Androgen receptor

AR
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesAR, AIS, AR8, DHTR, HUMARA, HYSP1, KD, NR3C4, SBMA, SMAX1, TFM, androgen receptor
External IDsOMIM: 313700 MGI: 88064 HomoloGene: 28 GeneCards: AR
RNA expression pattern


More reference expression data
Orthologs
SpeciesHumanMouse
Entrez

367

11835

Ensembl

ENSG00000169083

ENSMUSG00000046532

UniProt

P10275

P19091

RefSeq (mRNA)

NM_001011645
NM_000044

NM_013476

RefSeq (protein)

NP_038504

Location (UCSC)Chr X: 67.54 – 67.73 MbChr X: 98.15 – 98.32 Mb
PubMed search[1][2]
Wikidata
View/Edit HumanView/Edit Mouse
Androgen_recep

crystal structure of the human androgen receptor ligand binding domain bound with an androgen receptor nh2-terminal peptide, ar20-30, and r1881
Identifiers
Symbol Androgen_recep
Pfam PF02166
InterPro IPR001103
Normal function of the androgen receptor. Testosterone (T) enters the cell and, if 5-alpha-reductase is present, is converted into dihydrotestone (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.[3][4][5][6]

The androgen receptor (AR), also known as NR3C4 (nuclear receptor subfamily 3, group C, member 4), is a type of nuclear receptor[7] that is activated by binding either of the androgenic hormones, testosterone, or dihydrotestosterone[8] in the cytoplasm and then translocating into the nucleus. The androgen receptor is most closely related to the progesterone receptor, and progestins in higher dosages can block the androgen receptor.[9][10]

The main function of the androgen receptor is as a DNA-binding transcription factor that regulates gene expression;[11] however, the androgen receptor has other functions as well.[12] 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 to dihydrotestosterone, an even more potent agonist for androgen receptor activation.[13] 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 follicles.[14] Hence, testosterone is responsible primarily for the development of male primary sexual characteristics, whereas dihydrotestosterone is responsible for secondary male characteristics.

Androgens cause slow epiphysis, or maturation of the bones, but more of the potent epiphysis 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.[15]

Also, AR knockout-mice studies have shown that AR is essential for normal female fertility, being required for development and full functionality of the ovarian follicles and ovulation, working through both intra-ovarian and neuroendocrine mechanisms.[16]

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 osteoblasts and osteocytes.[17]

Mechanism of action

Genomic

The primary mechanism of action for androgen receptors is direct regulation of gene transcription. 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 proteins, transport from the cytosol into the cell nucleus, and dimerization. The androgen receptor dimer binds to a specific sequence of DNA known as a hormone response element. Androgen receptors interact with other proteins in the nucleus, resulting in up- or down-regulation of specific gene transcription.[18] 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 I receptor (IGF-1R).[19] 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 proteins. One example is serum response factor, a protein that activates several genes that cause muscle growth.[20]

Androgen receptor is modified by post translational modification through acetylation,[21] which directly promotes AR mediated transactivation, apoptosis[22] and contact independent growth of prostate cancer cells.[23] AR acetylation is induced by androgens [24] and determines recruitment into chromatin.[25] The AR acetylation site is a key target of NAD-dependent and TSA-dependent histone deacetylases [26] and long non coding RNA.[27]

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 receptors, androgen receptors can have actions that are independent of their interactions with DNA.[12][28] 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 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.[29][30]

AR deficiencies

The androgen insensitivity syndrome, formerly known as testicular feminization, is caused by a mutation of the androgen receptor gene located on the X chromosome (locus:Xq11-Xq12).[31] The androgen receptor seems to affect neuron physiology and is defective in Kennedy's disease.[32][33] In addition, point mutations and trinucleotide repeat polymorphisms has been linked to a number of additional disorders.[34]

CAG repeats

The AR gene contains CAG repeats which 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, with African-Americans having less repeats, Caucasians having an intermediate number of repeats, and Asians having the longest.[35] The racial trends in CAG repeats parallels the incidence and mortality of prostate cancer in these groups.

Structure

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 isoforms of the androgen receptor (A and B) have been identified:[36]

Domains

Like other nuclear receptors, the androgen receptor is modular in structure and is composed of the following functional domains labeled A through F:[38]

Splice variants

AR-V7 is an androgen receptor splice variant that can be detected in circulating tumor cells of metastatic prostate cancer patients.[48][49] and is predictive of resistance to some drugs.[50]

Ligands

Agonists

Mixed

Antagonists

As a drug target

The AR is important for therapeutic target in prostate cancer, thus many different inhibitors have been developed, primarily targeting the ligand binding domain of the protein, while inhibitors that target the N-terminal domain of the protein are still under development.[51] 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 antagonists).[52]

Interactions

Androgen receptor has been shown to interact with:

See also

References

  1. ↑ "Human PubMed Reference:".
  2. ↑ "Mouse PubMed Reference:".
  3. ↑ Quigley CA, De Bellis A, Marschke KB, el-Awady MK, Wilson EM, French FS (June 1995). "Androgen receptor defects: historical, clinical, and molecular perspectives". Endocrine Reviews. 16 (3): 271–321. PMID 7671849. doi:10.1210/edrv-16-3-271.
  4. ↑ Gottlieb B, Lombroso R, Beitel LK, Trifiro MA (January 2005). "Molecular pathology of the androgen receptor in male (in)fertility". Reproductive Biomedicine Online. 10 (1): 42–8. PMID 15705293. doi:10.1016/S1472-6483(10)60802-4.
  5. ↑ Choong CS, Wilson EM (December 1998). "Trinucleotide repeats in the human androgen receptor: a molecular basis for disease". Journal of Molecular Endocrinology. 21 (3): 235–57. PMID 9845666. doi:10.1677/jme.0.0210235.
  6. ↑ Meehan KL, Sadar MD (May 2003). "Androgens and androgen receptor in prostate and ovarian malignancies". Frontiers in Bioscience. 8 (1-3): d780–800. PMID 12700055. doi:10.2741/1063.
  7. ↑ 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 (December 2006). "International Union of Pharmacology. LXV. The pharmacology and classification of the nuclear receptor superfamily: glucocorticoid, mineralocorticoid, progesterone, and androgen receptors". Pharmacological Reviews. 58 (4): 782–97. PMID 17132855. doi:10.1124/pr.58.4.9.
  8. ↑ Roy AK, Lavrovsky Y, Song CS, Chen S, Jung MH, Velu NK, Bi BY, Chatterjee B (1999). "Regulation of androgen action". Vitamins and Hormones. Vitamins & Hormones. 55: 309–52. ISBN 978-0-12-709855-5. PMID 9949684. doi:10.1016/S0083-6729(08)60938-3.
  9. ↑ Bardin CW, Brown T, Isomaa VV, Jänne OA (1983). "Progestins can mimic, inhibit and potentiate the actions of androgens". Pharmacology & Therapeutics. 23 (3): 443–59. PMID 6371845. doi:10.1016/0163-7258(83)90023-2.
  10. ↑ Raudrant D, Rabe T (2003). "Progestogens with antiandrogenic properties". Drugs. 63 (5): 463–92. PMID 12600226. doi:10.2165/00003495-200363050-00003.
  11. ↑ Mooradian AD, Morley JE, Korenman SG (February 1987). "Biological actions of androgens". Endocrine Reviews. 8 (1): 1–28. PMID 3549275. doi:10.1210/edrv-8-1-1.
  12. 1 2 Heinlein CA, Chang C (October 2002). "The roles of androgen receptors and androgen-binding proteins in nongenomic androgen actions". Molecular Endocrinology. 16 (10): 2181–7. PMID 12351684. doi:10.1210/me.2002-0070.
  13. ↑ Davison SL, Bell R (April 2006). "Androgen physiology". Seminars in Reproductive Medicine. 24 (2): 71–7. PMID 16633980. doi:10.1055/s-2006-939565.
  14. ↑ Sinisi AA, Pasquali D, Notaro A, Bellastella A (2003). "Sexual differentiation". Journal of Endocrinological Investigation. 26 (3 Suppl): 23–8. PMID 12834017.
  15. ↑ Frank GR (September 2003). "Role of estrogen and androgen in pubertal skeletal physiology". Medical and Pediatric Oncology. 41 (3): 217–21. PMID 12868122. doi:10.1002/mpo.10340.
  16. ↑ Walters KA, Simanainen U, Handelsman DJ (March 2010). "Molecular insights into androgen actions in male and female reproductive function from androgen receptor knockout models". Human Reproduction Update. 16 (5): 543–58. PMID 20231167. doi:10.1093/humupd/dmq003.
  17. ↑ Sinnesael M, Claessens F, Laurent M, Dubois V, Boonen S, Deboel L, Vanderschueren D (December 2012). "Androgen receptor (AR) in osteocytes is important for the maintenance of male skeletal integrity: evidence from targeted AR disruption in mouse osteocytes". Journal of Bone and Mineral Research. 27 (12): 2535–43. PMID 22836391. doi:10.1002/jbmr.1713.
  18. ↑ Heemers HV, Tindall DJ (December 2007). "Androgen receptor (AR) coregulators: a diversity of functions converging on and regulating the AR transcriptional complex". Endocrine Reviews. 28 (7): 778–808. PMID 17940184. doi:10.1210/er.2007-0019.
  19. ↑ Pandini G, Mineo R, Frasca F, Roberts CT, Marcelli M, Vigneri R, Belfiore A (March 2005). "Androgens up-regulate the insulin-like growth factor-I receptor in prostate cancer cells". Cancer Research. 65 (5): 1849–57. PMID 15753383. doi:10.1158/0008-5472.CAN-04-1837.
  20. ↑ Vlahopoulos S, Zimmer WE, Jenster G, Belaguli NS, Balk SP, Brinkmann AO, Lanz RB, Zoumpourlis VC, Schwartz RJ (March 2005). "Recruitment of the androgen receptor via serum response factor facilitates expression of a myogenic gene". The Journal of Biological Chemistry. 280 (9): 7786–92. PMID 15623502. doi:10.1074/jbc.M413992200.
  21. ↑ Fu, M; Wang, C; Reutens, AT; Wang, J; Angeletti, RH; Siconolfi-Baez, L; Ogryzko, V; Avantaggiati, ML; Pestell, RG (7 July 2000). "p300 and p300/cAMP-response element-binding protein-associated factor acetylate the androgen receptor at sites governing hormone-dependent transactivation.". The Journal of Biological Chemistry. 275 (27): 20853–60. PMID 10779504. doi:10.1074/jbc.M000660200.
  22. ↑ 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 (May 2002). "Androgen receptor acetylation governs trans activation and MEKK1-induced apoptosis without affecting in vitro sumoylation and trans-repression function". Molecular and Cellular Biology. 22 (10): 3373–88. PMC 133781 Freely accessible. PMID 11971970. doi:10.1128/mcb.22.10.3373-3388.2002.
  23. ↑ 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 (December 2003). "Acetylation of androgen receptor enhances coactivator binding and promotes prostate cancer cell growth.". Molecular and Cellular Biology. 23 (23): 8563–75. PMC 262657 Freely accessible. PMID 14612401. doi:10.1128/mcb.23.23.8563-8575.2003.
  24. ↑ Gong J, Zhu J, Goodman OB, Pestell RG, Schlegel PN, Nanus DM, Shen R (March 2006). "Activation of p300 histone acetyltransferase activity and acetylation of the androgen receptor by bombesin in prostate cancer cells". Oncogene. 25 (14): 2011–21. PMID 16434977. doi:10.1038/sj.onc.1209231.
  25. ↑ Fu M, Rao M, Wu K, Wang C, Zhang X, Hessien M, Yeung YG, Gioeli D, Weber MJ, Pestell RG (July 2004). "The androgen receptor acetylation site regulates cAMP and AKT but not ERK-induced activity". The Journal of Biological Chemistry. 279 (28): 29436–49. PMID 15123687. doi:10.1074/jbc.M313466200.
  26. ↑ Fu M, Liu M, Sauve AA, Jiao X, Zhang X, Wu X, Powell MJ, Yang T, Gu W, Avantaggiati ML, Pattabiraman N, Pestell TG, Wang F, Quong AA, Wang C, Pestell RG (November 2006). "Hormonal control of androgen receptor function through SIRT1". Molecular and Cellular Biology. 26 (21): 8122–35. PMC 1636736 Freely accessible. PMID 16923962. doi:10.1128/MCB.00289-06.
  27. ↑ Yang L, Lin C, Jin C, Yang JC, Tanasa B, Li W, Merkurjev D, Ohgi KA, Meng D, Zhang J, Evans CP, Rosenfeld MG (August 2013). "lncRNA-dependent mechanisms of androgen-receptor-regulated gene activation programs". Nature. 500 (7464): 598–602. PMC 4034386 Freely accessible. PMID 23945587. doi:10.1038/nature12451.
  28. ↑ Fix C, Jordan C, Cano P, Walker WH (July 2004). "Testosterone activates mitogen-activated protein kinase and the cAMP response element binding protein transcription factor in Sertoli cells". Proceedings of the National Academy of Sciences of the United States of America. 101 (30): 10919–24. PMC 503720 Freely accessible. PMID 15263086. doi:10.1073/pnas.0404278101.
  29. ↑ Chang CS, Kokontis J, Liao ST (April 1988). "Molecular cloning of human and rat complementary DNA encoding androgen receptors". Science. 240 (4850): 324–6. PMID 3353726. doi:10.1126/science.3353726.
  30. ↑ 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 (May 1988). "Cloning, structure and expression of a cDNA encoding the human androgen receptor". Biochemical and Biophysical Research Communications. 153 (1): 241–8. PMID 3377788. doi:10.1016/S0006-291X(88)81214-2.
  31. ↑ Brown TR (1995). "Human androgen insensitivity syndrome". Journal of Andrology. 16 (4): 299–303. PMID 8537246. Archived from the original (abstract) on 2008-07-24.
  32. ↑ Kennedy WR, Alter M, Sung JH (July 1968). "Progressive proximal spinal and bulbar muscular atrophy of late onset. A sex-linked recessive trait". Neurology. 18 (7): 671–80. PMID 4233749. doi:10.1212/WNL.18.7.671.
  33. ↑ Yu Z, Dadgar N, Albertelli M, Gruis K, Jordan C, Robins DM, Lieberman AP (October 2006). "Androgen-dependent pathology demonstrates myopathic contribution to the Kennedy disease phenotype in a mouse knock-in model". The Journal of Clinical Investigation. 116 (10): 2663–72. PMC 1564432 Freely accessible. PMID 16981011. doi:10.1172/JCI28773.
  34. ↑ Rajender S, Singh L, Thangaraj K (March 2007). "Phenotypic heterogeneity of mutations in androgen receptor gene". Asian Journal of Andrology. 9 (2): 147–79. PMID 17334586. doi:10.1111/j.1745-7262.2007.00250.x.
  35. ↑ Sartor O, Zheng Q, Eastham JA (February 1999). "Androgen receptor gene CAG repeat length varies in a race-specific fashion in men without prostate cancer". Urology. 53 (2): 378–80. PMID 9933058. doi:10.1016/s0090-4295(98)00481-6.
  36. ↑ Wilson CM, McPhaul MJ (February 1994). "A and B forms of the androgen receptor are present in human genital skin fibroblasts". Proceedings of the National Academy of Sciences of the United States of America. 91 (4): 1234–8. PMC 43131 Freely accessible. PMID 8108393. doi:10.1073/pnas.91.4.1234.
  37. ↑ Gregory CW, He B, Wilson EM (December 2001). "The putative androgen receptor-A form results from in vitro proteolysis". Journal of Molecular Endocrinology. 27 (3): 309–19. PMID 11719283. doi:10.1677/jme.0.0270309.
  38. ↑ 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 (1989). "Structure and function of the androgen receptor". Urological Research. 17 (2): 87–93. PMID 2734982. doi:10.1007/BF00262026.
  39. ↑ Jenster G, van der Korput HA, Trapman J, Brinkmann AO (March 1995). "Identification of two transcription activation units in the N-terminal domain of the human androgen receptor". The Journal of Biological Chemistry. 270 (13): 7341–6. PMID 7706276. doi:10.1074/jbc.270.13.7341.
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  43. ↑ Langley E, Zhou ZX, Wilson EM (December 1995). "Evidence for an anti-parallel orientation of the ligand-activated human androgen receptor dimer". The Journal of Biological Chemistry. 270 (50): 29983–90. PMID 8530400. doi:10.1074/jbc.270.50.29983.
  44. ↑ Berrevoets CA, Doesburg P, Steketee K, Trapman J, Brinkmann AO (August 1998). "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)". Molecular Endocrinology. 12 (8): 1172–83. PMID 9717843. doi:10.1210/me.12.8.1172.
  45. 1 2 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 (September 2004). "Distinct recognition modes of FXXLF and LXXLL motifs by the androgen receptor". Molecular Endocrinology. 18 (9): 2132–50. PMID 15178743. doi:10.1210/me.2003-0375.
  46. ↑ Kaku N, Matsuda K, Tsujimura A, Kawata M (August 2008). "Characterization of nuclear import of the domain-specific androgen receptor in association with the importin alpha/beta and Ran-guanosine 5'-triphosphate systems". Endocrinology. 149 (8): 3960–9. PMC 2488236 Freely accessible. PMID 18420738. doi:10.1210/en.2008-0137.
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  49. ↑ 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 (September 2014). "AR-V7 and resistance to enzalutamide and abiraterone in prostate cancer". The New England Journal of Medicine. 371 (11): 1028–38. PMC 4201502 Freely accessible. PMID 25184630. doi:10.1056/NEJMoa1315815.
  50. ↑ "Biomarker-Driven Therapy With Nivolumab and Ipilimumab in Treating Patients With Metastatic Hormone-Resistant Prostate Cancer Expressing AR-V7 - Full Text View - ClinicalTrials.gov". clinicaltrials.gov. Retrieved 2016-02-27.
  51. ↑ Helsen C, Van den Broeck T, Voet A, Prekovic S, Van Poppel H, Joniau S, Claessens F (August 2014). "Androgen receptor antagonists for prostate cancer therapy". Endocrine-Related Cancer. 21 (4): T105–18. PMID 24639562. doi:10.1530/ERC-13-0545.
  52. ↑ Gao W, Bohl CE, Dalton JT (September 2005). "Chemistry and structural biology of androgen receptor". Chemical Reviews. 105 (9): 3352–70. PMC 2096617 Freely accessible. PMID 16159155. doi:10.1021/cr020456u.
  53. 1 2 Lin HK, Yeh S, Kang HY, Chang C (June 2001). "Akt suppresses androgen-induced apoptosis by phosphorylating and inhibiting androgen receptor". Proceedings of the National Academy of Sciences of the United States of America. 98 (13): 7200–5. PMC 34646 Freely accessible. PMID 11404460. doi:10.1073/pnas.121173298.
  54. ↑ Shatkina L, Mink S, Rogatsch H, Klocker H, Langer G, Nestl A, Cato AC (October 2003). "The cochaperone Bag-1L enhances androgen receptor action via interaction with the NH2-terminal region of the receptor". Molecular and Cellular Biology. 23 (20): 7189–97. PMC 230325 Freely accessible. PMID 14517289. doi:10.1128/MCB.23.20.7189-7197.2003.
  55. ↑ Knee DA, Froesch BA, Nuber U, Takayama S, Reed JC (April 2001). "Structure-function analysis of Bag1 proteins. Effects on androgen receptor transcriptional activity". The Journal of Biological Chemistry. 276 (16): 12718–24. PMID 11278763. doi:10.1074/jbc.M010841200.
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  57. 1 2 3 4 Song LN, Coghlan M, Gelmann EP (January 2004). "Antiandrogen effects of mifepristone on coactivator and corepressor interactions with the androgen receptor". Molecular Endocrinology. 18 (1): 70–85. PMID 14593076. doi:10.1210/me.2003-0189.
  58. 1 2 3 Masiello D, Chen SY, Xu Y, Verhoeven MC, Choi E, Hollenberg AN, Balk SP (October 2004). "Recruitment of beta-catenin by wild-type or mutant androgen receptors correlates with ligand-stimulated growth of prostate cancer cells". Molecular Endocrinology. 18 (10): 2388–401. PMID 15256534. doi:10.1210/me.2003-0436.
  59. ↑ Yang F, Li X, Sharma M, Sasaki CY, Longo DL, Lim B, Sun Z (March 2002). "Linking beta-catenin to androgen-signaling pathway". The Journal of Biological Chemistry. 277 (13): 11336–44. PMID 11792709. doi:10.1074/jbc.M111962200.
  60. ↑ Amir AL, Barua M, McKnight NC, Cheng S, Yuan X, Balk SP (August 2003). "A direct beta-catenin-independent interaction between androgen receptor and T cell factor 4". The Journal of Biological Chemistry. 278 (33): 30828–34. PMID 12799378. doi:10.1074/jbc.M301208200.
  61. ↑ Mulholland DJ, Read JT, Rennie PS, Cox ME, Nelson CC (August 2003). "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". Oncogene. 22 (36): 5602–13. PMID 12944908. doi:10.1038/sj.onc.1206802.
  62. ↑ Pawlowski JE, Ertel JR, Allen MP, Xu M, Butler C, Wilson EM, Wierman ME (June 2002). "Liganded androgen receptor interaction with beta-catenin: nuclear co-localization and modulation of transcriptional activity in neuronal cells". The Journal of Biological Chemistry. 277 (23): 20702–10. PMID 11916967. doi:10.1074/jbc.M200545200.
  63. ↑ Park JJ, Irvine RA, Buchanan G, Koh SS, Park JM, Tilley WD, Stallcup MR, Press MF, Coetzee GA (November 2000). "Breast cancer susceptibility gene 1 (BRCAI) is a coactivator of the androgen receptor". Cancer Research. 60 (21): 5946–9. PMID 11085509.
  64. ↑ Yeh S, Hu YC, Rahman M, Lin HK, Hsu CL, Ting HJ, Kang HY, Chang C (October 2000). "Increase of androgen-induced cell death and androgen receptor transactivation by BRCA1 in prostate cancer cells". Proceedings of the National Academy of Sciences of the United States of America. 97 (21): 11256–61. PMC 17187 Freely accessible. PMID 11016951. doi:10.1073/pnas.190353897.
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