Androgen receptor

Androgen receptor

Structure of the ligand binding domain of the androgen receptor (rainbow cartoon) complexed with testosterone (white sticks).[1]
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
Symbols AR ; AIS; AR8; DHTR; HUMARA; HYSP1; KD; NR3C4; SBMA; SMAX1; TFM
External IDs OMIM: 313700 MGI: 88064 HomoloGene: 28 IUPHAR: 628 ChEMBL: 1871 GeneCards: AR Gene
RNA expression pattern
More reference expression data
Orthologs
Species Human Mouse
Entrez 367 11835
Ensembl ENSG00000169083 ENSMUSG00000046532
UniProt P10275 P19091
RefSeq (mRNA) NM_000044 NM_013476
RefSeq (protein) NP_000035 NP_038504
Location (UCSC) Chr X:
67.54 – 67.73 Mb		 Chr X:
98.15 – 98.32 Mb
PubMed search
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.[2][3][4][5]

The androgen receptor (AR), also known as NR3C4 (nuclear receptor subfamily 3, group C, member 4), is a type of nuclear receptor[6] that is activated by binding either of the androgenic hormones, testosterone, or dihydrotestosterone [7] 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.[8][9]

The main function of the androgen receptor is as a DNA-binding transcription factor that regulates gene expression;[10] however, the androgen receptor has other functions as well.[11] 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.[12] 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.[13] 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.[14]

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.[15]

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.[16]

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.[17] 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).[18] 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.[19]

Androgen receptor is modified by acetylation, which directly promotes contact independent growth of prostate cancer cells.[20]

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.[11][21] 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.[22][23]

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).[24] The androgen receptor seems to affect neuron physiology and is defective in Kennedy's disease.[25][26] In addition, point mutations and trinucleotide repeat polymorphisms has been linked to a number of additional disorders.[27]

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:[28]

Domains

Like other nuclear receptors, the androgen receptor is modular in structure and is composed of the following functional domains labeled A through F:[30]

Interactions

Androgen receptor has been shown to interact with:

See also

References

  1. ↑ PDB: 2AM9​; Pereira de Jésus-Tran K, Côté PL, Cantin L, Blanchet J, Labrie F, Breton R (May 2006). "Comparison of crystal structures of human androgen receptor ligand-binding domain complexed with various agonists reveals molecular determinants responsible for binding affinity". Protein Sci. 15 (5): 987–99. doi:10.1110/ps.051905906. PMC 2242507. PMID 16641486.
  2. ↑ Quigley CA, De Bellis A, Marschke KB, el-Awady MK, Wilson EM, French FS (June 1995). "Androgen receptor defects: historical, clinical, and molecular perspectives". Endocr. Rev. 16 (3): 271–321. doi:10.1210/edrv-16-3-271. PMID 7671849.
  3. ↑ Gottlieb B, Lombroso R, Beitel LK, Trifiro MA (January 2005). "Molecular pathology of the androgen receptor in male (in)fertility". Reprod. Biomed. Online 10 (1): 42–8. doi:10.1016/S1472-6483(10)60802-4. PMID 15705293.
  4. ↑ Choong CS, Wilson EM (December 1998). "Trinucleotide repeats in the human androgen receptor: a molecular basis for disease". J. Mol. Endocrinol. 21 (3): 235–57. doi:10.1677/jme.0.0210235. PMID 9845666.
  5. ↑ Meehan KL, Sadar MD (May 2003). "Androgens and androgen receptor in prostate and ovarian malignancies". Front. Biosci. 8 (1-3): d780–800. doi:10.2741/1063. PMID 12700055.
  6. ↑ 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". Pharmacol. Rev. 58 (4): 782–97. doi:10.1124/pr.58.4.9. PMID 17132855.
  7. ↑ Roy AK, Lavrovsky Y, Song CS, Chen S, Jung MH, Velu NK, Bi BY, Chatterjee B (1999). "Regulation of androgen action". Vitam. Horm. Vitamins & Hormones 55: 309–52. doi:10.1016/S0083-6729(08)60938-3. ISBN 978-0-12-709855-5. PMID 9949684.
  8. ↑ Bardin CW, Brown T, Isomaa VV, Jänne OA (1983). "Progestins can mimic, inhibit and potentiate the actions of androgens". Pharmacol. Ther. 23 (3): 443–59. doi:10.1016/0163-7258(83)90023-2. PMID 6371845.
  9. ↑ Raudrant D, Rabe T (2003). "Progestogens with antiandrogenic properties". Drugs 63 (5): 463–92. doi:10.2165/00003495-200363050-00003. PMID 12600226.
  10. ↑ Mooradian AD, Morley JE, Korenman SG (1987). "Biological actions of androgens". Endocr. Rev. 8 (1): 1–28. doi:10.1210/edrv-8-1-1. PMID 3549275.
  11. 1 2 Heinlein CA, Chang C (2002). "The roles of androgen receptors and androgen-binding proteins in nongenomic androgen actions". Mol. Endocrinol. 16 (10): 2181–7. doi:10.1210/me.2002-0070. PMID 12351684.
  12. ↑ Davison SL, Bell R (April 2006). "Androgen physiology". Semin. Reprod. Med. 24 (2): 71–7. doi:10.1055/s-2006-939565. PMID 16633980.
  13. ↑ Sinisi AA, Pasquali D, Notaro A, Bellastella A (2003). "Sexual differentiation". J. Endocrinol. Invest. 26 (3 Suppl): 23–8. PMID 12834017.
  14. ↑ Frank GR (September 2003). "Role of estrogen and androgen in pubertal skeletal physiology". Med. Pediatr. Oncol. 41 (3): 217–21. doi:10.1002/mpo.10340. PMID 12868122.
  15. ↑ Walters KA, Simanainen U, Handelsman DJ (March 2010). "Molecular insights into androgen actions in male and female reproductive function from androgen receptor knockout models". Hum Reprod Update 16 (5): 543–58. doi:10.1093/humupd/dmq003. PMID 20231167.
  16. ↑ Sinnesael M., Claessens F., Laurent M., Dubois V., Boonen S., Deboel L., Vanderschueren D. (Dec 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. doi:10.1002/jbmr.1713. PMID 22836391.
  17. ↑ Heemers HV, Tindall DJ (December 2007). "Androgen receptor (AR) coregulators: a diversity of functions converging on and regulating the AR transcriptional complex". Endocr. Rev. 28 (7): 778–808. doi:10.1210/er.2007-0019. PMID 17940184.
  18. ↑ Pandini G, Mineo R, Frasca F, Roberts CT Jr, Marcelli M, Vigneri R, Belfiore A (March 2005). "Androgens up-regulate the insulin-like growth factor-I receptor in prostate cancer cells". Cancer Res. 65 (5): 1849–57. doi:10.1158/0008-5472.CAN-04-1837. PMID 15753383.
  19. ↑ Vlahopoulos S, Zimmer WE, Jenster G, Belaguli NS, Balk SP, Brinkmann AO, Lanz RB, Zoumpourlis VC, Schwartz RJ (2005). "Recruitment of the androgen receptor via serum response factor facilitates expression of a myogenic gene". J. Biol. Chem. 280 (9): 7786–92. doi:10.1074/jbc.M413992200. PMID 15623502.
  20. 1 2 Fu M, Wang C, Reutens AT, Wang J, Angeletti RH, Siconolfi-Baez L, Ogryzko V, Avantaggiati ML, Pestell RG (July 2000). "p300 and p300/cAMP-response element-binding protein-associated factor acetylate the androgen receptor at sites governing hormone-dependent transactivation". J. Biol. Chem. 275 (27): 20853–60. doi:10.1074/jbc.M000660200. PMID 10779504.
  21. ↑ Fix C, Jordan C, Cano P, Walker WH (2004). "Testosterone activates mitogen-activated protein kinase and the cAMP response element binding protein transcription factor in Sertoli cells". Proc Natl Acad Sci USA 101 (30): 10919–24. doi:10.1073/pnas.0404278101. PMC 503720. PMID 15263086.
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  23. ↑ 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 (1988). "Cloning, structure and expression of a cDNA encoding the human androgen receptor". Biochem. Biophys. Res. Commun. 153 (1): 241–8. doi:10.1016/S0006-291X(88)81214-2. PMID 3377788.
  24. ↑ Brown TR (1995). "Human androgen insensitivity syndrome" (abstract). J. Androl. 16 (4): 299–303. PMID 8537246.
  25. ↑ Kennedy WR, Alter M, Sung JH (1968). "Progressive proximal spinal and bulbar muscular atrophy of late onset. A sex-linked recessive trait". Neurology 18 (7): 671–80. doi:10.1212/WNL.18.7.671. PMID 4233749.
  26. ↑ Yu Z, Dadgar N, Albertelli M, Gruis K, Jordan C, Robins DM, Lieberman AP (2006). "Androgen-dependent pathology demonstrates myopathic contribution to the Kennedy disease phenotype in a mouse knock-in model". J. Clin. Invest. 116 (10): 2663–72. doi:10.1172/JCI28773. PMC 1564432. PMID 16981011.
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  28. ↑ Wilson CM, McPhaul MJ (1994). "A and B forms of the androgen receptor are present in human genital skin fibroblasts". Proc. Natl. Acad. Sci. U.S.A. 91 (4): 1234–8. doi:10.1073/pnas.91.4.1234. PMC 43131. PMID 8108393.
  29. ↑ Gregory CW, He B, Wilson EM. (2001). "The putative androgen receptor-A form results from in vitro proteolysis". J Mol Endocrinol 27 (3): 309–19. doi:10.1677/jme.0.0270309. PMID 11719283.
  30. ↑ 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, Voorhorst MM, Mulder E, Trapman J (1989). "Structure and function of the androgen receptor". Urol. Res. 17 (2): 87–93. doi:10.1007/BF00262026. PMID 2734982.
  31. ↑ Jenster G, van der Korput HA, Trapman J, Brinkmann AO (1995). "Identification of two transcription activation units in the N-terminal domain of the human androgen receptor". J. Biol. Chem. 270 (13): 7341–6. doi:10.1074/jbc.270.13.7341. PMID 7706276.
  32. ↑ Schaufele F, Carbonell X, Guerbadot M, Borngraeber S, Chapman MS, Ma AA, Miner JN, Diamond MI (July 2005). "The structural basis of androgen receptor activation: Intramolecular and intermolecular amino–carboxy interactions". Proc. Natl. Acad. Sci. U.S.A. 102 (28): 9802–7. doi:10.1073/pnas.0408819102. PMC 1168953. PMID 15994236.
  33. ↑ Klokk TI, Kurys P, Elbi C, Nagaich AK, Hendarwanto A, Slagsvold T, Chang CY, Hager GL, Saatcioglu F (March 2007). "Ligand-Specific Dynamics of the Androgen Receptor at Its Response Element in Living Cells". Mol. Cell. Biol. 27 (5): 1823–43. doi:10.1128/MCB.01297-06. PMC 1820481. PMID 17189428.
  34. ↑ van Royen ME, Cunha SM, Brink MC, Mattern KA, Nigg AL, Dubbink HJ, Verschure PJ, Trapman J, Houtsmuller AB (April 2007). "Compartmentalization of androgen receptor protein–protein interactions in living cells". J. Cell Biol. 177 (1): 63–72. doi:10.1083/jcb.200609178. PMC 2064112. PMID 17420290.
  35. ↑ Langley E, Zhou ZX, Wilson EM (1995). "Evidence for an anti-parallel orientation of the ligand-activated human androgen receptor dimer". J. Biol. Chem. 270 (50): 29983–90. doi:10.1074/jbc.270.50.29983. PMID 8530400.
  36. ↑ Berrevoets CA, Doesburg P, Steketee K, Trapman J, Brinkmann AO (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)". Mol. Endocrinol. 12 (8): 1172–83. doi:10.1210/me.12.8.1172. PMID 9717843.
  37. 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 (2004). "Distinct recognition modes of FXXLF and LXXLL motifs by the androgen receptor". Mol. Endocrinol. 18 (9): 2132–50. doi:10.1210/me.2003-0375. PMID 15178743.
  38. ↑ Kaku N, Matsuda KI, Tsujimura A, Kawata M (April 2008). "Characterization of Nuclear Import of the Domain-Specific Androgen Receptor in Association with the Importin α/β and Ran-Guanosine 5′-Triphosphate Systems". Endocrinology 149 (8): 3960–9. doi:10.1210/en.2008-0137. PMC 2488236. PMID 18420738.
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  56. ↑ Beauchemin AM, Gottlieb B, Beitel LK, Elhaji YA, Pinsky L, Trifiro MA (2001). "Cytochrome c oxidase subunit Vb interacts with human androgen receptor: a potential mechanism for neurotoxicity in spinobulbar muscular atrophy". Brain Res. Bull. 56 (3–4): 285–97. doi:10.1016/S0361-9230(01)00583-4. PMID 11719263.
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  59. 1 2 3 Ishitani K, Yoshida T, Kitagawa H, Ohta H, Nozawa S, Kato S (July 2003). "p54nrb acts as a transcriptional coactivator for activation function 1 of the human androgen receptor". Biochem. Biophys. Res. Commun. 306 (3): 660–5. doi:10.1016/S0006-291X(03)01021-0. PMID 12810069.
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