1186/bcr79 | pmc=138656}}</ref><ref name="Paterni_2014">{{cite journal | vauthors = Paterni I, Granchi C, Katzenellenbogen JA, Minutolo F | title = Estrogen receptors alpha (ERα) and beta (ERβ): subtype-selective ligands and clinical potential | journal = Steroids | volume = 90 | pages = 13–29 | date = November 2014 | pmid = 24971815 | pmc = 4192010 | doi = 10.1016/j.steroids.2014.06.012 }}</ref> The development and function of these tissues is disrupted in [[Model organism|animal models]] lacking active ERα genes, such as the ERα [[knockout mouse]] (ERKO), providing a preliminary understanding of ERα function at specific [[Biological target|target]] organs.<ref name="Bondesson_2015" /><ref name="Lee_2012">{{cite journal | vauthors = Lee HR, Kim TH, Choi KC | title = Functions and physiological roles of two types of estrogen receptors, ERα and ERβ, identified by estrogen receptor knockout mouse | journal = Laboratory Animal Research | volume = 28 | issue = 2 | pages = 71–6 | date = June 2012 | pmid = 22787479 | pmc = 3389841 | doi = 10.5625/lar.2012.28.2.71 }}</ref>
 
=== Uterus and ovary ===
ERα is essential in the maturation of the [[Female reproductive system|female reproductive phenotype]]. In the absence of ERα, the ERKO mouse develops an adult [[uterus]], indicating that ERα may not mediate the initial growth of the uterus.<ref name="Bondesson_2015" /><ref name="Curtis_Hewitt_2000" /> However, ERα plays a role in the completion of this development, and the subsequent function of the tissue.<ref name="Lee_2012" /> Activation of ERα is known to trigger [[Cell growth|cell proliferation]] in the uterus.<ref name="Paterni_2014" /> The [[uterus]] of female ERKO mice is [[Hypoplasia|hypoplastic]], suggesting that ERα mediates [[mitosis]] and [[Cellular differentiation|differentiation]] in the uterus in response to [[estrogen]] stimulation.<ref name="Curtis_Hewitt_2000" />
 
Similarly, [[Preadolescence|prepubertal]] female ERKO mice develop [[Ovary|ovaries]] that are nearly indistinguishable from those of their [[Wild type|wildtype]] counterparts. However, as the ERKO mice mature they progressively present an abnormal [[Ovary|ovarian]] phenotype in both [[physiology]] and function.<ref name="Curtis_Hewitt_2000" /><ref name="Lee_2012" /> Specifically, female ERKO mice develop enlarged [[Ovary|ovaries]] containing [[hemorrhagic]] [[Follicular cyst of ovary|follicular cysts]], which also lack the [[corpus luteum]], and therefore do not [[Ovulation|ovulate]].<ref name="Bondesson_2015" /><ref name="Curtis_Hewitt_2000" /><ref name="Lee_2012" /> This adult [[Ovary|ovarian]] phenotype suggests that in the absence of ERα, [[estrogen]] is no longer able to perform [[negative feedback]] on the [[hypothalamus]], resulting in [[Chronic condition|chronically]] elevated [[Luteinizing hormone|LH]] levels and constant [[Ovary|ovarian]] stimulation.<ref name="Curtis_Hewitt_2000" /> These results identify a pivotal role for ERα in the [[hypothalamus]], in addition to its role in the [[estrogen]]-driven maturation through [[theca]] and [[Interstitial cell|interstitial cells]] of the [[ovary]].<ref name="Curtis_Hewitt_2000" />
 
=== Male reproductive organs ===
ERα is similarly essential in the maturation and maintenance of the [[Male reproductive system|male reproductive phenotype]], as male ERKO mice are [[Infertility|infertile]] and present undersized [[Testicle|testes]].<ref name="Bondesson_2015" /><ref name="Lee_2012" /> The integrity of [[Testicle|testicular structures]] of ERKO mice, such as the [[Seminiferous tubule|seminiferous tubules]] of the [[Testicle|testes]] and the [[Germinal epithelium (male)|seminiferous epithelium]], declines over time.<ref name="Bondesson_2015" /><ref name="Curtis_Hewitt_2000" /> Furthermore, the [[Fitness (biology)|reproductive performance]] of male ERKO mice is hindered abnormalities in [[Sex organ|sexual physiology]] and [[Reproductive behavior of mice|behavior]], such as impaired [[spermatogenesis]] and loss of [[Intromittent organ|intromission]] <nowiki/>and [[Ejaculation|ejaculatory]] responses.<ref name="Bondesson_2015" /><ref name="Curtis_Hewitt_2000" />
 
=== Mammary gland ===
[[Estrogen]] stimulation of ERα is known to stimulate [[Cell growth|cell proliferation]] in breast tissue.<ref name="Paterni_2014" /> ERα may be responsible for [[Puberty|pubertal]] development of the adult [[phenotype]], through mediation of [[mammary gland]] response to [[Endocrine system|ovarian hormones]].<ref name="Lee_2012" /> This role is consistent with the abnormalities of female ERKO mice: the [[Lactiferous duct|epithelial ducts]] of female ERKO mice fail to grow beyond their [[Preadolescence|pre-pubertal]] length, and [[Lactation|lactational]] structures do not develop.<ref name="Curtis_Hewitt_2000" /> As a result, the functions of the [[mammary gland]] -- including both [[lactation]] <nowiki/>and release of [[prolactin]] -- are greatly impaired in ERKO mice.<ref name="Lee_2012" />
 
=== Bone ===
Though its expression in [[bone]] is moderate, ERα is known to be responsible for maintenance of [[Bone health|bone integrity]].<ref name="Paterni_2014" /><ref name="Lee_2012" /> It is hypothesized that [[estrogen]] stimulation of ERα may trigger the release of [[Growth factor|growth factors]], such as [[epidermal growth factor]] or [[Insulin-like growth factor 1|insulin-like growth factor-1]], which in turn regulate [[Bone|bone development]] and maintenance.<ref name="Lee_2012" /><ref name="Curtis_Hewitt_2000" /> Accordingly, male and female ERKO mice exhibit decreased bone [[length]] and [[size]].<ref name="Lee_2012" /><ref name="Curtis_Hewitt_2000" />
 
=== Brain ===
[[Estrogen]] signaling through ERα appears to be responsible for various aspects of [[Central nervous system|central nervous development]], such as [[synaptogenesis]] and [[Synaptic plasticity|synaptic remodeling]].<ref name="Lee_2012" /> In the brain, ERα is found in [[hypothalamus]], and [[preoptic area]], and [[arcuate nucleus]], all three of which have been linked to [[Reproduction|reproductive behavior]], and the [[Virilization|masculinization]] of the mouse brain appears to take place through ERα function.<ref name="Bondesson_2015" /><ref name="Lee_2012" /> Furthermore, studies in models of [[psychopathology]] and [[Neurodegeneration|neurodegenerative disease]] states suggest that [[Estrogen receptor|estrogen receptors]] mediate the [[Neuroprotection|neuroprotective]] role of [[estrogen]] in the brain.<ref name="Bondesson_2015" /><ref name="Paterni_2014" /> Finally, ERα appears to mediate [[positive feedback]] effects of [[estrogen]] on the brain's secretion of [[Gonadotropin-releasing hormone|GnRH]] and [[Luteinizing hormone|LH]], by way increasing expression of [[kisspeptin]] in neurons of the [[arcuate nucleus]] and [[anteroventral periventricular nucleus]].<ref>{{cite journal | vauthors = Clarkson J | title = Effects of estradiol on kisspeptin neurons during puberty | journal = Frontiers in Neuroendocrinology | volume = 34 | issue = 2 | pages = 120–31 | date = April 2013 | pmid = 23500175 | doi = 10.1016/j.yfrne.2013.02.002 }}</ref><ref>{{cite journal | vauthors = Moenter SM, Chu Z, Christian CA | title = Neurobiological mechanisms underlying oestradiol negative and positive feedback regulation of gonadotrophin-releasing hormone neurones | journal = Journal of Neuroendocrinology | volume = 21 | issue = 4 | pages = 327–33 | date = March 2009 | pmid = 19207821 | pmc = 2738426 | doi = 10.1111/j.1365-2826.2009.01826.x }}</ref> Although classical studies have suggested that [[negative feedback]] effects of [[estrogen]] also operate through ERα, female mice lacking ERα in [[kisspeptin]]-expressing neurons continue to demonstrate a degree of [[negative feedback]] response.<ref>{{cite journal | vauthors = Plant TM | title = 60 YEARS OF NEUROENDOCRINOLOGY: The hypothalamo-pituitary-gonadal axis | journal = The Journal of Endocrinology | volume = 226 | issue = 2 | pages = T41-54 | date = August 2015 | pmid = 25901041 | pmc = 4498991 | doi = 10.1530/JOE-15-0113 }}</ref>
 
==Clinical significance==
[[Estrogen insensitivity syndrome]] is a very rare condition characterized by a defective ERα that is insensitive to estrogens.<ref name="JamesonGroot2015">{{cite book | first1 = J. Larry | last1 = Jameson | first2 = Leslie J. | last2 = De Groot | name-list-format = vanc | title = Endocrinology: Adult and Pediatric | url = https://books.google.com/books?id=xmLeBgAAQBAJ&pg=PT238 | date = February 2015 | publisher = Elsevier Health Sciences | isbn = 978-0-323-32195-2 | pages = 238– }}</ref><ref name="pmid8701078">{{cite journal | vauthors = Korach KS, Couse JF, Curtis SW, Washburn TF, Lindzey J, Kimbro KS, Eddy EM, Migliaccio S, Snedeker SM, Lubahn DB, Schomberg DW, Smith EP | title = Estrogen receptor gene disruption: molecular characterization and experimental and clinical phenotypes | journal = Recent Progress in Hormone Research | volume = 51 | issue =  | pages = 159–86; discussion 186–8 | year = 1996 | pmid = 8701078 | doi =  }}</ref><ref name="SmithBoyd1994">{{cite journal | vauthors = Smith EP, Boyd J, Frank GR, Takahashi H, Cohen RM, Specker B, Williams TC, Lubahn DB, Korach KS | title = Estrogen resistance caused by a mutation in the estrogen-receptor gene in a man | journal = The New England Journal of Medicine | volume = 331 | issue = 16 | pages = 1056–61 | date = Oct 1994 | pmid = 8090165 | doi = 10.1056/NEJM199410203311604 }}</ref><ref name="QuaynorStradtman2013">{{cite journal | vauthors = Quaynor SD, Stradtman EW, Kim HG, Shen Y, Chorich LP, Schreihofer DA, Layman LC | title = Delayed puberty and estrogen resistance in a woman with estrogen receptor α variant | journal = The New England Journal of Medicine | volume = 369 | issue = 2 | pages = 164–71 | date = Jul 2013 | pmid = 23841731 | doi = 10.1056/NEJMoa1303611 | pmc=3823379}}</ref> The clinical presentation of a female was observed to include absence of [[breast development]] and other female [[secondary sexual characteristic]]s at [[puberty]], [[hypoplasia|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]].<ref name="QuaynorStradtman2013" /> The clinical presentation in a male was reported to include lack of [[epiphyseal closure]], [[tall stature]], [[osteoporosis]], and poor [[sperm viability]].<ref name="SmithBoyd1994" /> Both individuals were completely insensitive to exogenous estrogen treatment, even with high doses.<ref name="SmithBoyd1994" /><ref name="QuaynorStradtman2013" />
 
[[Genetic polymorphism]]s in the gene encoding the ERα have been associated with [[breast cancer]] in women and [[gynecomastia]] in men.<ref name="pmid28599754">{{cite journal | vauthors = Jahandoost S, Farhanghian P, Abbasi S | title = The Effects of Sex Protein Receptors and Sex Steroid Hormone Gene Polymorphisms on Breast Cancer Risk | journal = J Natl Med Assoc | volume = 109 | issue = 2 | pages = 126–138 | year = 2017 | pmid = 28599754 | doi = 10.1016/j.jnma.2017.02.003 }}</ref><ref name="pmid24625355">{{cite journal | vauthors = Eren E, Edgunlu T, Korkmaz HA, Cakir ED, Demir K, Cetin ES, Celik SK | title = Genetic variants of estrogen beta and leptin receptors may cause gynecomastia in adolescent | journal = Gene | volume = 541 | issue = 2 | pages = 101–6 | year = 2014 | pmid = 24625355 | doi = 10.1016/j.gene.2014.03.013 }}</ref>
 
==Coactivators==
[[Coactivator (genetics)|Coactivators]] of ER-α include:
* [[Nuclear receptor coactivator 1|SRC-1]]<ref name="Shang_2002">{{cite journal | vauthors = Shang Y, Brown M | title = Molecular determinants for the tissue specificity of SERMs | journal = Science | volume = 295 | issue = 5564 | pages = 2465–8 | year = 2002 | pmid = 11923541 | doi = 10.1126/science.1068537 }}</ref><ref name="Smith_2004">{{cite journal | vauthors = Smith CL, O'Malley BW | title = Coregulator function: a key to understanding tissue specificity of selective receptor modulators | journal = Endocr Rev | volume = 25 | issue = 1 | pages = 45–71 | year = 2004 | pmid = 14769827 | doi = 10.1210/er.2003-0023 }}</ref>
* [[Nuclear receptor coactivator 3|AIB1]] – amplified in breast 1<ref name="Anzick_1997">{{cite journal | vauthors = Anzick SL, Kononen J, Walker RL, Azorsa DO, Tanner MM, Guan XY, Sauter G, Kallioniemi OP, Trent JM, Meltzer PS | title = AIB1, a steroid receptor coactivator amplified in breast and ovarian cancer | journal = Science | volume = 277 | issue = 5328 | pages = 965–8 | year = 1997 | pmid = 9252329 | doi = 10.1126/science.277.5328.965 }}</ref>
* [[BCAS3]] – Breast carcinoma amplified sequence 3<ref name="pmid17505058">{{cite journal | vauthors = Gururaj AE, Peng S, Vadlamudi RK, Kumar R | title = Estrogen induces expression of BCAS3, a novel estrogen receptor-alpha coactivator, through proline-, glutamic acid-, and leucine-rich protein-1 (PELP1) | journal = Mol. Endocrinol. | volume = 21 | issue = 8 | pages = 1847–60 | date = August 2007 | pmid = 17505058 | doi = 10.1210/me.2006-0514 }}</ref>
* [[PELP-1]] – Proline-, glutamic acid-, leucine-rich protein 1<ref name="pmid11481323">{{cite journal | vauthors = Vadlamudi RK, Wang RA, Mazumdar A, Kim Y, Shin J, Sahin A, Kumar R | title = Molecular cloning and characterization of PELP1, a novel human coregulator of estrogen receptor alpha | journal = J. Biol. Chem. | volume = 276 | issue = 41 | pages = 38272–9 | year = 2001 | pmid = 11481323 | doi = 10.1074/jbc.M103783200 }}</ref>
 
==Interactions==
Estrogen receptor alpha has been shown to [[Protein-protein interaction|interact]] with:
{{div col|colwidth=10em}}
* [[AKAP13]]<ref name=pmid9627117>{{cite journal | vauthors = Rubino D, Driggers P, Arbit D, Kemp L, Miller B, Coso O, Pagliai K, Gray K, Gutkind S, Segars J | title = Characterization of Brx, a novel Dbl family member that modulates estrogen receptor action | journal = Oncogene | volume = 16 | issue = 19 | pages = 2513–26 | date = May 1998 | pmid = 9627117 | doi = 10.1038/sj.onc.1201783 }}</ref>
* [[Aryl hydrocarbon receptor|AHR]]<ref name=pmid12612060>{{cite journal | vauthors = Wormke M, Stoner M, Saville B, Walker K, Abdelrahim M, Burghardt R, Safe S | title = The Aryl Hydrocarbon Receptor Mediates Degradation of Estrogen Receptor α through Activation of Proteasomes | journal = Mol. Cell. Biol. | volume = 23 | issue = 6 | pages = 1843–55 | date = Mar 2003 | pmid = 12612060 | pmc = 149455 | doi = 10.1128/MCB.23.6.1843-1855.2003 }}</ref><ref name=pmid10620335>{{cite journal | vauthors = Klinge CM, Kaur K, Swanson HI | title = The aryl hydrocarbon receptor interacts with estrogen receptor alpha and orphan receptors COUP-TFI and ERRalpha1 | journal = Arch. Biochem. Biophys. | volume = 373 | issue = 1 | pages = 163–74 | date = Jan 2000 | pmid = 10620335 | doi = 10.1006/abbi.1999.1552 }}</ref>
* [[BRCA1]]<ref name=pmid11493692>{{cite journal | vauthors = Zheng L, Annab LA, Afshari CA, Lee WH, Boyer TG | title = BRCA1 mediates ligand-independent transcriptional repression of the estrogen receptor | journal = [[PNAS|Proc. Natl. Acad. Sci. U.S.A.]] | volume = 98 | issue = 17 | pages = 9587–92 | date = Aug 2001 | pmid = 11493692 | pmc = 55496 | doi = 10.1073/pnas.171174298 }}</ref><ref name=pmid11244506>{{cite journal | vauthors = Fan S, Ma YX, Wang C, Yuan RQ, Meng Q, Wang JA, Erdos M, Goldberg ID, Webb P, Kushner PJ, Pestell RG, Rosen EM | title = Role of direct interaction in BRCA1 inhibition of estrogen receptor activity | journal = Oncogene | volume = 20 | issue = 1 | pages = 77–87 | date = Jan 2001 | pmid = 11244506 | doi = 10.1038/sj.onc.1204073 }}</ref><ref name=pmid12400015>{{cite journal | vauthors = Kawai H, Li H, Chun P, Avraham S, Avraham HK | title = Direct interaction between BRCA1 and the estrogen receptor regulates vascular endothelial growth factor (VEGF) transcription and secretion in breast cancer cells | journal = Oncogene | volume = 21 | issue = 50 | pages = 7730–9 | date = Oct 2002 | pmid = 12400015 | doi = 10.1038/sj.onc.1205971 }}</ref><ref name=pmid11782371/>
* [[Caveolin 1|CAV1]]<ref name=pmid11563984>{{cite journal | vauthors = Schlegel A, Wang C, Pestell RG, Lisanti MP | title = Ligand-independent activation of oestrogen receptor alpha by caveolin-1 | journal = Biochem. J. | volume = 359 | issue = Pt 1 | pages = 203–10 | date = Oct 2001 | pmid = 11563984 | pmc = 1222136 | doi = 10.1042/0264-6021:3590203 }}</ref>
* [[CCNC (gene)|CCNC]]<ref name=pmid11867769/>
* [[CDC25B]]<ref name=pmid11689696>{{cite journal | vauthors = Ma ZQ, Liu Z, Ngan ES, Tsai SY | title = Cdc25B Functions as a Novel Coactivator for the Steroid Receptors | journal = Mol. Cell. Biol. | volume = 21 | issue = 23 | pages = 8056–67 | date = Dec 2001 | pmid = 11689696 | pmc = 99972 | doi = 10.1128/MCB.21.23.8056-8067.2001 }}</ref>
* [[CEBPB]]<ref name=pmid9817600>{{cite journal | vauthors = Boruk M, Savory JG, Haché RJ | title = AF-2-dependent potentiation of CCAAT enhancer binding protein beta-mediated transcriptional activation by glucocorticoid receptor | journal = Mol. Endocrinol. | volume = 12 | issue = 11 | pages = 1749–63 | date = Nov 1998 | pmid = 9817600 | doi = 10.1210/mend.12.11.0191 }}</ref><ref name=pmid7651415>{{cite journal | vauthors = Stein B, Yang MX | title = Repression of the interleukin-6 promoter by estrogen receptor is mediated by NF-kappa B and C/EBP beta | journal = Mol. Cell. Biol. | volume = 15 | issue = 9 | pages = 4971–9 | date = Sep 1995 | pmid = 7651415 | pmc = 230744 }}</ref>
* [[Cofactor of BRCA1|COBRA1]]<ref name=pmid15342491>{{cite journal | vauthors = Aiyar SE, Sun JL, Blair AL, Moskaluk CA, Lu YZ, Ye QN, Yamaguchi Y, Mukherjee A, Ren DM, Handa H, Li R | title = Attenuation of estrogen receptor α-mediated transcription through estrogen-stimulated recruitment of a negative elongation factor | journal = Genes Dev. | volume = 18 | issue = 17 | pages = 2134–46 | date = Sep 2004 | pmid = 15342491 | pmc = 515291 | doi = 10.1101/gad.1214104 }}</ref>
* [[COUP-TFI]]<ref name=pmid12093745>{{cite journal | vauthors = Métivier R, Gay FA, Hübner MR, Flouriot G, Salbert G, Gannon F, Kah O, Pakdel F | title = Formation of an hERα–COUP-TFI complex enhances hERα AF-1 through Ser118 phosphorylation by MAPK | journal = EMBO J. | volume = 21 | issue = 13 | pages = 3443–53 | date = Jul 2002 | pmid = 12093745 | pmc = 126093 | doi = 10.1093/emboj/cdf344 }}</ref>
* [[CREB-binding protein|CREBBP]]<ref name=pmid11782371>{{cite journal | vauthors = Fan S, Ma YX, Wang C, Yuan RQ, Meng Q, Wang JA, Erdos M, Goldberg ID, Webb P, Kushner PJ, Pestell RG, Rosen EM | title = p300 Modulates the BRCA1 inhibition of estrogen receptor activity | journal = Cancer Res. | volume = 62 | issue = 1 | pages = 141–51 | date = Jan 2002 | pmid = 11782371 }}</ref><ref name=pmid11113179>{{cite journal | vauthors = Sheppard HM, Harries JC, Hussain S, Bevan C, Heery DM | title = Analysis of the Steroid Receptor Coactivator 1 (SRC1)-CREB Binding Protein Interaction Interface and Its Importance for the Function of SRC1 | journal = Mol. Cell. Biol. | volume = 21 | issue = 1 | pages = 39–50 | date = Jan 2001 | pmid = 11113179 | pmc = 86566 | doi = 10.1128/MCB.21.1.39-50.2001 }}</ref>
* [[CRSP3]]<ref name=pmid11867769/>
* [[Cyclin D1]]<ref name=pmid9039267>{{cite journal | vauthors = Zwijsen RM, Wientjens E, Klompmaker R, van der Sman J, Bernards R, Michalides RJ | title = CDK-independent activation of estrogen receptor by cyclin D1 | journal = Cell | volume = 88 | issue = 3 | pages = 405–15 | date = Feb 1997 | pmid = 9039267 | doi = 10.1016/S0092-8674(00)81879-6 }}</ref>
* [[DDX17]]<ref name=pmid11250900/>
* [[DDX5]]<ref name=pmid11250900/><ref name=pmid10409727>{{cite journal | vauthors = Endoh H, Maruyama K, Masuhiro Y, Kobayashi Y, Goto M, Tai H, Yanagisawa J, Metzger D, Hashimoto S, Kato S | title = Purification and Identification of p68 RNA Helicase Acting as a Transcriptional Coactivator Specific for the Activation Function 1 of Human Estrogen Receptor α | journal = Mol. Cell. Biol. | volume = 19 | issue = 8 | pages = 5363–72 | date = Aug 1999 | pmid = 10409727 | pmc = 84379 }}</ref>
* [[DNTTIP2]]<ref name=pmid15047147>{{cite journal | vauthors = Bu H, Kashireddy P, Chang J, Zhu YT, Zhang Z, Zheng W, Rao SM, Zhu YJ | title = ERBP, a novel estrogen receptor binding protein enhancing the activity of estrogen receptor | journal = Biochem. Biophys. Res. Commun. | volume = 317 | issue = 1 | pages = 54–9 | date = Apr 2004 | pmid = 15047147 | doi = 10.1016/j.bbrc.2004.02.179 | issn = 0006-291X }}</ref>
* [[EP300]]<ref name=pmid11782371/><ref name=pmid11867769/><ref name=pmid12479814>{{cite journal | vauthors = Fajas L, Egler V, Reiter R, Hansen J, Kristiansen K, Debril MB, Miard S, Auwerx J | title = The retinoblastoma-histone deacetylase 3 complex inhibits PPARgamma and adipocyte differentiation | journal = Dev. Cell | volume = 3 | issue = 6 | pages = 903–10 | date = Dec 2002 | pmid = 12479814 | doi = 10.1016/S1534-5807(02)00360-X }}</ref>
* [[Estrogen receptor beta|ESR2]]<ref name=pmid9473491>{{cite journal | vauthors = Ogawa S, Inoue S, Watanabe T, Hiroi H, Orimo A, Hosoi T, Ouchi Y, Muramatsu M | title = The complete primary structure of human estrogen receptor beta (hER beta) and its heterodimerization with ER alpha in vivo and in vitro | journal = Biochem. Biophys. Res. Commun. | volume = 243 | issue = 1 | pages = 122–6 | date = Feb 1998 | pmid = 9473491 | doi = 10.1006/bbrc.1997.7893 | issn = 0006-291X }}</ref><ref name=pmid10706629>{{cite journal | vauthors = Poelzl G, Kasai Y, Mochizuki N, Shaul PW, Brown M, Mendelsohn ME | title = Specific association of estrogen receptor β with the cell cycle spindle assembly checkpoint protein, MAD2 | journal = [[PNAS|Proc. Natl. Acad. Sci. U.S.A.]] | volume = 97 | issue = 6 | pages = 2836–9 | date = Mar 2000 | pmid = 10706629 | pmc = 16016 | doi = 10.1073/pnas.050580997 }}</ref>
* [[FOXO1]]<ref name=pmid11435445>{{cite journal | vauthors = Schuur ER, Loktev AV, Sharma M, Sun Z, Roth RA, Weigel RJ | title = Ligand-dependent interaction of estrogen receptor-alpha with members of the forkhead transcription factor family | journal = J. Biol. Chem. | volume = 276 | issue = 36 | pages = 33554–60 | date = Sep 2001 | pmid = 11435445 | doi = 10.1074/jbc.M105555200 }}</ref>
* [[GREB1]]<ref name=pmid17463000>{{cite journal | vauthors = Deschênes J, Bourdeau V, White JH, Mader S | title = Regulation of GREB1 transcription by estrogen receptor alpha through a multipartite enhancer spread over 20 kb of upstream flanking sequences. | journal = J. Biol. Chem. | volume = 282 | issue = 24 | pages = 17335–17339 | date = June 2007 | pmid = 17463000 | doi = 10.1074/jbc.C700030200 }}</ref>
* [[GTF2H1]]<ref name=pmid10949034>{{cite journal | vauthors = Chen D, Riedl T, Washbrook E, Pace PE, Coombes RC, Egly JM, Ali S | title = Activation of estrogen receptor alpha by S118 phosphorylation involves a ligand-dependent interaction with TFIIH and participation of CDK7 | journal = Mol. Cell | volume = 6 | issue = 1 | pages = 127–37 | date = Jul 2000 | pmid = 10949034 | doi = 10.1016/S1097-2765(00)00014-9 }}</ref>
* [[Heat shock protein 90kDa alpha (cytosolic), member A1|HSP90AA1]]<ref name=pmid9222609>{{cite journal | vauthors = Nair SC, Toran EJ, Rimerman RA, Hjermstad S, Smithgall TE, Smith DF | title = 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 | journal = Cell Stress Chaperones | volume = 1 | issue = 4 | pages = 237–50 | date = Dec 1996 | pmid = 9222609 | pmc = 376461 | doi = 10.1379/1466-1268(1996)001<0237:APOMCI>2.3.CO;2 }}</ref><ref name=pmid11911945>{{cite journal | vauthors = Lee MO, Kim EO, Kwon HJ, Kim YM, Kang HJ, Kang H, Lee JE | title = Radicicol represses the transcriptional function of the estrogen receptor by suppressing the stabilization of the receptor by heat shock protein 90 | journal = Mol. Cell. Endocrinol. | volume = 188 | issue = 1–2 | pages = 47–54 | date = Feb 2002 | pmid = 11911945 | doi = 10.1016/S0303-7207(01)00753-5 }}</ref>
* [[ISL1]]<ref name=pmid11043578>{{cite journal | vauthors = Gay F, Anglade I, Gong Z, Salbert G | title = The LIM/homeodomain protein islet-1 modulates estrogen receptor functions | journal = Mol. Endocrinol. | volume = 14 | issue = 10 | pages = 1627–48 | date = Oct 2000 | pmid = 11043578 | doi = 10.1210/me.14.10.1627 }}</ref>
* [[JARID1A]]<ref name=pmid11358960>{{cite journal | vauthors = Chan SW, Hong W | title = Retinoblastoma-binding protein 2 (Rbp2) potentiates nuclear hormone receptor-mediated transcription | journal = J. Biol. Chem. | volume = 276 | issue = 30 | pages = 28402–12 | date = Jul 2001 | pmid = 11358960 | doi = 10.1074/jbc.M100313200 }}</ref>
* [[Major vault protein|MVP]]<ref name=pmid9628887>{{cite journal | vauthors = Abbondanza C, Rossi V, Roscigno A, Gallo L, Belsito A, Piluso G, Medici N, Nigro V, Molinari AM, Moncharmont B, Puca GA | title = Interaction of Vault Particles with Estrogen Receptor in the MCF-7 Breast Cancer Cell | journal = J. Cell Biol. | volume = 141 | issue = 6 | pages = 1301–10 | date = Jun 1998 | pmid = 9628887 | pmc = 2132791 | doi = 10.1083/jcb.141.6.1301 }}</ref>
* [[MED1]]<ref name=pmid11867769/><ref name=pmid12837248/>
* [[MED12]]<ref name=pmid11867769/>
* [[MED14]]<ref name=pmid11867769>{{cite journal | vauthors = Kang YK, Guermah M, Yuan CX, Roeder RG | title = 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 | journal = [[PNAS|Proc. Natl. Acad. Sci. U.S.A.]] | volume = 99 | issue = 5 | pages = 2642–7 | date = Mar 2002 | pmid = 11867769 | pmc = 122401 | doi = 10.1073/pnas.261715899 }}</ref>
* [[MED16]]<ref name=pmid11867769/>
* [[MED24]]<ref name=pmid11867769/><ref name=pmid12837248/>
* [[MED6]]<ref name=pmid11867769/>
* [[O-6-methylguanine-DNA methyltransferase|MGMT]]<ref name=pmid11564893/>
* [[MNAT1]]<ref name=pmid12527756>{{cite journal | vauthors = Talukder AH, Mishra SK, Mandal M, Balasenthil S, Mehta S, Sahin AA, Barnes CJ, Kumar R | title = MTA1 interacts with MAT1, a cyclin-dependent kinase-activating kinase complex ring finger factor, and regulates estrogen receptor transactivation functions | journal = J. Biol. Chem. | volume = 278 | issue = 13 | pages = 11676–85 | date = Mar 2003 | pmid = 12527756 | doi = 10.1074/jbc.M209570200 }}</ref>
* [[MTA1]]<ref name=pmid12167865>{{cite journal | vauthors = Kumar R, Wang RA, Mazumdar A, Talukder AH, Mandal M, Yang Z, Bagheri-Yarmand R, Sahin A, Hortobagyi G, Adam L, Barnes CJ, Vadlamudi RK | title = A naturally occurring MTA1 variant sequesters oestrogen receptor-alpha in the cytoplasm | journal = [[Nature (journal)|Nature]] | volume = 418 | issue = 6898 | pages = 654–7 | date = Aug 2002 | pmid = 12167865 | doi = 10.1038/nature00889 }}</ref><ref name=pmid11146623>{{cite journal | vauthors = Mazumdar A, Wang RA, Mishra SK, Adam L, Bagheri-Yarmand R, Mandal M, Vadlamudi RK, Kumar R | title = Transcriptional repression of oestrogen receptor by metastasis-associated protein 1 corepressor | journal = Nat. Cell Biol. | volume = 3 | issue = 1 | pages = 30–7 | date = Jan 2001 | pmid = 11146623 | doi = 10.1038/35050532 }}</ref>
* [[NCOA6]]<ref name=pmid10567404>{{cite journal | vauthors = Lee SK, Anzick SL, Choi JE, Bubendorf L, Guan XY, Jung YK, Kallioniemi OP, Kononen J, Trent JM, Azorsa D, Jhun BH, Cheong JH, Lee YC, Meltzer PS, Lee JW | title = A nuclear factor, ASC-2, as a cancer-amplified transcriptional coactivator essential for ligand-dependent transactivation by nuclear receptors in vivo | journal = J. Biol. Chem. | volume = 274 | issue = 48 | pages = 34283–93 | date = Nov 1999 | pmid = 10567404 | doi = 10.1074/jbc.274.48.34283 }}</ref><ref name=pmid11773444>{{cite journal | vauthors = Ko L, Cardona GR, Iwasaki T, Bramlett KS, Burris TP, Chin WW | title = Ser-884 adjacent to the LXXLL motif of coactivator TRBP defines selectivity for ERs and TRs | journal = Mol. Endocrinol. | volume = 16 | issue = 1 | pages = 128–40 | date = Jan 2002 | pmid = 11773444 | doi = 10.1210/mend.16.1.0755 }}</ref>
* [[Nuclear receptor coactivator 1|NCOA1]]<ref name=pmid11867769/><ref name=pmid11113179/><ref name=pmid11250900/><ref name=pmid11003650>{{cite journal | vauthors = DiRenzo J, Shang Y, Phelan M, Sif S, Myers M, Kingston R, Brown M | title = BRG-1 Is Recruited to Estrogen-Responsive Promoters and Cooperates with Factors Involved in Histone Acetylation | journal = Mol. Cell. Biol. | volume = 20 | issue = 20 | pages = 7541–9 | date = Oct 2000 | pmid = 11003650 | pmc = 86306 | doi = 10.1128/MCB.20.20.7541-7549.2000 }}</ref><ref name=pmid9427757>{{cite journal | vauthors = Kalkhoven E, Valentine JE, Heery DM, Parker MG | title = Isoforms of steroid receptor co-activator 1 differ in their ability to potentiate transcription by the oestrogen receptor | journal = EMBO J. | volume = 17 | issue = 1 | pages = 232–43 | date = Jan 1998 | pmid = 9427757 | pmc = 1170374 | doi = 10.1093/emboj/17.1.232 }}</ref>
* [[Nuclear receptor coactivator 2|NCOA2]]<ref name=pmid11250900>{{cite journal | vauthors = Watanabe M, Yanagisawa J, Kitagawa H, Takeyama K, Ogawa S, Arao Y, Suzawa M, Kobayashi Y, Yano T, Yoshikawa H, Masuhiro Y, Kato S | title = 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 | journal = EMBO J. | volume = 20 | issue = 6 | pages = 1341–52 | date = Mar 2001 | pmid = 11250900 | pmc = 145523 | doi = 10.1093/emboj/20.6.1341 }}</ref><ref name=pmid12837248>{{cite journal | vauthors = Kitagawa H, Fujiki R, Yoshimura K, Mezaki Y, Uematsu Y, Matsui D, Ogawa S, Unno K, Okubo M, Tokita A, Nakagawa T, Ito T, Ishimi Y, Nagasawa H, Matsumoto T, Yanagisawa J, Kato S | title = The chromatin-remodeling complex WINAC targets a nuclear receptor to promoters and is impaired in Williams syndrome | journal = Cell | volume = 113 | issue = 7 | pages = 905–17 | date = Jun 2003 | pmid = 12837248 | doi = 10.1016/S0092-8674(03)00436-7 }}</ref><ref name=pmid11937504>{{cite journal | vauthors = Wärnmark A, Treuter E, Gustafsson JA, Hubbard RE, Brzozowski AM, Pike AC | title = Interaction of transcriptional intermediary factor 2 nuclear receptor box peptides with the coactivator binding site of estrogen receptor alpha | journal = J. Biol. Chem. | volume = 277 | issue = 24 | pages = 21862–8 | date = Jun 2002 | pmid = 11937504 | doi = 10.1074/jbc.M200764200 }}</ref><ref name=pmid12612084>{{cite journal | vauthors = He B, Wilson EM | title = Electrostatic Modulation in Steroid Receptor Recruitment of LXXLL and FXXLF Motifs | journal = Mol. Cell. Biol. | volume = 23 | issue = 6 | pages = 2135–50 | date = Mar 2003 | pmid = 12612084 | pmc = 149467 | doi = 10.1128/MCB.23.6.2135-2150.2003 }}</ref><ref name=pmid18499756>{{cite journal | vauthors = Fenne IS, Hoang T, Hauglid M, Sagen JV, Lien EA, Mellgren G | title = 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 | journal = [[Endocrinology (journal)|Endocrinology]] | volume = 149 | issue = 9 | pages = 4336–45 | date = Sep 2008 | pmid = 18499756 | doi = 10.1210/en.2008-0037 }}</ref>
* [[Nuclear receptor coactivator 3|NCOA3]]<ref name=pmid11250900/><ref name=pmid11389589>{{cite journal | vauthors = Wong CW, Komm B, Cheskis BJ | title = Structure-function evaluation of ER alpha and beta interplay with SRC family coactivators. ER selective ligands | journal = Biochemistry | volume = 40 | issue = 23 | pages = 6756–65 | date = Jun 2001 | pmid = 11389589 | doi = 10.1021/bi010379h }}</ref><ref name=pmid11050174>{{cite journal | vauthors = Tikkanen MK, Carter DJ, Harris AM, Le HM, Azorsa DO, Meltzer PS, Murdoch FE | title = Endogenously expressed estrogen receptor and coactivator AIB1 interact in MCF-7 human breast cancer cells | journal = [[PNAS|Proc. Natl. Acad. Sci. U.S.A.]] | volume = 97 | issue = 23 | pages = 12536–40 | date = Nov 2000 | pmid = 11050174 | pmc = 18799 | doi = 10.1073/pnas.220427297 }}</ref>
* [[NRIP1]]<ref name=pmid7641693>{{cite journal | vauthors = Cavaillès V, Dauvois S, L'Horset F, Lopez G, Hoare S, Kushner PJ, Parker MG | title = Nuclear factor RIP140 modulates transcriptional activation by the estrogen receptor | journal = EMBO J. | volume = 14 | issue = 15 | pages = 3741–51 | date = Aug 1995 | pmid = 7641693 | pmc = 394449 }}</ref><ref name=pmid9115274>{{cite journal | vauthors = Thénot S, Henriquet C, Rochefort H, Cavaillès V | title = Differential interaction of nuclear receptors with the putative human transcriptional coactivator hTIF1 | journal = J. Biol. Chem. | volume = 272 | issue = 18 | pages = 12062–8 | date = May 1997 | pmid = 9115274 | doi = 10.1074/jbc.272.18.12062 }}</ref><ref name=pmid8887632>{{cite journal | vauthors = L'Horset F, Dauvois S, Heery DM, Cavaillès V, Parker MG | title = RIP-140 interacts with multiple nuclear receptors by means of two distinct sites | journal = Mol. Cell. Biol. | volume = 16 | issue = 11 | pages = 6029–36 | date = Nov 1996 | pmid = 8887632 | pmc = 231605 }}</ref>
* [[PDLIM1]]<ref name=pmid19117995>{{cite journal | vauthors = Johnsen SA, Güngör C, Prenzel T, Riethdorf S, Riethdorf L, Taniguchi-Ishigaki N, Rau T, Tursun B, Furlow JD, Sauter G, Scheffner M, Pantel K, Gannon F, Bach I | title = Regulation of Estrogen-Dependent Transcription by the LIM Cofactors CLIM and RLIM in Breast Cancer | journal = Cancer Res. | volume = 69 | issue = 1 | pages = 128–36 | date = Jan 2009 | pmid = 19117995 | pmc = 2713826 | doi = 10.1158/0008-5472.CAN-08-1630 | issn =  }}</ref>
* [[POU4F1]]<ref name=pmid9448000/>
* [[POU4F2]]<ref name=pmid9448000>{{cite journal | vauthors = Budhram-Mahadeo V, Parker M, Latchman DS | title = POU Transcription Factors Brn-3a and Brn-3b Interact with the Estrogen Receptor and Differentially Regulate Transcriptional Activity via an Estrogen Response Element | journal = Mol. Cell. Biol. | volume = 18 | issue = 2 | pages = 1029–41 | date = Feb 1998 | pmid = 9448000 | pmc = 108815 | doi=10.1128/mcb.18.2.1029}}</ref>
* [[PRDM2]]<ref name=pmid10706618>{{cite journal | vauthors = Abbondanza C, Medici N, Nigro V, Rossi V, Gallo L, Piluso G, Belsito A, Roscigno A, Bontempo P, Puca AA, Molinari AM, Moncharmont B, Puca GA | title = The retinoblastoma-interacting zinc-finger protein RIZ is a downstream effector of estrogen action | journal = [[PNAS|Proc. Natl. Acad. Sci. U.S.A.]] | volume = 97 | issue = 7 | pages = 3130–5 | date = Mar 2000 | pmid = 10706618 | pmc = 16204 | doi = 10.1073/pnas.050015697 }}</ref>
* [[PRMT2]]<ref name=pmid12039952>{{cite journal | vauthors = Qi C, Chang J, Zhu Y, Yeldandi AV, Rao SM, Zhu YJ | title = Identification of protein arginine methyltransferase 2 as a coactivator for estrogen receptor alpha | journal = J. Biol. Chem. | volume = 277 | issue = 32 | pages = 28624–30 | date = Aug 2002 | pmid = 12039952 | doi = 10.1074/jbc.M201053200 }}</ref>
* [[RBM39]]<ref name=pmid11704680>{{cite journal | vauthors = Jung DJ, Na SY, Na DS, Lee JW | title = Molecular cloning and characterization of CAPER, a novel coactivator of activating protein-1 and estrogen receptors | journal = J. Biol. Chem. | volume = 277 | issue = 2 | pages = 1229–34 | date = Jan 2002 | pmid = 11704680 | doi = 10.1074/jbc.M110417200 }}</ref>
* [[RNF12]]<ref name=pmid19117995/>
* [[SAFB]]<ref name=pmid15066997>{{cite journal | vauthors = Townson SM, Kang K, Lee AV, Oesterreich S | title = Structure-function analysis of the estrogen receptor alpha corepressor scaffold attachment factor-B1: identification of a potent transcriptional repression domain | journal = J. Biol. Chem. | volume = 279 | issue = 25 | pages = 26074–81 | date = Jun 2004 | pmid = 15066997 | doi = 10.1074/jbc.M313726200 }}</ref><ref name=pmid10707955>{{cite journal | vauthors = Oesterreich S, Zhang Q, Hopp T, Fuqua SA, Michaelis M, Zhao HH, Davie JR, Osborne CK, Lee AV | title = Tamoxifen-bound estrogen receptor (ER) strongly interacts with the nuclear matrix protein HET/SAF-B, a novel inhibitor of ER-mediated transactivation | journal = Mol. Endocrinol. | volume = 14 | issue = 3 | pages = 369–81 | date = Mar 2000 | pmid = 10707955 | doi = 10.1210/mend.14.3.0432 | authorlink =  }}</ref>
* [[SAFB2]]<ref name=pmid12660241>{{cite journal | vauthors = Townson SM, Dobrzycka KM, Lee AV, Air M, Deng W, Kang K, Jiang S, Kioka N, Michaelis K, Oesterreich S | title = SAFB2, a new scaffold attachment factor homolog and estrogen receptor corepressor | journal = J. Biol. Chem. | volume = 278 | issue = 22 | pages = 20059–68 | date = May 2003 | pmid = 12660241 | doi = 10.1074/jbc.M212988200 }}</ref>
* [[SHC1]]<ref name=pmid11773443>{{cite journal | vauthors = Song RX, McPherson RA, Adam L, Bao Y, Shupnik M, Kumar R, Santen RJ | title = Linkage of rapid estrogen action to MAPK activation by ERalpha-Shc association and Shc pathway activation | journal = Mol. Endocrinol. | volume = 16 | issue = 1 | pages = 116–27 | date = Jan 2002 | pmid = 11773443 | doi = 10.1210/me.16.1.116 }}</ref>
* [[Small heterodimer partner|SHP]]<ref name=pmid9773978>{{cite journal | vauthors = Seol W, Hanstein B, Brown M, Moore DD | title = Inhibition of estrogen receptor action by the orphan receptor SHP (short heterodimer partner) | journal = Mol. Endocrinol. | volume = 12 | issue = 10 | pages = 1551–7 | date = Oct 1998 | pmid = 9773978 | doi = 10.1210/me.12.10.1551 }}</ref><ref name=pmid11861507>{{cite journal | vauthors = Klinge CM, Jernigan SC, Risinger KE | title = The agonist activity of tamoxifen is inhibited by the short heterodimer partner orphan nuclear receptor in human endometrial cancer cells | journal = [[Endocrinology (journal)|Endocrinology]] | volume = 143 | issue = 3 | pages = 853–67 | date = Mar 2002 | pmid = 11861507 | doi = 10.1210/en.143.3.853 }}</ref>
* [[SMARCA4]]<ref name=pmid11003650/><ref name=pmid9099865>{{cite journal | vauthors = Ichinose H, Garnier JM, Chambon P, Losson R | title = Ligand-dependent interaction between the estrogen receptor and the human homologues of SWI2/SNF2 | journal = Gene | volume = 188 | issue = 1 | pages = 95–100 | date = Mar 1997 | pmid = 9099865 | doi = 10.1016/S0378-1119(96)00785-8 }}</ref>
* [[SMARCE1]]<ref name=pmid12145209>{{cite journal | vauthors = Belandia B, Orford RL, Hurst HC, Parker MG | title = Targeting of SWI/SNF chromatin remodelling complexes to estrogen-responsive genes | journal = EMBO J. | volume = 21 | issue = 15 | pages = 4094–103 | date = Aug 2002 | pmid = 12145209 | pmc = 126156 | doi = 10.1093/emboj/cdf412 }}</ref>
* [[SRA1]]<ref name=pmid11250900/>
* [[Src (gene)|Src]]<ref name=pmid11564893>{{cite journal | vauthors = Teo AK, Oh HK, Ali RB, Li BF | title = The Modified Human DNA Repair Enzyme O6-Methylguanine-DNA Methyltransferase Is a Negative Regulator of Estrogen Receptor-Mediated Transcription upon Alkylation DNA Damage | journal = Mol. Cell. Biol. | volume = 21 | issue = 20 | pages = 7105–14 | date = Oct 2001 | pmid = 11564893 | pmc = 99886 | doi = 10.1128/MCB.21.20.7105-7114.2001 }}</ref><ref name=pmid11032808>{{cite journal | vauthors = Migliaccio A, Castoria G, Di Domenico M, de Falco A, Bilancio A, Lombardi M, Barone MV, Ametrano D, Zannini MS, Abbondanza C, Auricchio F | title = Steroid-induced androgen receptor–oestradiol receptor β–Src complex triggers prostate cancer cell proliferation | journal = EMBO J. | volume = 19 | issue = 20 | pages = 5406–17 | date = Oct 2000 | pmid = 11032808 | pmc = 314017 | doi = 10.1093/emboj/19.20.5406 }}</ref><ref name=pmid10454579>{{cite journal | vauthors = Kim HJ, Yi JY, Sung HS, Moore DD, Jhun BH, Lee YC, Lee JW | title = Activating Signal Cointegrator 1, a Novel Transcription Coactivator of Nuclear Receptors, and Its Cytosolic Localization under Conditions of Serum Deprivation | journal = Mol. Cell. Biol. | volume = 19 | issue = 9 | pages = 6323–32 | date = Sep 1999 | pmid = 10454579 | pmc = 84603 | doi=10.1128/mcb.19.9.6323}}</ref><ref name=pmid11013076>{{cite journal | vauthors = Slentz-Kesler K, Moore JT, Lombard M, Zhang J, Hollingsworth R, Weiner MP | title = Identification of the human Mnk2 gene (MKNK2) through protein interaction with estrogen receptor beta | journal = Genomics | volume = 69 | issue = 1 | pages = 63–71 | date = Oct 2000 | pmid = 11013076 | doi = 10.1006/geno.2000.6299 }}</ref>
* [[Testicular receptor 2|TR2]]<ref name=pmid12093804>{{cite journal | vauthors = Hu YC, Shyr CR, Che W, Mu XM, Kim E, Chang C | title = Suppression of estrogen receptor-mediated transcription and cell growth by interaction with TR2 orphan receptor | journal = J. Biol. Chem. | volume = 277 | issue = 37 | pages = 33571–9 | date = Sep 2002 | pmid = 12093804 | doi = 10.1074/jbc.M203531200 }}</ref>
* [[Testicular receptor 4|TR4]]<ref name=pmid11844790>{{cite journal | vauthors = Shyr CR, Hu YC, Kim E, Chang C | title = Modulation of estrogen receptor-mediated transactivation by orphan receptor TR4 in MCF-7 cells | journal = J. Biol. Chem. | volume = 277 | issue = 17 | pages = 14622–8 | date = Apr 2002 | pmid = 11844790 | doi = 10.1074/jbc.M110051200 }}</ref>
* [[Thymine-DNA glycosylase|TDG]]<ref name=pmid12874288>{{cite journal | vauthors = Chen D, Lucey MJ, Phoenix F, Lopez-Garcia J, Hart SM, Losson R, Buluwela L, Coombes RC, Chambon P, Schär P, Ali S | title = T:G mismatch-specific thymine-DNA glycosylase potentiates transcription of estrogen-regulated genes through direct interaction with estrogen receptor alpha | journal = J. Biol. Chem. | volume = 278 | issue = 40 | pages = 38586–92 | date = Oct 2003 | pmid = 12874288 | doi = 10.1074/jbc.M304286200 }}</ref>
* [[TRIM24]]<ref name=pmid9115274/><ref name=pmid10598587>{{cite journal | vauthors = Thénot S, Bonnet S, Boulahtouf A, Margeat E, Royer CA, Borgna JL, Cavaillès V | title = Effect of ligand and DNA binding on the interaction between human transcription intermediary factor 1alpha and estrogen receptors | journal = Mol. Endocrinol. | volume = 13 | issue = 12 | pages = 2137–50 | date = Dec 1999 | pmid = 10598587 | doi = 10.1210/me.13.12.2137 }}</ref> and
* [[XBP1]].<ref name=pmid12954762>{{cite journal | vauthors = Ding L, Yan J, Zhu J, Zhong H, Lu Q, Wang Z, Huang C, Ye Q | title = Ligand-independent activation of estrogen receptor α by XBP-1 | journal = Nucleic Acids Res. | volume = 31 | issue = 18 | pages = 5266–74 | date = Sep 2003 | pmid = 12954762 | pmc = 203316 | doi = 10.1093/nar/gkg731 | issn = }}</ref>
{{Div col end}}
{{Clear}}


==References==
==References==
{{reflist|2}}
{{Reflist|2}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
* {{cite journal | vauthors = McDonnell DP, Norris JD | title = Connections and regulation of the human estrogen receptor | journal = Science | volume = 296 | issue = 5573 | pages = 1642–4 | year = 2002 | pmid = 12040178 | doi = 10.1126/science.1071884 }}
| citations =
* {{cite journal | vauthors = Simoncini T, Fornari L, Mannella P, Varone G, Caruso A, Liao JK, Genazzani AR | title = Novel non-transcriptional mechanisms for estrogen receptor signaling in the cardiovascular system. Interaction of estrogen receptor alpha with phosphatidylinositol 3-OH kinase | journal = Steroids | volume = 67 | issue = 12 | pages = 935–9 | year = 2003 | pmid = 12398989 | doi = 10.1016/S0039-128X(02)00040-5 }}
*{{cite journal | author=McDonnell DP, Norris JD |title=Connections and regulation of the human estrogen receptor. |journal=Science |volume=296 |issue= 5573 |pages= 1642-4 |year= 2002 |pmid= 12040178 |doi= 10.1126/science.1071884 }}
* {{cite journal | vauthors = Lannigan DA | title = Estrogen receptor phosphorylation | journal = Steroids | volume = 68 | issue = 1 | pages = 1–9 | year = 2003 | pmid = 12475718 | doi = 10.1016/S0039-128X(02)00110-1 }}
*{{cite journal | author=Simoncini T, Fornari L, Mannella P, ''et al.'' |title=Novel non-transcriptional mechanisms for estrogen receptor signaling in the cardiovascular system. Interaction of estrogen receptor alpha with phosphatidylinositol 3-OH kinase. |journal=Steroids |volume=67 |issue= 12 |pages= 935-9 |year= 2003 |pmid= 12398989 |doi= }}
* {{cite journal | vauthors = Herrington DM | title = Role of estrogen receptor-alpha in pharmacogenetics of estrogen action | journal = Curr. Opin. Lipidol. | volume = 14 | issue = 2 | pages = 145–50 | year = 2003 | pmid = 12642782 | doi = 10.1097/00041433-200304000-00005 }}
*{{cite journal | author=Lannigan DA |title=Estrogen receptor phosphorylation. |journal=Steroids |volume=68 |issue= 1 |pages= 1-9 |year= 2003 |pmid= 12475718 |doi= }}
* {{cite journal | vauthors = Tanaka Y, Sasaki M, Kaneuchi M, Fujimoto S, Dahiya R | title = Estrogen receptor alpha polymorphisms and renal cell carcinoma--a possible risk | journal = Mol. Cell. Endocrinol. | volume = 202 | issue = 1–2 | pages = 109–16 | year = 2004 | pmid = 12770739 | doi = 10.1016/S0303-7207(03)00071-6 }}
*{{cite journal | author=Herrington DM |title=Role of estrogen receptor-alpha in pharmacogenetics of estrogen action. |journal=Curr. Opin. Lipidol. |volume=14 |issue= 2 |pages= 145-50 |year= 2003 |pmid= 12642782 |doi= 10.1097/01.mol.0000064045.68936.23 }}
* {{cite journal | vauthors = Ali S, Coombes RC | title = Estrogen receptor alpha in human breast cancer: occurrence and significance | journal = Journal of Mammary Gland Biology and Neoplasia | volume = 5 | issue = 3 | pages = 271–81 | year = 2004 | pmid = 14973389 | doi = 10.1023/A:1009594727358 }}
*{{cite journal | author=Tanaka Y, Sasaki M, Kaneuchi M, ''et al.'' |title=Estrogen receptor alpha polymorphisms and renal cell carcinoma--a possible risk. |journal=Mol. Cell. Endocrinol. |volume=202 |issue= 1-2 |pages= 109-16 |year= 2004 |pmid= 12770739 |doi= }}
* {{cite journal | vauthors = Olsson H | title = Estrogen receptor content in malignant breast tumors in men--a review | journal = Journal of Mammary Gland Biology and Neoplasia | volume = 5 | issue = 3 | pages = 283–7 | year = 2004 | pmid = 14973390 | doi = 10.1023/A:1009546811429 }}
*{{cite journal | author=Ali S, Coombes RC |title=Estrogen receptor alpha in human breast cancer: occurrence and significance. |journal=Journal of mammary gland biology and neoplasia |volume=5 |issue= 3 |pages= 271-81 |year= 2004 |pmid= 14973389 |doi= }}
* {{cite journal | vauthors = Surmacz E, Bartucci M | title = Role of estrogen receptor alpha in modulating IGF-I receptor signaling and function in breast cancer | journal = J. Exp. Clin. Cancer Res. | volume = 23 | issue = 3 | pages = 385–94 | year = 2005 | pmid = 15595626 | doi =  }}
*{{cite journal | author=Olsson H |title=Estrogen receptor content in malignant breast tumors in men--a review. |journal=Journal of mammary gland biology and neoplasia |volume=5 |issue= 3 |pages= 283-7 |year= 2004 |pmid= 14973390 |doi= }}
* {{cite journal | vauthors = Evinger AJ, Levin ER | title = Requirements for estrogen receptor alpha membrane localization and function | journal = Steroids | volume = 70 | issue = 5–7 | pages = 361–3 | year = 2005 | pmid = 15862818 | doi = 10.1016/j.steroids.2005.02.015 }}
*{{cite journal | author=Surmacz E, Bartucci M |title=Role of estrogen receptor alpha in modulating IGF-I receptor signaling and function in breast cancer. |journal=J. Exp. Clin. Cancer Res. |volume=23 |issue= 3 |pages= 385-94 |year= 2005 |pmid= 15595626 |doi=  }}
* {{cite journal | vauthors = Wang CL, Tang XY, Chen WQ, Su YX, Zhang CX, Chen YM | title = Association of estrogen receptor alpha gene polymorphisms with bone mineral density in Chinese women: a meta-analysis | journal = Osteoporosis international : a journal established as result of cooperation between the European Foundation for Osteoporosis and the National Osteoporosis Foundation of the USA | volume = 18 | issue = 3 | pages = 295–305 | year = 2007 | pmid = 17089081 | doi = 10.1007/s00198-006-0239-2 }}
*{{cite journal | author=Evinger AJ, Levin ER |title=Requirements for estrogen receptor alpha membrane localization and function. |journal=Steroids |volume=70 |issue= 5-7 |pages= 361-3 |year= 2005 |pmid= 15862818 |doi= 10.1016/j.steroids.2005.02.015 }}
* {{cite journal | vauthors = Keaveney M, Klug J, Gannon F | title = Sequence analysis of the 5' flanking region of the human estrogen receptor gene | journal = DNA Seq. | volume = 2 | issue = 6 | pages = 347–58 | year = 1992 | pmid = 1476547 | doi = 10.3109/10425179209020816 }}
*{{cite journal | author=Wang CL, Tang XY, Chen WQ, ''et al.'' |title=Association of estrogen receptor alpha gene polymorphisms with bone mineral density in Chinese women: a meta-analysis. |journal=Osteoporosis international : a journal established as result of cooperation between the European Foundation for Osteoporosis and the National Osteoporosis Foundation of the USA |volume=18 |issue= 3 |pages= 295-305 |year= 2007 |pmid= 17089081 |doi= 10.1007/s00198-006-0239-2 }}
* {{cite journal | vauthors = Piva R, Gambari R, Zorzato F, Kumar L, del Senno L | title = Analysis of upstream sequences of the human estrogen receptor gene | journal = Biochem. Biophys. Res. Commun. | volume = 183 | issue = 3 | pages = 996–1002 | year = 1992 | pmid = 1567414 | doi = 10.1016/S0006-291X(05)80289-X }}
*{{cite journal | author=Keaveney M, Klug J, Gannon F |title=Sequence analysis of the 5' flanking region of the human estrogen receptor gene. |journal=DNA Seq. |volume=2 |issue= 6 |pages= 347-58 |year= 1992 |pmid= 1476547 |doi= }}
* {{cite journal | vauthors = Reese JC, Katzenellenbogen BS | title = 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 | journal = J. Biol. Chem. | volume = 267 | issue = 14 | pages = 9868–73 | year = 1992 | pmid = 1577818 | doi =  }}
*{{cite journal | author=Piva R, Gambari R, Zorzato F, ''et al.'' |title=Analysis of upstream sequences of the human estrogen receptor gene. |journal=Biochem. Biophys. Res. Commun. |volume=183 |issue= 3 |pages= 996-1002 |year= 1992 |pmid= 1567414 |doi= }}
* {{cite journal | vauthors = Dotzlaw H, Alkhalaf M, Murphy LC | title = Characterization of estrogen receptor variant mRNAs from human breast cancers | journal = Mol. Endocrinol. | volume = 6 | issue = 5 | pages = 773–85 | year = 1992 | pmid = 1603086 | doi = 10.1210/me.6.5.773 }}
*{{cite journal | author=Reese JC, Katzenellenbogen BS |title=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. |journal=J. Biol. Chem. |volume=267 |issue= 14 |pages= 9868-73 |year= 1992 |pmid= 1577818 |doi=  }}
* {{cite journal | vauthors = Keaveney M, Klug J, Dawson MT, Nestor PV, Neilan JG, Forde RC, Gannon F | title = Evidence for a previously unidentified upstream exon in the human oestrogen receptor gene | journal = J. Mol. Endocrinol. | volume = 6 | issue = 1 | pages = 111–5 | year = 1991 | pmid = 2015052 | doi = 10.1677/jme.0.0060111 }}
*{{cite journal | author=Dotzlaw H, Alkhalaf M, Murphy LC |title=Characterization of estrogen receptor variant mRNAs from human breast cancers. |journal=Mol. Endocrinol. |volume=6 |issue= 5 |pages= 773-85 |year= 1992 |pmid= 1603086 |doi= }}
* {{cite journal | vauthors = Reese JC, Katzenellenbogen BS | title = 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 | journal = J. Biol. Chem. | volume = 266 | issue = 17 | pages = 10880–7 | year = 1991 | pmid = 2040605 | doi =  }}
*{{cite journal | author=Keaveney M, Klug J, Dawson MT, ''et al.'' |title=Evidence for a previously unidentified upstream exon in the human oestrogen receptor gene. |journal=J. Mol. Endocrinol. |volume=6 |issue= 1 |pages= 111-5 |year= 1991 |pmid= 2015052 |doi= }}
* {{cite journal | vauthors = Schwabe JW, Neuhaus D, Rhodes D | title = Solution structure of the DNA-binding domain of the oestrogen receptor | journal = Nature | volume = 348 | issue = 6300 | pages = 458–61 | year = 1991 | pmid = 2247153 | doi = 10.1038/348458a0 }}
*{{cite journal | author=Reese JC, Katzenellenbogen BS |title=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. |journal=J. Biol. Chem. |volume=266 |issue= 17 |pages= 10880-7 |year= 1991 |pmid= 2040605 |doi=  }}
* {{cite journal | vauthors = Tora L, Mullick A, Metzger D, Ponglikitmongkol M, Park I, Chambon P | title = The cloned human oestrogen receptor contains a mutation which alters its hormone binding properties | journal = EMBO J. | volume = 8 | issue = 7 | pages = 1981–6 | year = 1989 | pmid = 2792078 | pmc = 401066 | doi =  }}
*{{cite journal | author=Schwabe JW, Neuhaus D, Rhodes D |title=Solution structure of the DNA-binding domain of the oestrogen receptor. |journal=Nature |volume=348 |issue= 6300 |pages= 458-61 |year= 1991 |pmid= 2247153 |doi= 10.1038/348458a0 }}
* {{cite journal | vauthors = Ponglikitmongkol M, Green S, Chambon P | title = Genomic organization of the human oestrogen receptor gene | journal = EMBO J. | volume = 7 | issue = 11 | pages = 3385–8 | year = 1989 | pmid = 3145193 | pmc = 454836 | doi =  }}
*{{cite journal | author=Tora L, Mullick A, Metzger D, ''et al.'' |title=The cloned human oestrogen receptor contains a mutation which alters its hormone binding properties. |journal=EMBO J. |volume=8 |issue= 7 |pages= 1981-6 |year= 1989 |pmid= 2792078 |doi=  }}
* {{cite journal | vauthors = Greene GL, Gilna P, Waterfield M, Baker A, Hort Y, Shine J | title = Sequence and expression of human estrogen receptor complementary DNA | journal = Science | volume = 231 | issue = 4742 | pages = 1150–4 | year = 1986 | pmid = 3753802 | doi = 10.1126/science.3753802 }}
*{{cite journal | author=Ponglikitmongkol M, Green S, Chambon P |title=Genomic organization of the human oestrogen receptor gene. |journal=EMBO J. |volume=7 |issue= 11 |pages= 3385-8 |year= 1989 |pmid= 3145193 |doi=  }}
*{{cite journal | author=Greene GL, Gilna P, Waterfield M, ''et al.'' |title=Sequence and expression of human estrogen receptor complementary DNA. |journal=Science |volume=231 |issue= 4742 |pages= 1150-4 |year= 1986 |pmid= 3753802 |doi= }}
}}
{{refend}}
{{refend}}


==External links==
* {{FactorBook|ERalpha_a}}
{{NLM content}}
{{NLM content}}
{{protein-stub}}
 
{{Transcription factors}}
{{PDB Gallery|geneid=2099}}
{{Transcription factors|g2}}
{{Estrogen receptor modulators}}
 
[[Category:Intracellular receptors]]
[[Category:Intracellular receptors]]
[[Category:Transcription factors]]
[[Category:Transcription factors]]

Latest revision as of 11:23, 5 March 2018

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External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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RefSeq (mRNA)

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View/Edit Human

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

Non-selective

Selective

Agonists of ERα selective over ERβ include:

Mixed

Antagonists

Non-selective

Selective

Antagonists of ERα selective over ERβ include:

Tissue distribution and function

ERα plays a role in the physiological development and function of a variety of organ systems to varying degrees, including the reproductive, central nervous, skeletal, and cardiovascular systems.[7] Accordingly, ERα is widely expressed throughout the body, including the uterus and ovary, male reproductive organs, mammary gland, bone, heart, hypothalamus, pituitary gland, liver, lung, kidney, spleen, and adipose tissue.[7][8][9] The development and function of these tissues is disrupted in animal models lacking active ERα genes, such as the ERα knockout mouse (ERKO), providing a preliminary understanding of ERα function at specific target organs.[7][10]

Uterus and ovary

ERα is essential in the maturation of the female reproductive phenotype. In the absence of ERα, the ERKO mouse develops an adult uterus, indicating that ERα may not mediate the initial growth of the uterus.[7][8] However, ERα plays a role in the completion of this development, and the subsequent function of the tissue.[10] Activation of ERα is known to trigger cell proliferation in the uterus.[9] The uterus of female ERKO mice is hypoplastic, suggesting that ERα mediates mitosis and differentiation in the uterus in response to estrogen stimulation.[8]

Similarly, prepubertal female ERKO mice develop ovaries that are nearly indistinguishable from those of their wildtype counterparts. However, as the ERKO mice mature they progressively present an abnormal ovarian phenotype in both physiology and function.[8][10] Specifically, female ERKO mice develop enlarged ovaries containing hemorrhagic follicular cysts, which also lack the corpus luteum, and therefore do not ovulate.[7][8][10] This adult ovarian phenotype suggests that in the absence of ERα, estrogen is no longer able to perform negative feedback on the hypothalamus, resulting in chronically elevated LH levels and constant ovarian stimulation.[8] These results identify a pivotal role for ERα in the hypothalamus, in addition to its role in the estrogen-driven maturation through theca and interstitial cells of the ovary.[8]

Male reproductive organs

ERα is similarly essential in the maturation and maintenance of the male reproductive phenotype, as male ERKO mice are infertile and present undersized testes.[7][10] The integrity of testicular structures of ERKO mice, such as the seminiferous tubules of the testes and the seminiferous epithelium, declines over time.[7][8] Furthermore, the reproductive performance of male ERKO mice is hindered abnormalities in sexual physiology and behavior, such as impaired spermatogenesis and loss of intromission and ejaculatory responses.[7][8]

Mammary gland

Estrogen stimulation of ERα is known to stimulate cell proliferation in breast tissue.[9] ERα may be responsible for pubertal development of the adult phenotype, through mediation of mammary gland response to ovarian hormones.[10] This role is consistent with the abnormalities of female ERKO mice: the epithelial ducts of female ERKO mice fail to grow beyond their pre-pubertal length, and lactational structures do not develop.[8] As a result, the functions of the mammary gland -- including both lactation and release of prolactin -- are greatly impaired in ERKO mice.[10]

Bone

Though its expression in bone is moderate, ERα is known to be responsible for maintenance of bone integrity.[9][10] It is hypothesized that estrogen stimulation of ERα may trigger the release of growth factors, such as epidermal growth factor or insulin-like growth factor-1, which in turn regulate bone development and maintenance.[10][8] Accordingly, male and female ERKO mice exhibit decreased bone length and size.[10][8]

Brain

Estrogen signaling through ERα appears to be responsible for various aspects of central nervous development, such as synaptogenesis and synaptic remodeling.[10] In the brain, ERα is found in hypothalamus, and preoptic area, and arcuate nucleus, all three of which have been linked to reproductive behavior, and the masculinization of the mouse brain appears to take place through ERα function.[7][10] Furthermore, studies in models of psychopathology and neurodegenerative disease states suggest that estrogen receptors mediate the neuroprotective role of estrogen in the brain.[7][9] Finally, ERα appears to mediate positive feedback effects of estrogen on the brain's secretion of GnRH and LH, by way increasing expression of kisspeptin in neurons of the arcuate nucleus and anteroventral periventricular nucleus.[11][12] Although classical studies have suggested that negative feedback effects of estrogen also operate through ERα, female mice lacking ERα in kisspeptin-expressing neurons continue to demonstrate a degree of negative feedback response.[13]

Clinical significance

Estrogen insensitivity syndrome is a very rare condition characterized by a defective ERα that is insensitive to estrogens.[14][15][16][17] 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.[17] The clinical presentation in a male was reported to include lack of epiphyseal closure, tall stature, osteoporosis, and poor sperm viability.[16] Both individuals were completely insensitive to exogenous estrogen treatment, even with high doses.[16][17]

Genetic polymorphisms in the gene encoding the ERα have been associated with breast cancer in women and gynecomastia in men.[18][19]

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. ↑ 7.0 7.1 7.2 7.3 7.4 7.5 7.6 7.7 7.8 7.9 Bondesson M, Hao R, Lin CY, Williams C, Gustafsson JÅ (February 2015). "Estrogen receptor signaling during vertebrate development". Biochimica et Biophysica Acta. 1849 (2): 142–51. doi:10.1016/j.bbagrm.2014.06.005. PMC 4269570. PMID 24954179.
  8. ↑ 8.00 8.01 8.02 8.03 8.04 8.05 8.06 8.07 8.08 8.09 8.10 8.11 Curtis Hewitt S, Couse JF, Korach KS (2000). "Estrogen receptor transcription and transactivation: Estrogen receptor knockout mice: what their phenotypes reveal about mechanisms of estrogen action". Breast Cancer Research. 2 (5): 345–52. doi:10.1186/bcr79. PMC 138656. PMID 11250727.
  9. ↑ 9.0 9.1 9.2 9.3 9.4 Paterni I, Granchi C, Katzenellenbogen JA, Minutolo F (November 2014). "Estrogen receptors alpha (ERα) and beta (ERβ): subtype-selective ligands and clinical potential". Steroids. 90: 13–29. doi:10.1016/j.steroids.2014.06.012. PMC 4192010. PMID 24971815.
  10. ↑ 10.00 10.01 10.02 10.03 10.04 10.05 10.06 10.07 10.08 10.09 10.10 10.11 Lee HR, Kim TH, Choi KC (June 2012). "Functions and physiological roles of two types of estrogen receptors, ERα and ERβ, identified by estrogen receptor knockout mouse". Laboratory Animal Research. 28 (2): 71–6. doi:10.5625/lar.2012.28.2.71. PMC 3389841. PMID 22787479.
  11. ↑ Clarkson J (April 2013). "Effects of estradiol on kisspeptin neurons during puberty". Frontiers in Neuroendocrinology. 34 (2): 120–31. doi:10.1016/j.yfrne.2013.02.002. PMID 23500175.
  12. ↑ Moenter SM, Chu Z, Christian CA (March 2009). "Neurobiological mechanisms underlying oestradiol negative and positive feedback regulation of gonadotrophin-releasing hormone neurones". Journal of Neuroendocrinology. 21 (4): 327–33. doi:10.1111/j.1365-2826.2009.01826.x. PMC 2738426. PMID 19207821.
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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, 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.

External links

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