View source for Androgen receptor

{{Short description|Mammalian protein found in humans}}
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{{Infobox gene}}
{{Infobox protein family
| Symbol = Androgen_recep
| Name = Androgen_recep
| image = PDB 1xow EBI.jpg
| width =
| caption = crystal structure of the human androgen receptor ligand binding domain bound with an androgen receptor nh2-terminal peptide, ar20-30, and r1881
| Pfam = PF02166
| Pfam_clan = 
| InterPro = IPR001103
| SMART =
| PROSITE =
| MEROPS =
| SCOP =
| TCDB =
| OPM family =
| OPM protein =
| CAZy =
| CDD =
}}
[[File:Human androgen receptor and androgen binding.svg|thumb|294 px|Normal function of the androgen receptor. Testosterone (T) enters the cell and, if 5-alpha-reductase is present, is converted into dihydrotestosterone (DHT). Upon steroid binding, the androgen receptor (AR) undergoes a conformational change and releases heat-shock proteins (hsps). Phosphorylation (P) occurs before or after steroid binding. The AR translocates to the nucleus where dimerization, DNA binding, and the recruitment of coactivators occur. Target genes are transcribed (mRNA) and translated into proteins.<ref name="pmid7671849">{{cite journal | vauthors = Quigley CA, De Bellis A, Marschke KB, el-Awady MK, Wilson EM, French FS | title = Androgen receptor defects: historical, clinical, and molecular perspectives | journal = Endocrine Reviews | volume = 16 | issue = 3 | pages = 271–321 | date = June 1995 | pmid = 7671849 | doi = 10.1210/edrv-16-3-271 }}</ref><ref name="pmid15705293">{{cite journal | vauthors = Gottlieb B, Lombroso R, Beitel LK, Trifiro MA | title = Molecular pathology of the androgen receptor in male (in)fertility | journal = Reproductive Biomedicine Online | volume = 10 | issue = 1 | pages = 42–8 | date = January 2005 | pmid = 15705293 | doi = 10.1016/S1472-6483(10)60802-4 }}</ref><ref name="pmid9845666">{{cite journal | vauthors = Choong CS, Wilson EM | title = Trinucleotide repeats in the human androgen receptor: a molecular basis for disease | journal = Journal of Molecular Endocrinology | volume = 21 | issue = 3 | pages = 235–57 | date = December 1998 | pmid = 9845666 | doi = 10.1677/jme.0.0210235 | doi-access = free }}</ref><ref name="pmid12700055">{{cite journal | vauthors = Meehan KL, Sadar MD | title = Androgens and androgen receptor in prostate and ovarian malignancies | journal = Frontiers in Bioscience | volume = 8 | issue = 1–3 | pages = d780–800 | date = May 2003 | pmid = 12700055 | doi = 10.2741/1063 | doi-access = free }}</ref>]]

The '''androgen receptor''' ('''AR'''), also known as '''NR3C4''' (nuclear receptor subfamily 3, group C, member 4), is a type of [[nuclear receptor]]<ref name="pmid17132855">{{cite journal | vauthors = Lu NZ, Wardell SE, Burnstein KL, Defranco D, Fuller PJ, Giguere V, Hochberg RB, McKay L, Renoir JM, Weigel NL, Wilson EM, McDonnell DP, Cidlowski JA | title = International Union of Pharmacology. LXV. The pharmacology and classification of the nuclear receptor superfamily: glucocorticoid, mineralocorticoid, progesterone, and androgen receptors | journal = Pharmacological Reviews | volume = 58 | issue = 4 | pages = 782–97 | date = December 2006 | pmid = 17132855 | doi = 10.1124/pr.58.4.9 | s2cid = 28626145 }}</ref> that is activated by binding any of the [[androgen]]ic [[hormones]], including [[testosterone]] and [[dihydrotestosterone]],<ref name="pmid9949684">{{cite book | vauthors = Roy AK, Lavrovsky Y, Song CS, Chen S, Jung MH, Velu NK, Bi BY, Chatterjee B | title = Regulation of androgen action | volume = 55 | pages = 309–52 | year = 1999 | pmid = 9949684 | doi = 10.1016/S0083-6729(08)60938-3 | isbn = 978-0-12-709855-5 | series = Vitamins & Hormones | publisher = Elsevier }}</ref> in the [[cytoplasm]] and then translocating into the [[Cell nucleus|nucleus]]. The androgen receptor is most closely related to the [[progesterone receptor]], and [[progestin]]s in higher dosages can block the androgen receptor.<ref name="pmid6371845">{{cite journal | vauthors = Bardin CW, Brown T, Isomaa VV, Jänne OA | title = Progestins can mimic, inhibit and potentiate the actions of androgens | journal = Pharmacology & Therapeutics | volume = 23 | issue = 3 | pages = 443–59 | year = 1983 | pmid = 6371845 | doi = 10.1016/0163-7258(83)90023-2 }}</ref><ref name="pmid12600226">{{cite journal | vauthors = Raudrant D, Rabe T | title = Progestogens with antiandrogenic properties | journal = Drugs | volume = 63 | issue = 5 | pages = 463–92 | year = 2003 | pmid = 12600226 | doi = 10.2165/00003495-200363050-00003 | s2cid = 28436828 }}</ref>

The main function of the androgen receptor is as a [[DNA-binding protein|DNA-binding]] [[transcription factor]] that [[Gene expression regulation|regulates gene expression]];<ref name="pmid3549275">{{cite journal | vauthors = Mooradian AD, Morley JE, Korenman SG | title = Biological actions of androgens | journal = Endocrine Reviews | volume = 8 | issue = 1 | pages = 1–28 | date = February 1987 | pmid = 3549275 | doi = 10.1210/edrv-8-1-1 }}</ref> however, the androgen receptor has other functions as well.<ref name="pmid12351684">{{cite journal | vauthors = Heinlein CA, Chang C | title = The roles of androgen receptors and androgen-binding proteins in nongenomic androgen actions | journal = Molecular Endocrinology | volume = 16 | issue = 10 | pages = 2181–7 | date = October 2002 | pmid = 12351684 | doi = 10.1210/me.2002-0070 | doi-access = free }}</ref> Androgen-regulated genes are critical for the development and maintenance of the male sexual [[phenotype]].

== Function ==

=== Effect on development ===
In some cell types, testosterone interacts directly with androgen receptors, whereas, in others, testosterone is converted by [[5-alpha reductase|5-alpha-reductase]] to dihydrotestosterone, an even more potent [[agonist]] for androgen receptor activation.<ref name="pmid16633980">{{cite journal | vauthors = Davison SL, Bell R | title = Androgen physiology | journal = Seminars in Reproductive Medicine | volume = 24 | issue = 2 | pages = 71–7 | date = April 2006 | pmid = 16633980 | doi = 10.1055/s-2006-939565 | s2cid = 260321076 }}</ref> Testosterone appears to be the primary androgen receptor-activating hormone in the [[Wolffian duct]], whereas dihydrotestosterone is the main androgenic hormone in the [[urogenital sinus]], [[urogenital tubercle]], and [[hair follicle]]s.<ref name="pmid12834017">{{cite journal | vauthors = Sinisi AA, Pasquali D, Notaro A, Bellastella A | title = Sexual differentiation | journal = [[Journal of Endocrinological Investigation]] | volume = 26 | issue = 3 Suppl | pages = 23–28 | year = 2003 | pmid = 12834017 }}</ref> Testosterone is therefore responsible primarily for the development of male [[sex organ|primary sexual characteristics]], whilst dihydrotestosterone is responsible for [[secondary sex characteristic|secondary male characteristics]].

Androgens cause slow maturation of the bones, but more of the potent maturation effect comes from the [[estrogen]] produced by [[aromatization]] of androgens. [[Steroid]] users of teen age may find that their growth had been stunted by androgen and/or estrogen excess. People with too little sex hormones can be short during puberty but end up taller as adults as in [[androgen insensitivity syndrome]] or [[estrogen insensitivity syndrome]].<ref name="pmid12868122">{{cite journal | vauthors = Frank GR | title = Role of estrogen and androgen in pubertal skeletal physiology | journal = Medical and Pediatric Oncology | volume = 41 | issue = 3 | pages = 217–21 | date = September 2003 | pmid = 12868122 | doi = 10.1002/mpo.10340 }}</ref>

[[Knockout-mice]] studies have shown that the androgen receptor is essential for normal female fertility, being required for development and full functionality of the [[ovarian follicle]]s and [[ovulation]], working through both intra-ovarian and [[neuroendocrine]] mechanisms.<ref name = "Walters_2010">{{cite journal | vauthors = Walters KA, Simanainen U, Handelsman DJ | title = Molecular insights into androgen actions in male and female reproductive function from androgen receptor knockout models | journal = Human Reproduction Update | volume = 16 | issue = 5 | pages = 543–58 | date = March 2010 | pmid = 20231167 | doi = 10.1093/humupd/dmq003 | doi-access = free }}</ref>

=== Maintenance of male skeletal integrity ===
Via the androgen receptor, androgens play a key role in the maintenance of male skeletal integrity. The regulation of this integrity by androgen receptor (AR) signaling can be attributed to both [[osteoblast]]s and [[osteocyte]]s.<ref>{{cite journal | vauthors = Sinnesael M, Claessens F, Laurent M, Dubois V, Boonen S, Deboel L, Vanderschueren D | title = Androgen receptor (AR) in osteocytes is important for the maintenance of male skeletal integrity: evidence from targeted AR disruption in mouse osteocytes | journal = Journal of Bone and Mineral Research | volume = 27 | issue = 12 | pages = 2535–43 | date = December 2012 | pmid = 22836391 | doi = 10.1002/jbmr.1713 | doi-access = free }}</ref>

=== Role in females ===

The AR plays a role in regulating female sexual, somatic, and behavioral functions. Experimental data using AR [[Knockout mouse|knockout]] female mice, provides evidence that the promotion of cardiac growth, kidney hypertrophy, cortical bone growth and regulation of [[trabecular]] bone structure is a result of DNA-binding-dependent actions of the AR in females.

Moreover, the importance of understanding female androgen receptors lies in their role in several genetic disorders including androgen insensitivity syndrome (AIS). [[Complete androgen insensitivity syndrome|Complete]] (CAIS) and [[Partial androgen insensitivity syndrome|partial]] (PAIS) which are a result of [[mutation]]s in the genes that code for AR. These mutations cause the inactivation of AR due to mutations conferring resistance to circulating testosterone, with more than 400 different AR mutations reported.{{Citation needed|date=December 2019|reason=removed citation to predatory publisher content}}

=== Mechanism of action ===

==== Genomic ====
The primary mechanism of action for androgen receptors is [[Transcription factor|direct regulation]] of [[gene transcription]].

Androgens (also called androgenic hormones), such as testosterone or dihydrotestosterone, are understood to exert their primary effects through binding to an androgen receptor in the cytosol. The receptor is translocated to the nucleus upon androgen binding and ultimately results in the transcriptional regulation of a number of genes via androgen responsive elements.<ref name="pmid12089231">{{cite journal | vauthors = Gelmann EP | title = Molecular biology of the androgen receptor | journal = Journal of Clinical Oncology | volume = 20 | issue = 13 | pages = 3001–3015 | date = July 2002 | pmid = 12089231 | doi = 10.1200/JCO.2002.10.018 }}</ref> This androgen response mechanism is perhaps best known and characterized in the context of male sexual differentiation and puberty, but plays a role in a variety of tissue types and processes.<ref>{{cite journal | vauthors = Li J, Al-Azzawi F | title = Mechanism of androgen receptor action | journal = Maturitas | volume = 63 | issue = 2 | pages = 142–148 | date = June 2009 | pmid = 19372015 | doi = 10.1016/j.maturitas.2009.03.008 }}</ref><ref name=wj>{{cite journal|doi=10.15347/WJM/2023.003  |doi-access=free |title=Alternative androgen pathways |year=2023 | vauthors = Masiutin M, Yadav M |journal=WikiJournal of Medicine |volume=10 |pages=X |s2cid=257943362}}</ref> Upon binding to androgens, the androgen receptor dissociates from accessory proteins, translocates into the nucleus, dimerizes, and then stimulates transcription of androgen-responsive genes.<ref name="pmid22872761">{{cite journal | vauthors = Coffey K, Robson CN | title = Regulation of the androgen receptor by post-translational modifications | journal = The Journal of Endocrinology | volume = 215 | issue = 2 | pages = 221–237 | date = November 2012 | pmid = 22872761 | doi = 10.1530/JOE-12-0238 | s2cid = 20933176 | doi-access = free }}</ref>

The binding of an androgen to the androgen receptor results in a [[conformational change]] in the receptor that, in turn, causes dissociation of [[heat shock protein]]s, transport from the [[cytosol]] into the [[cell nucleus]], and [[Dimerization (chemistry)|dimerization]]. The androgen receptor dimer binds to a specific sequence of DNA known as a [[hormone response element]], where it forms macromolacular protein condensates that might facilitate rapid gene regulation as consequence of local high protein concentrations together with other coregulators.<ref name="pmid37791849">{{cite journal | vauthors = Yavuz S, Kabbech H | title = Compartmentalization of androgen receptors at endogenous genes in living cells | journal = Nucleic Acids Research | date = October 2023 | volume = 51 | issue = 20 | pages = 10992–11009 | pmid = 37791849 | doi = 10.1093/nar/gkad803 | pmc = 10639085 }}</ref> Androgen receptors interact with other proteins in the nucleus, resulting in up- or down-regulation of specific [[gene]] transcription.<ref name="pmid17940184">{{cite journal | vauthors = Heemers HV, Tindall DJ | title = Androgen receptor (AR) coregulators: a diversity of functions converging on and regulating the AR transcriptional complex | journal = Endocrine Reviews | volume = 28 | issue = 7 | pages = 778–808 | date = December 2007 | pmid = 17940184 | doi = 10.1210/er.2007-0019 | doi-access = free }}</ref> Up-regulation or activation of transcription results in increased synthesis of [[messenger RNA]], which, in turn, is translated by [[ribosomes]] to produce specific proteins. One of the known target genes of androgen receptor activation is the [[insulin-like growth factor 1 receptor]] (IGF-1R).<ref name="pmid15753383">{{cite journal | vauthors = Pandini G, Mineo R, Frasca F, Roberts CT, Marcelli M, Vigneri R, Belfiore A | title = Androgens up-regulate the insulin-like growth factor-I receptor in prostate cancer cells | journal = Cancer Research | volume = 65 | issue = 5 | pages = 1849–57 | date = March 2005 | pmid = 15753383 | doi = 10.1158/0008-5472.CAN-04-1837 | doi-access = free }}</ref> Thus, changes in levels of specific proteins in cells is one way that androgen receptors control cell behavior.

One function of androgen receptor that is independent of direct binding to its target DNA sequence is facilitated by recruitment via other [[DNA-binding protein]]s. One example is [[serum response factor]], a protein that activates several genes that cause muscle growth.<ref name="pmid15623502">{{cite journal | vauthors = Vlahopoulos S, Zimmer WE, Jenster G, Belaguli NS, Balk SP, Brinkmann AO, Lanz RB, Zoumpourlis VC, Schwartz RJ | title = Recruitment of the androgen receptor via serum response factor facilitates expression of a myogenic gene | journal = The Journal of Biological Chemistry | volume = 280 | issue = 9 | pages = 7786–92 | date = March 2005 | pmid = 15623502 | doi = 10.1074/jbc.M413992200 | doi-access = free }}</ref>

Androgen receptor is modified by [[post-translational modification]] through [[acetylation]],<ref>{{cite journal | vauthors = Fu M, Wang C, Reutens AT, Wang J, Angeletti RH, Siconolfi-Baez L, Ogryzko V, Avantaggiati ML, Pestell RG | title = p300 and p300/cAMP-response element-binding protein-associated factor acetylate the androgen receptor at sites governing hormone-dependent transactivation | journal = The Journal of Biological Chemistry | volume = 275 | issue = 27 | pages = 20853–60 | date = July 2000 | pmid = 10779504 | doi = 10.1074/jbc.M000660200 | doi-access = free }}</ref> which directly promotes AR-mediated [[transactivation]], [[apoptosis]]<ref>{{cite journal | vauthors = Fu M, Wang C, Wang J, Zhang X, Sakamaki T, Yeung YG, Chang C, Hopp T, Fuqua SA, Jaffray E, Hay RT, Palvimo JJ, Jänne OA, Pestell RG | title = Androgen receptor acetylation governs trans activation and MEKK1-induced apoptosis without affecting in vitro sumoylation and trans-repression function | journal = Molecular and Cellular Biology | volume = 22 | issue = 10 | pages = 3373–88 | date = May 2002 | pmid = 11971970 | pmc = 133781 | doi = 10.1128/mcb.22.10.3373-3388.2002 }}</ref> and contact-independent growth of [[prostate cancer]] cells.<ref>{{cite journal | vauthors = Fu M, Rao M, Wang C, Sakamaki T, Wang J, Di Vizio D, Zhang X, Albanese C, Balk S, Chang C, Fan S, Rosen E, Palvimo JJ, Jänne OA, Muratoglu S, Avantaggiati ML, Pestell RG | title = Acetylation of androgen receptor enhances coactivator binding and promotes prostate cancer cell growth | journal = Molecular and Cellular Biology | volume = 23 | issue = 23 | pages = 8563–75 | date = December 2003 | pmid = 14612401 | pmc = 262657 | doi = 10.1128/mcb.23.23.8563-8575.2003 }}</ref> AR acetylation is induced by androgens<ref>{{cite journal | vauthors = Gong J, Zhu J, Goodman OB, Pestell RG, Schlegel PN, Nanus DM, Shen R | title = Activation of p300 histone acetyltransferase activity and acetylation of the androgen receptor by bombesin in prostate cancer cells | journal = Oncogene | volume = 25 | issue = 14 | pages = 2011–21 | date = March 2006 | pmid = 16434977 | doi = 10.1038/sj.onc.1209231 | doi-access = free }}</ref> and determines recruitment into [[chromatin]].<ref>{{cite journal | vauthors = Fu M, Rao M, Wu K, Wang C, Zhang X, Hessien M, Yeung YG, Gioeli D, Weber MJ, Pestell RG | title = The androgen receptor acetylation site regulates cAMP and AKT but not ERK-induced activity | journal = The Journal of Biological Chemistry | volume = 279 | issue = 28 | pages = 29436–49 | date = July 2004 | pmid = 15123687 | doi = 10.1074/jbc.M313466200 | doi-access = free }}</ref> The AR acetylation site is a key target of [[Nicotinamide adenine dinucleotide|NAD]]-dependent and [[Trichostatin A|TSA]]-dependent [[histone deacetylase]]s<ref name="pmid16923962"/> and [[long non-coding RNA]].<ref>{{cite journal | vauthors = Yang L, Lin C, Jin C, Yang JC, Tanasa B, Li W, Merkurjev D, Ohgi KA, Meng D, Zhang J, Evans CP, Rosenfeld MG | title = lncRNA-dependent mechanisms of androgen-receptor-regulated gene activation programs | journal = Nature | volume = 500 | issue = 7464 | pages = 598–602 | date = August 2013 | pmid = 23945587 | pmc = 4034386 | doi = 10.1038/nature12451 | bibcode = 2013Natur.500..598Y }}</ref>

==== Non-genomic ====
More recently, androgen receptors have been shown to have a second mode of action. As has been also found for other [[steroid hormone receptors]] such as [[estrogen receptor]]s, androgen receptors can have actions that are independent of their interactions with DNA.<ref name="pmid12351684"/><ref name="Fix_2004">{{cite journal | vauthors = Fix C, Jordan C, Cano P, Walker WH | title = Testosterone activates mitogen-activated protein kinase and the cAMP response element binding protein transcription factor in Sertoli cells | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 101 | issue = 30 | pages = 10919–24 | date = July 2004 | pmid = 15263086 | pmc = 503720 | doi = 10.1073/pnas.0404278101 | bibcode = 2004PNAS..10110919F | doi-access = free }}</ref> Androgen receptors interact with certain [[signal transduction]] proteins in the cytoplasm. Androgen binding to cytoplasmic androgen receptors can cause rapid changes in cell function independent of changes in gene transcription, such as changes in [[Ion channel|ion transport]]. Regulation of signal transduction pathways by cytoplasmic androgen receptors can indirectly lead to changes in gene transcription, for example, by leading to phosphorylation of other transcription factors.

== Genetics ==

=== Gene ===
In humans, the androgen receptor is encoded by the ''AR'' [[gene]] located on the [[X chromosome]] at Xq11–12.<ref name="pmid3353726">{{cite journal | vauthors = Chang CS, Kokontis J, Liao ST | title = Molecular cloning of human and rat complementary DNA encoding androgen receptors | journal = Science | volume = 240 | issue = 4850 | pages = 324–6 | date = April 1988 | pmid = 3353726 | doi = 10.1126/science.3353726 | bibcode = 1988Sci...240..324C }}</ref><ref name="pmid3377788">{{cite journal | vauthors = Trapman J, Klaassen P, Kuiper GG, van der Korput JA, Faber PW, van Rooij HC, Geurts van Kessel A, Voorhorst MM, Mulder E, Brinkmann AO | title = Cloning, structure and expression of a cDNA encoding the human androgen receptor | journal = Biochemical and Biophysical Research Communications | volume = 153 | issue = 1 | pages = 241–8 | date = May 1988 | pmid = 3377788 | doi = 10.1016/S0006-291X(88)81214-2 }}</ref>

=== Deficiencies ===
At least 165 disease-causing mutations in this gene have been discovered.<ref name = "Šimčíková_2019 - supplementary table S7">{{cite journal | vauthors = Šimčíková D, Heneberg P | title = Refinement of evolutionary medicine predictions based on clinical evidence for the manifestations of Mendelian diseases | journal = Scientific Reports | volume = 9 | issue = 1 | pages = 18577 | date = December 2019 | pmid = 31819097 | pmc = 6901466 | doi = 10.1038/s41598-019-54976-4| bibcode = 2019NatSR...918577S }}</ref> The [[androgen insensitivity syndrome]], formerly known as testicular feminization, is caused by a mutation in the androgen receptor gene on the [[X chromosome]] (locus: Xq11–Xq12).<ref name="pmid8537246">{{cite journal|vauthors=Brown TR |title=Human androgen insensitivity syndrome |journal=Journal of Andrology |volume=16 |issue=4 |pages=299–303 |year=1995 |doi=10.1002/j.1939-4640.1995.tb00533.x |pmid=8537246 |s2cid=25940392 |doi-access=free }}</ref> The androgen receptor seems to affect neuron physiology and is defective in [[Kennedy's disease]].<ref name="pmid4233749">{{cite journal | vauthors = Kennedy WR, Alter M, Sung JH | title = Progressive proximal spinal and bulbar muscular atrophy of late onset. A sex-linked recessive trait | journal = Neurology | volume = 18 | issue = 7 | pages = 671–80 | date = July 1968 | pmid = 4233749 | doi = 10.1212/WNL.18.7.671 | s2cid = 45735233 }}</ref><ref name="pmid16981011">{{cite journal | vauthors = Yu Z, Dadgar N, Albertelli M, Gruis K, Jordan C, Robins DM, Lieberman AP | title = Androgen-dependent pathology demonstrates myopathic contribution to the Kennedy disease phenotype in a mouse knock-in model | journal = The Journal of Clinical Investigation | volume = 116 | issue = 10 | pages = 2663–72 | date = October 2006 | pmid = 16981011 | pmc = 1564432 | doi = 10.1172/JCI28773 }}</ref> In addition, [[point mutation]]s and [[Trinucleotide repeat expansion|trinucleotide repeat]] [[Gene polymorphism|polymorphism]]s have been linked to a number of additional disorders.<ref name="pmid17334586">{{cite journal | vauthors = Rajender S, Singh L, Thangaraj K | title = Phenotypic heterogeneity of mutations in androgen receptor gene | journal = Asian Journal of Andrology | volume = 9 | issue = 2 | pages = 147–79 | date = March 2007 | pmid = 17334586 | doi = 10.1111/j.1745-7262.2007.00250.x | doi-access = free }}</ref>

=== CAG repeats ===
The AR gene contains [[CAG repeat]]s that affect receptor function, where fewer repeats leads to increased receptor sensitivity to circulating androgens and more repeats leads to decreased receptor sensitivity. Studies have shown that racial variation in CAG repeats exists,<ref name="pmid9933058">{{cite journal | vauthors = Sartor O, Zheng Q, Eastham JA | title = Androgen receptor gene CAG repeat length varies in a race-specific fashion in men without prostate cancer | journal = Urology | volume = 53 | issue = 2 | pages = 378–80 | date = February 1999 | pmid = 9933058 | doi=10.1016/s0090-4295(98)00481-6}}</ref><ref name="pmid29584789">{{cite journal | vauthors = Weintrob N, Eyal O, Slakman M, Segev Becker A, Israeli G, Kalter-Leibovici O, Ben-Shachar S | title = The effect of CAG repeats length on differences in hirsutism among healthy Israeli women of different ethnicities | journal = PLOS ONE | volume = 13 | issue = 3 | pages = e0195046 | year = 2018 | pmid = 29584789 | pmc = 5871002 | doi = 10.1371/journal.pone.0195046 | bibcode = 2018PLoSO..1395046W | doi-access = free }}</ref> with African-Americans having fewer repeats than non-Hispanic white Americans.<ref name="pmid9933058"/> The racial trends in CAG repeats parallels the incidence and mortality of prostate cancer in these two groups.

=== Mutations ===
The [[Enhancer (genetics)|enhancer]] and the gene encoding for these receptors contain recurrent mutations, such as structural rearrangements and copy number changes, acquired in the progression of metastatic castration-resistant prostate cancer (mCRPC) treatment with therapy targeting these receptors (abiraterone, [[enzalutamide]]), make the disease progression determined by the androgen receptor genotype.<ref name=Herberts2022>{{cite journal | vauthors = Herberts C, Annala M, Sipola J, Ng SW, Chen XE, Nurminen A, Korhonen OV, Munzur AD, Beja K, Schönlau E, Bernales CQ, Ritch E, Bacon JV, Lack NA, Nykter M, Aggarwal R, Small EJ, Gleave ME, Quigley DA, Feng FY, Chi KN, Wyatt AW | title = Deep whole-genome ctDNA chronology of treatment-resistant prostate cancer | journal = Nature | volume = 608 | issue = 7921 | pages = 199–208 | date = August 2022 | pmid = 35859180 | doi = 10.1038/s41586-022-04975-9 | bibcode = 2022Natur.608..199H | s2cid = 250730778 }}</ref>

== Structure ==
[[File:Human androgen receptor.png|thumb|294 px|Structure of full length human androgen receptor including N-terminal domain, DNA binding domain, and Ligand binding domain. Corresponding PDB file is available at Sheikhhassani et al.<ref name = "Sheikhhassani_2022">{{cite journal | vauthors = Sheikhhassani V, Scalvini B, Ng J, Heling LW, Ayache Y, Evers TM, Estébanez-Perpiñá E, McEwan IJ, Mashaghi A | title = Topological dynamics of an intrinsically disordered N-terminal domain of the human androgen receptor | journal = Protein Science | volume = 31 | issue = 6 | pages = e4334 | date = June 2022 | pmid = 35634773 | doi = 10.1002/pro.4334 | hdl = 2164/19653 | hdl-access = free }}</ref> ]]
[[File:androgen receptor sequence.png|thumb|294 px|Structural domains of the two isoforms (''AR-A'' and ''AR-B'') of the human androgen receptor. Numbers above the bars refer to the amino acid residues that separate the domains starting from the N-terminus (left) to C-terminus (right). NTD = N-terminal domain, DBD = DNA-binding domain, LBD = ligand-binding domain, AF = activation function.]]

=== Isoforms ===
Two [[protein isoform|isoforms]] of the androgen receptor ('''A''' and '''B''') have been identified:<ref name="pmid8108393">{{cite journal | vauthors = Wilson CM, McPhaul MJ | title = A and B forms of the androgen receptor are present in human genital skin fibroblasts | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 91 | issue = 4 | pages = 1234–8 | date = February 1994 | pmid = 8108393 | pmc = 43131 | doi = 10.1073/pnas.91.4.1234 | bibcode = 1994PNAS...91.1234W | doi-access = free }}</ref>
* '''AR-A''' – 87 [[atomic mass unit|kDa]]; [[N-terminus]] truncated (lacks the first 187 [[amino acids]]), which results from ''in vitro'' [[proteolysis]].<ref name="pmid11719283 ">{{cite journal | vauthors = Gregory CW, He B, Wilson EM | title = The putative androgen receptor-A form results from in vitro proteolysis | journal = Journal of Molecular Endocrinology | volume = 27 | issue = 3 | pages = 309–19 | date = December 2001 | pmid = 11719283 | doi = 10.1677/jme.0.0270309 | doi-access = free }}</ref>
* '''AR-B''' – 110 kDa; full length

=== Domains ===
Like other nuclear receptors, the androgen receptor is modular in structure and is composed of the following functional [[structural domain|domains]] labeled '''A''' through '''F''':<ref name="pmid2734982">{{cite journal | vauthors = Brinkmann AO, Klaasen P, Kuiper GG, van der Korput JA, Bolt J, de Boer W, Smit A, Faber PW, van Rooij HC, Geurts van Kessel A | title = Structure and function of the androgen receptor | journal = Urological Research | volume = 17 | issue = 2 | pages = 87–93 | year = 1989 | pmid = 2734982 | doi = 10.1007/BF00262026 | s2cid = 19706366 }}</ref>
* '''A/B''') – N-terminal is a regulatory domain which is intrinsically disordered<ref>{{cite journal | vauthors = Zhang F, Biswas M, Massah S, Lee J, Lingadahalli S, Wong S, Wells C, Foo J, Khan N, Morin H, Saxena N, Kung SH, Sun B, Parra Nuñez AK, Sanchez C, Chan N, Ung L, Altıntaş UB, Bui JM, Wang Y, Fazli L, Oo HZ, Rennie PS, Lack NA, Cherkasov A, Gleave ME, Gsponer J, Lallous N | title = Dynamic phase separation of the androgen receptor and its coactivators key to regulate gene expression | journal = Nucleic Acids Research | volume = 51 | issue = 1 | pages = 99–116 | date = January 2023 | pmid = 36535377 | pmc = 9841400 | doi = 10.1093/nar/gkac1158 }}</ref> and contains several key motifs/segments:<ref name="pmid7706276">{{cite journal | vauthors = Jenster G, van der Korput HA, Trapman J, Brinkmann AO | title = Identification of two transcription activation units in the N-terminal domain of the human androgen receptor | journal = The Journal of Biological Chemistry | volume = 270 | issue = 13 | pages = 7341–7346 | date = March 1995 | pmid = 7706276 | doi = 10.1074/jbc.270.13.7341 | doi-access = free | hdl = 1765/8551 | hdl-access = free }}</ref>
** Dimerization surface involving residues 1–36, the <sup>23</sup>FQNLF<sup>27</sup> motif<ref>{{cite journal | vauthors = Asangani I, Blair IA, Van Duyne G, Hilser VJ, Moiseenkova-Bell V, Plymate S, Sprenger C, Wand AJ, Penning TM | title = Using biochemistry and biophysics to extinguish androgen receptor signaling in prostate cancer | journal = The Journal of Biological Chemistry | volume = 296 | pages = 100240 | date = 2021 | pmid = 33384381 | pmc = 7949100 | doi = 10.1074/jbc.REV120.012411 | doi-access = free }}</ref> ('''B only''') nd 370–494, both of which interact with the ligand binding domain (LBD) in an intramolecular<ref name="pmid15994236">{{cite journal | vauthors = Schaufele F, Carbonell X, Guerbadot M, Borngraeber S, Chapman MS, Ma AA, Miner JN, Diamond MI | title = The structural basis of androgen receptor activation: intramolecular and intermolecular amino-carboxy interactions | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 102 | issue = 28 | pages = 9802–9807 | date = July 2005 | pmid = 15994236 | pmc = 1168953 | doi = 10.1073/pnas.0408819102 | bibcode = 2005PNAS..102.9802S | doi-access = free }}</ref><ref name="pmid17189428">{{cite journal | vauthors = Klokk TI, Kurys P, Elbi C, Nagaich AK, Hendarwanto A, Slagsvold T, Chang CY, Hager GL, Saatcioglu F | title = Ligand-specific dynamics of the androgen receptor at its response element in living cells | journal = Molecular and Cellular Biology | volume = 27 | issue = 5 | pages = 1823–1843 | date = March 2007 | pmid = 17189428 | pmc = 1820481 | doi = 10.1128/MCB.01297-06 }}</ref><ref name="pmid17420290">{{cite journal | vauthors = van Royen ME, Cunha SM, Brink MC, Mattern KA, Nigg AL, Dubbink HJ, Verschure PJ, Trapman J, Houtsmuller AB | title = Compartmentalization of androgen receptor protein-protein interactions in living cells | journal = The Journal of Cell Biology | volume = 177 | issue = 1 | pages = 63–72 | date = April 2007 | pmid = 17420290 | pmc = 2064112 | doi = 10.1083/jcb.200609178 }}</ref> head-to-tail interaction<ref name="pmid8530400">{{cite journal | vauthors = Langley E, Zhou ZX, Wilson EM | title = Evidence for an anti-parallel orientation of the ligand-activated human androgen receptor dimer | journal = The Journal of Biological Chemistry | volume = 270 | issue = 50 | pages = 29983–29990 | date = December 1995 | pmid = 8530400 | doi = 10.1074/jbc.270.50.29983 | doi-access = free }}</ref><ref name="pmid9717843">{{cite journal | vauthors = Berrevoets CA, Doesburg P, Steketee K, Trapman J, Brinkmann AO | title = Functional interactions of the AF-2 activation domain core region of the human androgen receptor with the amino-terminal domain and with the transcriptional coactivator TIF2 (transcriptional intermediary factor2) | journal = Molecular Endocrinology | volume = 12 | issue = 8 | pages = 1172–1183 | date = August 1998 | pmid = 9717843 | doi = 10.1210/mend.12.8.0153 | hdl-access = free | doi-access = free | hdl = 1765/8892 }}</ref><ref name="pmid15178743">{{cite journal | vauthors = Dubbink HJ, Hersmus R, Verma CS, van der Korput HA, Berrevoets CA, van Tol J, Ziel-van der Made AC, Brinkmann AO, Pike AC, Trapman J | title = Distinct recognition modes of FXXLF and LXXLL motifs by the androgen receptor | journal = Molecular Endocrinology | volume = 18 | issue = 9 | pages = 2132–2150 | date = September 2004 | pmid = 15178743 | doi = 10.1210/me.2003-0375 | doi-access = free | hdl = 1765/13416 | hdl-access = free }}</ref>
*** FXXLF motif; where F = [[phenylalanine]], L = [[leucine]], and X = any amino acid residue a
** Polyglutamine repeat<ref>{{cite journal | vauthors = Van-Duyne G, Blair IA, Sprenger C, Moiseenkova-Bell V, Plymate S, Penning TM | title = The androgen receptor | journal = Vitamins and Hormones | volume = 123 | pages = 439–481 | date = 2023-01-01 | pmid = 37717994 | doi = 10.1016/bs.vh.2023.01.001 | publisher = Academic Press | veditors = Litwack G | series = Hormone Receptors: Structures and Functions | isbn = 978-0-443-13455-5 }}</ref> (AR-B only)
** Transactivation unit 1 (TAU-1) between residues 101 and 370 required for full [[Ligand (biochemistry)|ligand]]-activated transcriptional activity <ref name = "Callewaert_2006">{{cite journal | vauthors = Callewaert L, Van Tilborgh N, Claessens F | title = Interplay between two hormone-independent activation domains in the androgen receptor | journal = Cancer Research | volume = 66 | issue = 1 | pages = 543–553 | date = January 2006 | pmid = 16397271 | doi = 10.1158/0008-5472.CAN-05-2389 }}</ref>
** Trans[[activation]] unit 5 (TAU-5) between residues 360–485 is responsible for the [[constitutive activity]] (activity without bound ligand)<ref name = "Callewaert_2006" />
Despite being highly disordered, the NTD domain adopts a 3D conformation in which two dynamically compact regions form, an N-terminal region (NR) and a C-terminal region (CR), each having distinct topological dynamics and function.<ref name = "Sheikhhassani_2022" />
* '''C''') – [[DNA binding domain]] (DBD)
** Contains two Zinc fingers<ref>{{cite journal | vauthors = Tan MH, Li J, Xu HE, Melcher K, Yong EL | title = Androgen receptor: structure, role in prostate cancer and drug discovery | journal = Acta Pharmacologica Sinica | volume = 36 | issue = 1 | pages = 3–23 | date = January 2015 | pmid = 24909511 | pmc = 4571323 | doi = 10.1038/aps.2014.18 }}</ref>
* '''D''') – Hinge region; flexible region that connects the DBD with the LBD; along with the DBD, contains a ligand dependent [[nuclear localization signal]]<ref name="pmid18420738">{{cite journal | vauthors = Kaku N, Matsuda K, Tsujimura A, Kawata M | title = Characterization of nuclear import of the domain-specific androgen receptor in association with the importin alpha/beta and Ran-guanosine 5'-triphosphate systems | journal = Endocrinology | volume = 149 | issue = 8 | pages = 3960–9 | date = August 2008 | pmid = 18420738 | pmc = 2488236 | doi = 10.1210/en.2008-0137 }}</ref>
* '''E''') – Ligand binding domain (LBD) containing
** activation function 2 (AF-2), responsible for agonist induced activity (activity in the presence of bound agonist)
** AF-2 binds either the N-terminal FXXFL motif [[Intramolecular force|intramolecular]]ly or [[coactivator (genetics)|coactivator]] proteins (containing the LXXLL or preferably FXXFL motifs)<ref name="pmid15178743"/>
** A ligand dependent [[nuclear export signal]]<ref name="pmid12923188">{{cite journal | vauthors = Saporita AJ, Zhang Q, Navai N, Dincer Z, Hahn J, Cai X, Wang Z | title = Identification and characterization of a ligand-regulated nuclear export signal in androgen receptor | journal = The Journal of Biological Chemistry | volume = 278 | issue = 43 | pages = 41998–2005 | date = October 2003 | pmid = 12923188 | doi = 10.1074/jbc.M302460200 | doi-access = free }}</ref>
* '''F''') – [[C-terminal]] domain

=== Splice variants ===
'''AR-V7''' is an androgen receptor [[splice variant]] that can be detected in [[circulating tumor cell]]s of metastatic [[prostate cancer]] patients<ref name=Silberstein2016>{{cite journal | vauthors = Silberstein JL, Taylor MN, Antonarakis ES | title = Novel Insights into Molecular Indicators of Response and Resistance to Modern Androgen-Axis Therapies in Prostate Cancer | language = en | journal = Current Urology Reports | volume = 17 | issue = 4 | pages = 29 | date = April 2016 | pmid = 26902623 | doi = 10.1007/s11934-016-0584-4 | pmc=4888068}}</ref><ref name=Antonarakis2014>{{cite journal | vauthors = Antonarakis ES, Lu C, Wang H, Luber B, Nakazawa M, Roeser JC, Chen Y, Mohammad TA, Chen Y, Fedor HL, Lotan TL, Zheng Q, De Marzo AM, Isaacs JT, Isaacs WB, Nadal R, Paller CJ, Denmeade SR, Carducci MA, Eisenberger MA, Luo J | title = AR-V7 and resistance to enzalutamide and abiraterone in prostate cancer | journal = The New England Journal of Medicine | volume = 371 | issue = 11 | pages = 1028–38 | date = September 2014 | pmid = 25184630 | pmc = 4201502 | doi = 10.1056/NEJMoa1315815 }}</ref> and is predictive of resistance to some drugs (caused by missing Ligand-binding domain in this splice variant).<ref>{{cite web
| url = https://clinicaltrials.gov/ct2/show/NCT02601014
| title = Biomarker-Driven Therapy With Nivolumab and Ipilimumab in Treating Patients With Metastatic Hormone-Resistant Prostate Cancer Expressing AR-V7 - Full Text View - ClinicalTrials.gov
| website = clinicaltrials.gov
| access-date = 2016-02-27
}}</ref>

== Clinical significance ==

High expression in androgen receptor has been linked to aggression and sex drive by affecting the HPA and HPG axis<ref>{{cite journal | vauthors = Cunningham RL, Lumia AR, McGinnis MY | title = Androgen receptors, sex behavior, and aggression | journal = Neuroendocrinology | volume = 96 | issue = 2 | pages = 131–40 | date = 2012 | pmid = 22414851 | pmc = 3474193 | doi = 10.1159/000337663 }}</ref>

Aberrant androgen receptor [[transcription coregulator|coregulator]] activity may contribute to the progression of [[prostate cancer]].<ref>{{cite journal | vauthors = Heinlein CA, Chang C | title = Androgen receptor (AR) coregulators: an overview | journal = Endocrine Reviews | volume = 23 | issue = 2 | pages = 175–200 | date = April 2002 | pmid = 11943742 | doi = 10.1210/edrv.23.2.0460 | doi-access = free }}</ref><ref name=Herberts2022 />

== Ligands ==
{{Affinities of selected androgen receptor ligands}}

=== Agonists ===
* [[Endogenous]] [[androgen]]s (e.g., [[testosterone]], [[dihydrotestosterone]], [[androstenedione]], [[androstenediol]], [[dehydroepiandrosterone]])
* [[Synthetic compound|Synthetic]] [[androgen]]s (e.g., [[methyltestosterone]], [[metandienone]], [[nandrolone]], [[trenbolone]], [[oxandrolone]], [[stanozolol]])

=== Mixed ===
* [[Selective androgen receptor modulator]]s (e.g., [[andarine]], [[enobosarm]])

=== Antagonists ===
* [[Steroidal antiandrogen]]s (e.g., [[cyproterone acetate]], [[chlormadinone acetate]], [[spironolactone]], [[oxendolone]])
* [[Nonsteroidal antiandrogen]]s (e.g., [[flutamide]], [[nilutamide]], [[bicalutamide]], [[enzalutamide]], [[apalutamide]], [[RU-58841]])
* [[N-Terminal domain antiandrogen]]s (e.g., [[bisphenol A]], [[EPI-001]], [[ralaniten]], JN compounds)<ref name=Elshan2019>{{cite journal | vauthors = Elshan ND, Rettig MB, Jung ME |title=Molecules targeting the androgen receptor (AR) signaling axis beyond the AR-Ligand binding domain |journal=Medicinal Research Reviews |volume=39 |issue=3 |pages=910–960 |date=22 November 2018 |doi=10.1002/med.21548|pmid=30565725 |pmc=6608750 }}</ref>

== As a drug target ==
The AR is an important therapeutic target in [[prostate cancer]]. Thus many different [[antiandrogen]]s have been developed, primarily targeting the [[ligand-binding domain]] of the protein.<ref name="Helsen_2014">{{cite journal | vauthors = Helsen C, Van den Broeck T, Voet A, Prekovic S, Van Poppel H, Joniau S, Claessens F | title = Androgen receptor antagonists for prostate cancer therapy | journal = Endocrine-Related Cancer | volume = 21 | issue = 4 | pages = T105–18 | date = August 2014 | pmid = 24639562 | doi = 10.1530/ERC-13-0545 | doi-access = free }}</ref> AR [[ligands]] can either be classified based on their structure ([[steroidal]] or [[nonsteroidal]]) or based on their ability to activate or inhibit transcription ([[agonists]] or [[Receptor antagonist|antagonist]]s).<ref name="Gao_2005">{{cite journal | vauthors = Gao W, Bohl CE, Dalton JT | title = Chemistry and structural biology of androgen receptor | journal = Chemical Reviews | volume = 105 | issue = 9 | pages = 3352–70 | date = September 2005 | pmid = 16159155 | pmc = 2096617 | doi = 10.1021/cr020456u }}</ref> Inhibitors that target alternative functional domains ([[N-terminal domain]], [[DNA-binding domain]]) of the protein are still under development.<ref name=Elshan2019 />

===Drug resistance===
Alteration of ARs may lead to treatment resistance (castration resistance) in prostate cancer as there may be [[missense mutations]] of the [[ligand binding domain]], amplifications of the gene coding for this receptor or in its enhancer, mostly, suggesting the presence of different subclones with different genotypes of these receptors.<ref name=Herberts2022 />

==Interactions==
Androgen receptor has been shown to [[Protein-protein interaction|interact]] with:

{{div col|colwidth=20em}}
* [[AKT1]],<ref name="pmid11404460">{{cite journal | vauthors = Lin HK, Yeh S, Kang HY, Chang C | title = Akt suppresses androgen-induced apoptosis by phosphorylating and inhibiting androgen receptor | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 98 | issue = 13 | pages = 7200–5 | date = June 2001 | pmid = 11404460 | pmc = 34646 | doi = 10.1073/pnas.121173298 | bibcode = 2001PNAS...98.7200L | doi-access = free }}</ref>
* [[BAG1]],<ref name="pmid14517289">{{cite journal | vauthors = Shatkina L, Mink S, Rogatsch H, Klocker H, Langer G, Nestl A, Cato AC | title = The cochaperone Bag-1L enhances androgen receptor action via interaction with the NH2-terminal region of the receptor | journal = Molecular and Cellular Biology | volume = 23 | issue = 20 | pages = 7189–97 | date = October 2003 | pmid = 14517289 | pmc = 230325 | doi = 10.1128/MCB.23.20.7189-7197.2003 }}</ref><ref name="pmid11278763">{{cite journal | vauthors = Knee DA, Froesch BA, Nuber U, Takayama S, Reed JC | title = Structure-function analysis of Bag1 proteins. Effects on androgen receptor transcriptional activity | journal = The Journal of Biological Chemistry | volume = 276 | issue = 16 | pages = 12718–24 | date = April 2001 | pmid = 11278763 | doi = 10.1074/jbc.M010841200 | doi-access = free }}</ref><ref name="pmid9565586">{{cite journal | vauthors = Froesch BA, Takayama S, Reed JC | title = BAG-1L protein enhances androgen receptor function | journal = The Journal of Biological Chemistry | volume = 273 | issue = 19 | pages = 11660–6 | date = May 1998 | pmid = 9565586 | doi = 10.1074/jbc.273.19.11660 | doi-access = free }}</ref>
* [[Beta-catenin]],<ref name=pmid14593076/><ref name=pmid15256534/><ref name="pmid11792709">{{cite journal | vauthors = Yang F, Li X, Sharma M, Sasaki CY, Longo DL, Lim B, Sun Z | title = Linking beta-catenin to androgen-signaling pathway | journal = The Journal of Biological Chemistry | volume = 277 | issue = 13 | pages = 11336–44 | date = March 2002 | pmid = 11792709 | doi = 10.1074/jbc.M111962200 | doi-access = free }}</ref><ref name="pmid12799378">{{cite journal | vauthors = Amir AL, Barua M, McKnight NC, Cheng S, Yuan X, Balk SP | title = A direct beta-catenin-independent interaction between androgen receptor and T cell factor 4 | journal = The Journal of Biological Chemistry | volume = 278 | issue = 33 | pages = 30828–34 | date = August 2003 | pmid = 12799378 | doi = 10.1074/jbc.M301208200 | doi-access = free }}</ref><ref name="pmid12944908">{{cite journal | vauthors = Mulholland DJ, Read JT, Rennie PS, Cox ME, Nelson CC | title = Functional localization and competition between the androgen receptor and T-cell factor for nuclear beta-catenin: a means for inhibition of the Tcf signaling axis | journal = Oncogene | volume = 22 | issue = 36 | pages = 5602–13 | date = August 2003 | pmid = 12944908 | doi = 10.1038/sj.onc.1206802 | doi-access = free }}</ref><ref name="pmid11916967">{{cite journal | vauthors = Pawlowski JE, Ertel JR, Allen MP, Xu M, Butler C, Wilson EM, Wierman ME | title = Liganded androgen receptor interaction with beta-catenin: nuclear co-localization and modulation of transcriptional activity in neuronal cells | journal = The Journal of Biological Chemistry | volume = 277 | issue = 23 | pages = 20702–10 | date = June 2002 | pmid = 11916967 | doi = 10.1074/jbc.M200545200 | doi-access = free }}</ref>
* [[BRCA1]],<ref name="pmid11085509">{{cite journal | vauthors = Park JJ, Irvine RA, Buchanan G, Koh SS, Park JM, Tilley WD, Stallcup MR, Press MF, Coetzee GA | title = Breast cancer susceptibility gene 1 (BRCAI) is a coactivator of the androgen receptor | journal = Cancer Research | volume = 60 | issue = 21 | pages = 5946–9 | date = November 2000 | pmid = 11085509 }}</ref><ref name="pmid11016951">{{cite journal | vauthors = Yeh S, Hu YC, Rahman M, Lin HK, Hsu CL, Ting HJ, Kang HY, Chang C | title = Increase of androgen-induced cell death and androgen receptor transactivation by BRCA1 in prostate cancer cells | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 97 | issue = 21 | pages = 11256–61 | date = October 2000 | pmid = 11016951 | pmc = 17187 | doi = 10.1073/pnas.190353897 | bibcode = 2000PNAS...9711256Y | doi-access = free }}</ref>
* [[C-jun]],<ref name="pmid9211894">{{cite journal | vauthors = Sato N, Sadar MD, Bruchovsky N, Saatcioglu F, Rennie PS, Sato S, Lange PH, Gleave ME | title = Androgenic induction of prostate-specific antigen gene is repressed by protein-protein interaction between the androgen receptor and AP-1/c-Jun in the human prostate cancer cell line LNCaP | journal = The Journal of Biological Chemistry | volume = 272 | issue = 28 | pages = 17485–94 | date = July 1997 | pmid = 9211894 | doi = 10.1074/jbc.272.28.17485 | doi-access = free }}</ref>
* [[Calmodulin 1]],<ref name="pmid14695896">{{cite journal | vauthors = Cifuentes E, Mataraza JM, Yoshida BA, Menon M, Sacks DB, Barrack ER, Reddy GP | title = Physical and functional interaction of androgen receptor with calmodulin in prostate cancer cells | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 101 | issue = 2 | pages = 464–9 | date = January 2004 | pmid = 14695896 | pmc = 327170 | doi = 10.1073/pnas.0307161101 | bibcode = 2004PNAS..101..464C | doi-access = free }}</ref>
* [[Caveolin 1]],<ref name="pmid11278309">{{cite journal | vauthors = Lu ML, Schneider MC, Zheng Y, Zhang X, Richie JP | title = Caveolin-1 interacts with androgen receptor. A positive modulator of androgen receptor mediated transactivation | journal = The Journal of Biological Chemistry | volume = 276 | issue = 16 | pages = 13442–51 | date = April 2001 | pmid = 11278309 | doi = 10.1074/jbc.M006598200 | doi-access = free }}</ref>
* [[CDK9]],<ref name="pmid11266437">{{cite journal | vauthors = Lee DK, Duan HO, Chang C | title = Androgen receptor interacts with the positive elongation factor P-TEFb and enhances the efficiency of transcriptional elongation | journal = The Journal of Biological Chemistry | volume = 276 | issue = 13 | pages = 9978–84 | date = March 2001 | pmid = 11266437 | doi = 10.1074/jbc.M002285200 | doi-access = free }}</ref>
* [[COX5B]],<ref name="pmid11719263">{{cite journal | vauthors = Beauchemin AM, Gottlieb B, Beitel LK, Elhaji YA, Pinsky L, Trifiro MA | title = Cytochrome c oxidase subunit Vb interacts with human androgen receptor: a potential mechanism for neurotoxicity in spinobulbar muscular atrophy | journal = Brain Research Bulletin | volume = 56 | issue = 3–4 | pages = 285–97 | year = 2001 | pmid = 11719263 | doi = 10.1016/S0361-9230(01)00583-4 | s2cid = 24740136 }}</ref>
* [[CREB-binding protein]],<ref name="pmid15691881">{{cite journal | vauthors = Kim J, Jia L, Stallcup MR, Coetzee GA | title = The role of protein kinase A pathway and cAMP responsive element-binding protein in androgen receptor-mediated transcription at the prostate-specific antigen locus | journal = Journal of Molecular Endocrinology | volume = 34 | issue = 1 | pages = 107–18 | date = February 2005 | pmid = 15691881 | doi = 10.1677/jme.1.01701 | doi-access = free }}</ref><ref name="pmid9822653">{{cite journal | vauthors = Frønsdal K, Engedal N, Slagsvold T, Saatcioglu F | title = CREB binding protein is a coactivator for the androgen receptor and mediates cross-talk with AP-1 | journal = The Journal of Biological Chemistry | volume = 273 | issue = 48 | pages = 31853–9 | date = November 1998 | pmid = 9822653 | doi = 10.1074/jbc.273.48.31853 | doi-access = free }}</ref><ref name="pmid12810069">{{cite journal | vauthors = Ishitani K, Yoshida T, Kitagawa H, Ohta H, Nozawa S, Kato S | title = p54nrb acts as a transcriptional coactivator for activation function 1 of the human androgen receptor | journal = Biochemical and Biophysical Research Communications | volume = 306 | issue = 3 | pages = 660–5 | date = July 2003 | pmid = 12810069 | doi = 10.1016/S0006-291X(03)01021-0 }}</ref><ref name="pmid9482849">{{cite journal | vauthors = Aarnisalo P, Palvimo JJ, Jänne OA | title = CREB-binding protein in androgen receptor-mediated signaling | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 95 | issue = 5 | pages = 2122–7 | date = March 1998 | pmid = 9482849 | pmc = 19270 | doi = 10.1073/pnas.95.5.2122 | bibcode = 1998PNAS...95.2122A | doi-access = free }}</ref>
* [[Cyclin D1]],<ref>{{cite journal |vauthors=Reutens AT, Watanabe G, Albanese C, McPhaul MJ, Balk SP, Pestell RG | title = Cyclin D1 binds activating mutants of the androgen receptor | journal = US Endocrine Society Meeting |date= 1998 | issue = 1–528 }}</ref><ref name="pmid11328859">{{cite journal | vauthors = Reutens AT, Fu M, Wang C, Albanese C, McPhaul MJ, Sun Z, Balk SP, Jänne OA, Palvimo JJ, Pestell RG | title = Cyclin D1 binds the androgen receptor and regulates hormone-dependent signaling in a p300/CBP-associated factor (P/CAF)-dependent manner | journal = Molecular Endocrinology | volume = 15 | issue = 5 | pages = 797–811 | date = May 2001 | pmid = 11328859 | doi = 10.1210/mend.15.5.0641 | doi-access = free }}</ref><ref name="pmid15558026">{{cite journal | vauthors = Petre-Draviam CE, Williams EB, Burd CJ, Gladden A, Moghadam H, Meller J, Diehl JA, Knudsen KE | title = A central domain of cyclin D1 mediates nuclear receptor corepressor activity | journal = Oncogene | volume = 24 | issue = 3 | pages = 431–44 | date = January 2005 | pmid = 15558026 | doi = 10.1038/sj.onc.1208200 | doi-access = free }}</ref><ref name="pmid10344732">{{cite journal | vauthors = Knudsen KE, Cavenee WK, Arden KC | title = D-type cyclins complex with the androgen receptor and inhibit its transcriptional transactivation ability | journal = Cancer Research | volume = 59 | issue = 10 | pages = 2297–301 | date = May 1999 | pmid = 10344732 }}</ref>
* [[Cyclin-dependent kinase 7]],<ref name="pmid10734072">{{cite journal | vauthors = Lee DK, Duan HO, Chang C | title = From androgen receptor to the general transcription factor TFIIH. Identification of cdk activating kinase (CAK) as an androgen receptor NH(2)-terminal associated coactivator | journal = The Journal of Biological Chemistry | volume = 275 | issue = 13 | pages = 9308–13 | date = March 2000 | pmid = 10734072 | doi = 10.1074/jbc.275.13.9308 | doi-access = free }}</ref>
* [[DACH1]],<ref name= "pmid19351840">{{cite journal | vauthors = Wu K, Katiyar S, Witkiewicz A, Li A, McCue P, Song LN, Tian L, Jin M, Pestell RG | title = The cell fate determination factor dachshund inhibits androgen receptor signaling and prostate cancer cellular growth | journal = Cancer Research | volume = 69 | issue = 8 | pages = 3347–55 | date = April 2009 | pmid = 19351840 | pmc = 2669850 | doi = 10.1158/0008-5472.CAN-08-3821 }}</ref>
* [[Death associated protein 6]],<ref name="pmid15572661">{{cite journal | vauthors = Lin DY, Fang HI, Ma AH, Huang YS, Pu YS, Jenster G, Kung HJ, Shih HM | title = Negative modulation of androgen receptor transcriptional activity by Daxx | journal = Molecular and Cellular Biology | volume = 24 | issue = 24 | pages = 10529–41 | date = December 2004 | pmid = 15572661 | pmc = 533990 | doi = 10.1128/MCB.24.24.10529-10541.2004 }}</ref>
* [[L-DOPA]],<ref name="pmid12864730">{{cite journal | vauthors = Wafa LA, Cheng H, Rao MA, Nelson CC, Cox M, Hirst M, Sadowski I, Rennie PS | title = Isolation and identification of L-dopa decarboxylase as a protein that binds to and enhances transcriptional activity of the androgen receptor using the repressed transactivator yeast two-hybrid system | journal = The Biochemical Journal | volume = 375 | issue = Pt 2 | pages = 373–83 | date = October 2003 | pmid = 12864730 | pmc = 1223690 | doi = 10.1042/BJ20030689 }}</ref>
* [[EFCAB6]],<ref name="pmid12612053">{{cite journal | vauthors = Niki T, Takahashi-Niki K, Taira T, Iguchi-Ariga SM, Ariga H | title = DJBP: a novel DJ-1-binding protein, negatively regulates the androgen receptor by recruiting histone deacetylase complex, and DJ-1 antagonizes this inhibition by abrogation of this complex | journal = Molecular Cancer Research | volume = 1 | issue = 4 | pages = 247–61 | date = February 2003 | pmid = 12612053 }}</ref>
* [[Epidermal growth factor receptor]],<ref name="pmid15305378">{{cite journal | vauthors = Bonaccorsi L, Carloni V, Muratori M, Formigli L, Zecchi S, Forti G, Baldi E | title = EGF receptor (EGFR) signaling promoting invasion is disrupted in androgen-sensitive prostate cancer cells by an interaction between EGFR and androgen receptor (AR) | journal = International Journal of Cancer | volume = 112 | issue = 1 | pages = 78–86 | date = October 2004 | pmid = 15305378 | doi = 10.1002/ijc.20362 | url = https://flore.unifi.it/bitstream/2158/395766/1/Bonaccoris%20et%20al%20IJC.pdf | hdl = 2158/395766 | s2cid = 46121331 | hdl-access = free }}</ref><ref name="pmid15288768">{{cite journal | vauthors = Bonaccorsi L, Muratori M, Carloni V, Marchiani S, Formigli L, Forti G, Baldi E | title = The androgen receptor associates with the epidermal growth factor receptor in androgen-sensitive prostate cancer cells | journal = Steroids | volume = 69 | issue = 8–9 | pages = 549–52 | date = August 2004 | pmid = 15288768 | doi = 10.1016/j.steroids.2004.05.011 | hdl = 2158/395763 | s2cid = 23831527 | hdl-access = free }}</ref>
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* [[GNB2L1]],<ref name="pmid12958311">{{cite journal | vauthors = Rigas AC, Ozanne DM, Neal DE, Robson CN | title = The scaffolding protein RACK1 interacts with androgen receptor and promotes cross-talk through a protein kinase C signaling pathway | journal = The Journal of Biological Chemistry | volume = 278 | issue = 46 | pages = 46087–93 | date = November 2003 | pmid = 12958311 | doi = 10.1074/jbc.M306219200 | doi-access = free }}</ref>
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* [[HTATIP]],<ref name=pmid11994312/>
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* [[Nuclear receptor coactivator 3|NCOA3]],<ref name=pmid14966121/><ref name="pmid10965917">{{cite journal | vauthors = Tan JA, Hall SH, Petrusz P, French FS | title = Thyroid receptor activator molecule, TRAM-1, is an androgen receptor coactivator | journal = Endocrinology | volume = 141 | issue = 9 | pages = 3440–50 | date = September 2000 | pmid = 10965917 | doi = 10.1210/endo.141.9.7680 | doi-access = free }}</ref><ref name="pmid11747336">{{cite journal | vauthors = Gnanapragasam VJ, Leung HY, Pulimood AS, Neal DE, Robson CN | title = Expression of RAC 3, a steroid hormone receptor co-activator in prostate cancer | journal = British Journal of Cancer | volume = 85 | issue = 12 | pages = 1928–36 | date = December 2001 | pmid = 11747336 | pmc = 2364015 | doi = 10.1054/bjoc.2001.2179 }}</ref>
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* [[Nuclear receptor co-repressor 2|NCOR2]],<ref name=pmid14593076/><ref name="pmid12441355">{{cite journal | vauthors = Liao G, Chen LY, Zhang A, Godavarthy A, Xia F, Ghosh JC, Li H, Chen JD | title = Regulation of androgen receptor activity by the nuclear receptor corepressor SMRT | journal = The Journal of Biological Chemistry | volume = 278 | issue = 7 | pages = 5052–61 | date = February 2003 | pmid = 12441355 | doi = 10.1074/jbc.M206374200 | doi-access = free }}</ref><ref name="pmid11923464">{{cite journal | vauthors = Dotzlaw H, Moehren U, Mink S, Cato AC, Iñiguez Lluhí JA, Baniahmad A | title = The amino terminus of the human AR is target for corepressor action and antihormone agonism | journal = Molecular Endocrinology | volume = 16 | issue = 4 | pages = 661–73 | date = April 2002 | pmid = 11923464 | doi = 10.1210/mend.16.4.0798 | doi-access = free }}</ref>
* [[NONO]],<ref name=pmid12810069/>
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* [[PA2G4]],<ref name="pmid12165860">{{cite journal | vauthors = Zhang Y, Fondell JD, Wang Q, Xia X, Cheng A, Lu ML, Hamburger AW | title = Repression of androgen receptor mediated transcription by the ErbB-3 binding protein, Ebp1 | journal = Oncogene | volume = 21 | issue = 36 | pages = 5609–18 | date = August 2002 | pmid = 12165860 | doi = 10.1038/sj.onc.1205638 | doi-access = free }}</ref>
* [[PAK6]],<ref name="pmid11278661">{{cite journal | vauthors = Yang F, Li X, Sharma M, Zarnegar M, Lim B, Sun Z | title = Androgen receptor specifically interacts with a novel p21-activated kinase, PAK6 | journal = The Journal of Biological Chemistry | volume = 276 | issue = 18 | pages = 15345–53 | date = May 2001 | pmid = 11278661 | doi = 10.1074/jbc.M010311200 | doi-access = free }}</ref><ref name="pmid11773441">{{cite journal | vauthors = Lee SR, Ramos SM, Ko A, Masiello D, Swanson KD, Lu ML, Balk SP | title = AR and ER interaction with a p21-activated kinase (PAK6) | journal = Molecular Endocrinology | volume = 16 | issue = 1 | pages = 85–99 | date = January 2002 | pmid = 11773441 | doi = 10.1210/mend.16.1.0753 | doi-access = free }}</ref>
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* [[Protein inhibitor of activated STAT2|PIAS2]],<ref name="pmid11117529">{{cite journal | vauthors = Kotaja N, Aittomäki S, Silvennoinen O, Palvimo JJ, Jänne OA | title = ARIP3 (androgen receptor-interacting protein 3) and other PIAS (protein inhibitor of activated STAT) proteins differ in their ability to modulate steroid receptor-dependent transcriptional activation | journal = Molecular Endocrinology | volume = 14 | issue = 12 | pages = 1986–2000 | date = December 2000 | pmid = 11117529 | doi = 10.1210/mend.14.12.0569 | doi-access = free }}</ref><ref name="pmid9920921">{{cite journal | vauthors = Moilanen AM, Karvonen U, Poukka H, Yan W, Toppari J, Jänne OA, Palvimo JJ | title = A testis-specific androgen receptor coregulator that belongs to a novel family of nuclear proteins | journal = The Journal of Biological Chemistry | volume = 274 | issue = 6 | pages = 3700–4 | date = February 1999 | pmid = 9920921 | doi = 10.1074/jbc.274.6.3700 | doi-access = free }}</ref>
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* [[PTEN (gene)|PTEN]],<ref name="pmid15205473">{{cite journal | vauthors = Lin HK, Hu YC, Lee DK, Chang C | title = Regulation of androgen receptor signaling by PTEN (phosphatase and tensin homolog deleted on chromosome 10) tumor suppressor through distinct mechanisms in prostate cancer cells | journal = Molecular Endocrinology | volume = 18 | issue = 10 | pages = 2409–23 | date = October 2004 | pmid = 15205473 | doi = 10.1210/me.2004-0117 | doi-access = free }}</ref>
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* [[Src (gene)|Src]],<ref name="pmid15205473"/><ref name="pmid15466214">{{cite journal | vauthors = Unni E, Sun S, Nan B, McPhaul MJ, Cheskis B, Mancini MA, Marcelli M | title = Changes in androgen receptor nongenotropic signaling correlate with transition of LNCaP cells to androgen independence | journal = Cancer Research | volume = 64 | issue = 19 | pages = 7156–68 | date = October 2004 | pmid = 15466214 | doi = 10.1158/0008-5472.CAN-04-1121 | doi-access = free }}</ref><ref name="pmid15027889">{{cite journal | vauthors = Powell SM, Christiaens V, Voulgaraki D, Waxman J, Claessens F, Bevan CL | title = Mechanisms of androgen receptor signalling via steroid receptor coactivator-1 in prostate | journal = Endocrine-Related Cancer | volume = 11 | issue = 1 | pages = 117–30 | date = March 2004 | pmid = 15027889 | doi = 10.1677/erc.0.0110117 | doi-access = free }}</ref>
* [[SRY]],<ref name="pmid11585838">{{cite journal | vauthors = Yuan X, Lu ML, Li T, Balk SP | title = SRY interacts with and negatively regulates androgen receptor transcriptional activity | journal = The Journal of Biological Chemistry | volume = 276 | issue = 49 | pages = 46647–54 | date = December 2001 | pmid = 11585838 | doi = 10.1074/jbc.M108404200 | doi-access = free }}</ref>
* [[STAT3]],<ref name="pmid11322786">{{cite journal | vauthors = Matsuda T, Junicho A, Yamamoto T, Kishi H, Korkmaz K, Saatcioglu F, Fuse H, Muraguchi A | title = Cross-talk between signal transducer and activator of transcription 3 and androgen receptor signaling in prostate carcinoma cells | journal = Biochemical and Biophysical Research Communications | volume = 283 | issue = 1 | pages = 179–87 | date = April 2001 | pmid = 11322786 | doi = 10.1006/bbrc.2001.4758 }}</ref><ref name="pmid11751884">{{cite journal | vauthors = Ueda T, Bruchovsky N, Sadar MD | title = Activation of the androgen receptor N-terminal domain by interleukin-6 via MAPK and STAT3 signal transduction pathways | journal = The Journal of Biological Chemistry | volume = 277 | issue = 9 | pages = 7076–85 | date = March 2002 | pmid = 11751884 | doi = 10.1074/jbc.M108255200 | doi-access = free }}</ref>
* [[SVIL]],<ref name="pmid11792840">{{cite journal | vauthors = Ting HJ, Yeh S, Nishimura K, Chang C | title = Supervillin associates with androgen receptor and modulates its transcriptional activity | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 99 | issue = 2 | pages = 661–6 | date = January 2002 | pmid = 11792840 | pmc = 117362 | doi = 10.1073/pnas.022469899 | bibcode = 2002PNAS...99..661T | doi-access = free }}</ref>
* [[Testicular receptor 2]],<ref name="pmid12949936">{{cite journal | vauthors = Mu X, Chang C | title = TR2 orphan receptor functions as negative modulator for androgen receptor in prostate cancer cells PC-3 | journal = The Prostate | volume = 57 | issue = 2 | pages = 129–33 | date = October 2003 | pmid = 12949936 | doi = 10.1002/pros.10282 | s2cid = 24134119 }}</ref>
* [[Testicular receptor 4]],<ref name="pmid10611280">{{cite journal | vauthors = Lee YF, Shyr CR, Thin TH, Lin WJ, Chang C | title = Convergence of two repressors through heterodimer formation of androgen receptor and testicular orphan receptor-4: a unique signaling pathway in the steroid receptor superfamily | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 96 | issue = 26 | pages = 14724–9 | date = December 1999 | pmid = 10611280 | pmc = 24715 | doi = 10.1073/pnas.96.26.14724 | bibcode = 1999PNAS...9614724L | doi-access = free }}</ref>
* [[TGFB1I1]],<ref name="pmid11779876">{{cite journal | vauthors = He B, Minges JT, Lee LW, Wilson EM | title = The FXXLF motif mediates androgen receptor-specific interactions with coregulators | journal = The Journal of Biological Chemistry | volume = 277 | issue = 12 | pages = 10226–35 | date = March 2002 | pmid = 11779876 | doi = 10.1074/jbc.M111975200 | doi-access = free }}</ref><ref name="pmid11856738">{{cite journal | vauthors = Wang X, Yang Y, Guo X, Sampson ER, Hsu CL, Tsai MY, Yeh S, Wu G, Guo Y, Chang C | title = Suppression of androgen receptor transactivation by Pyk2 via interaction and phosphorylation of the ARA55 coregulator | journal = The Journal of Biological Chemistry | volume = 277 | issue = 18 | pages = 15426–31 | date = May 2002 | pmid = 11856738 | doi = 10.1074/jbc.M111218200 | doi-access = free }}</ref>
* [[TMF1]],<ref name="pmid10428808">{{cite journal | vauthors = Hsiao PW, Chang C | title = Isolation and characterization of ARA160 as the first androgen receptor N-terminal-associated coactivator in human prostate cells | journal = The Journal of Biological Chemistry | volume = 274 | issue = 32 | pages = 22373–9 | date = August 1999 | pmid = 10428808 | doi = 10.1074/jbc.274.32.22373 | doi-access = free }}</ref>
* [[TRIM68]],<ref name="pmid18451177">{{cite journal | vauthors = Miyajima N, Maruyama S, Bohgaki M, Kano S, Shigemura M, Shinohara N, Nonomura K, Hatakeyama S | title = TRIM68 regulates ligand-dependent transcription of androgen receptor in prostate cancer cells | journal = Cancer Research | volume = 68 | issue = 9 | pages = 3486–94 | date = May 2008 | pmid = 18451177 | doi = 10.1158/0008-5472.CAN-07-6059 | doi-access = free }}</ref>
* [[UBE2I]],<ref name=pmid14593076/><ref name="pmid15256534">{{cite journal | vauthors = Masiello D, Chen SY, Xu Y, Verhoeven MC, Choi E, Hollenberg AN, Balk SP | title = Recruitment of beta-catenin by wild-type or mutant androgen receptors correlates with ligand-stimulated growth of prostate cancer cells | journal = Molecular Endocrinology | volume = 18 | issue = 10 | pages = 2388–401 | date = October 2004 | pmid = 15256534 | doi = 10.1210/me.2003-0436 | doi-access = free }}</ref><ref name="pmid10383460">{{cite journal | vauthors = Poukka H, Aarnisalo P, Karvonen U, Palvimo JJ, Jänne OA | title = Ubc9 interacts with the androgen receptor and activates receptor-dependent transcription | journal = The Journal of Biological Chemistry | volume = 274 | issue = 27 | pages = 19441–6 | date = July 1999 | pmid = 10383460 | doi = 10.1074/jbc.274.27.19441 | doi-access = free }}</ref><ref name="pmid10654935">{{cite journal | vauthors = Müller JM, Isele U, Metzger E, Rempel A, Moser M, Pscherer A, Breyer T, Holubarsch C, Buettner R, Schüle R | title = FHL2, a novel tissue-specific coactivator of the androgen receptor | journal = The EMBO Journal | volume = 19 | issue = 3 | pages = 359–69 | date = February 2000 | pmid = 10654935 | pmc = 305573 | doi = 10.1093/emboj/19.3.359 }}</ref><ref name="pmid12089345">{{cite journal | vauthors = Cheng S, Brzostek S, Lee SR, Hollenberg AN, Balk SP | title = Inhibition of the dihydrotestosterone-activated androgen receptor by nuclear receptor corepressor | journal = Molecular Endocrinology | volume = 16 | issue = 7 | pages = 1492–501 | date = July 2002 | pmid = 12089345 | doi = 10.1210/mend.16.7.0870 | doi-access = free }}</ref><ref name="pmid15598662">{{cite journal | vauthors = Hodgson MC, Astapova I, Cheng S, Lee LJ, Verhoeven MC, Choi E, Balk SP, Hollenberg AN | title = The androgen receptor recruits nuclear receptor CoRepressor (N-CoR) in the presence of mifepristone via its N and C termini revealing a novel molecular mechanism for androgen receptor antagonists | journal = The Journal of Biological Chemistry | volume = 280 | issue = 8 | pages = 6511–9 | date = February 2005 | pmid = 15598662 | doi = 10.1074/jbc.M408972200 | doi-access = free }}</ref>
* [[UXT]],<ref name="pmid11854421">{{cite journal | vauthors = Markus SM, Taneja SS, Logan SK, Li W, Ha S, Hittelman AB, Rogatsky I, Garabedian MJ | title = Identification and characterization of ART-27, a novel coactivator for the androgen receptor N terminus | journal = Molecular Biology of the Cell | volume = 13 | issue = 2 | pages = 670–82 | date = February 2002 | pmid = 11854421 | pmc = 65658 | doi = 10.1091/mbc.01-10-0513 }}</ref> and
* [[ZMIZ1]].<ref name="pmid14609956">{{cite journal | vauthors = Sharma M, Li X, Wang Y, Zarnegar M, Huang CY, Palvimo JJ, Lim B, Sun Z | title = hZimp10 is an androgen receptor co-activator and forms a complex with SUMO-1 at replication foci | journal = The EMBO Journal | volume = 22 | issue = 22 | pages = 6101–14 | date = November 2003 | pmid = 14609956 | pmc = 275443 | doi = 10.1093/emboj/cdg585 }}</ref>
{{Div col end}}

==See also==
* [[Membrane androgen receptor]]
* [[Discovery and development of antiandrogens]]

==References==
{{Reflist}}

== Further reading ==
{{refbegin}}
* {{cite book | vauthors = Brinkmann AO | veditors = McLachlan R | title = Endocrinology of Male Reproduction | date = November 2009 | access-date = 2008-04-29 | publisher = Endotext.org | chapter = Androgen physiology: receptor and metabolic disorders | chapter-url = http://www.endotext.org/male/male3/male3.pdf | archive-date = 2012-02-22 | archive-url = https://web.archive.org/web/20120222032949/http://www.endotext.org/male/male3/male3.pdf | url-status = dead }}
* {{cite web | url = http://androgendb.mcgill.ca/ | title = The Androgen Receptor Gene Mutations Database Server | vauthors = Gottlieb B | date = 2007-07-24 | publisher = McGill University | access-date = 2008-04-29| archive-url= https://web.archive.org/web/20080422174339/http://androgendb.mcgill.ca/| archive-date= 22 April 2008 | url-status= live}}
* {{cite thesis | vauthors = Thompson J | url = http://ethesis.helsinki.fi/julkaisut/laa/biola/vk/thompson/molecula.pdf | title = Molecular Mechanisms of Androgen Receptor Interactions | degree = Ph.D. | date = 2006-09-30 | id = Biomedical Dissertations No. 80 | publisher = University of Helsinki | access-date = 2008-04-29 | archive-url = https://web.archive.org/web/20080406084901/http://ethesis.helsinki.fi/julkaisut/laa/biola/vk/thompson/molecula.pdf | archive-date = 6 April 2008 | url-status = dead }}
{{refend}}

==External links==
{{Commons category|Androgen receptor}}
* [https://www.ncbi.nlm.nih.gov/books/NBK1429/  GeneReviews/NCBI/NIH/UW entry on Androgen Insensitivity Syndrome]
* [https://www.ncbi.nlm.nih.gov/omim/300068,313700,300068,313700  OMIM entries on Androgen Insensitivity Syndrome]
* [https://www.ncbi.nlm.nih.gov/bookshelf/br.fcgi?book=gene&part=kennedy  GeneReviews/NIH/NCBI/UW entry on Spinal and Bulbar Muscular Atrophy, Kennedy's Disease, SBMA, X-Linked Spinal and Bulbar Muscular Atrophy]
* [https://www.ncbi.nlm.nih.gov/omim/313200,313700,313200,313700 OMIM entries on Spinal and Bulbar Muscular Atrophy, Kennedy's Disease, SBMA, X-Linked Spinal and Bulbar Muscular Atrophy]
* {{MeshName|Androgen+Receptors}}
* {{UCSC gene info|AR}}
* {{PDBe-KB2|P10275|Human Androgen receptor}}
* {{PDBe-KB2|P19091|Mouse Androgen receptor}}

{{Transcription factors|g2}}
{{Androgen receptor modulators}}

{{DEFAULTSORT:Androgen Receptor}}
[[Category:Genes on human chromosome X]]
[[Category:Nuclear receptors|3]]