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 1e3g, 1gs4, 1i37, 1i38, 1r4i, 1t5z, 1t63, 1t65, 1t73, 1t74, 1t76, 1t79, 1t7f, 1t7m, 1t7r, 1t7t, 1xj7, 1xnn, 1xow, 1xq3, 1z95, 2am9, 2ama, 2amb, 2ao6, 2ax6, 2ax7, 2ax8, 2ax9, 2axa, 2ihq, 2nw4, 2oz7
Identifiers
Symbols	AR; AIS; DHTR; HUMARA; KD; NR3C4; SBMA; SMAX1; TFM
External IDs	OMIM: 313700 MGI: 88064 HomoloGene: 28 IUPHAR: NR3C4 GeneCards: AR Gene
Gene Ontology Molecular function • transcription factor activity • receptor activity • androgen receptor activity • steroid binding • androgen binding • zinc ion binding • lipid binding • sequence-specific DNA binding • metal ion binding • protein dimerization activity Cellular component • nucleus • cytoplasm Biological process • in utero embryonic development • transcription • regulation of transcription, DNA-dependent • transport • signal transduction • cell-cell signaling • sex differentiation • cell proliferation • male gonad development • cell growth • male somatic sex determination • androgen receptor signaling pathway • prostate gland development Sources: Amigo / QuickGO
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: 66.68 – 66.87 Mb	Chr X: 94.35 – 94.52 Mb
PubMed search	[1]	[2]

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
Available protein structures: Pfam structures PDB RCSB PDB; PDBe PDBsum structure summary

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 of 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]

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.^[16] 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 insulin-like growth factor I (IGF-1).^[17] 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.^[18]

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][19] 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.^[20][21]

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).^[22] The androgen receptor seems to affect neuron physiology and is defective in Kennedy disease.^[23][24] In addition, point mutations and trinucleotide repeat polymorphisms has been linked to a number of additional disorders.^[25]

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:^[26]

• AR-A - 87 kDa - N-terminus truncated (lacks the first 187 amino acids), which results from in vitro proteolysis.^[27]
• 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 domains labeled A through F:^[28]

• A/B) - N-terminal regulatory domain contains:^[29]
  • activation function 1 (AF-1) between residues 101 and 370 required for full ligand activated transcriptional activity
  • activation function 5 (AF-5) between residues 360-485 is responsible for the constitutive activity (activity without bound ligand)
  • dimerization surface involving residues 1-36 (containing the FXXLF motif where F = phenylalanine, L = leucine, and X = any amino acid residue) and 370-494, both of which interact with the LBD in an intramolecular^[30][31][32] head-to-tail interaction^[33][34][35]
• C) - DNA binding domain (DBD)
• D) - Hinge region - flexible region that connects the DBD with the LBD; along with the DBD, contains a ligand dependent nuclear localization signal^[36]
• 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 intramolecularly or coactivator proteins (containing the LXXLL or preferably FXXFL motifs)^[35]
  • A ligand dependent nuclear export signal^[37]
• F) - C-terminal domain

Interactions

Androgen receptor has been shown to interact with:

• AKT1,^[38]
• BAG1,^[39][40][41]
• Beta-catenin,^{[42][43][44][45][46][47]}
• BRCA1,^[48][49]
• C-jun,^[50]
• Calmodulin 1,^[51]
• Caveolin 1,^[52]
• CDK9,^[53]
• COX5B,^[54]
• CREB-binding protein,^{[55][56][57][58]}
• Cyclin D1,^[59][60]
• Cyclin-dependent kinase 7,^[61]
• Death associated protein 6,^[62]
• Deleted in Colorectal Cancer,^[63]
• EFCAB6,^[64]
• Epidermal growth factor receptor,^[65][66]
• FOXO1,^[67]
• GAPDH,^[68]
• Gelsolin,^[69]
• GNB2L1,^[70]
• GSK3B,^[71]
• HDAC1,^[72]
• HSP90AA1,^[73][74]
• HTATIP,^[72]
• MAGEA11,^[75][76]
• MED1,^[77]
• MYST2,^[78]
• NCOA1,^[43][79][80]
• NCOA2,^{[42][57][75][81][82]}
• NCOA3,^[81][83][84]
• NCOA4,^{[38][82][85][86][87][88][89][90][91]}
• NCOA6,^[92]
• NCOR2,^[42][93][94]
• NONO,^[57]
• PA2G4,^[95]
• PAK6,^[96][97]
• PATZ1,^[98]
• PIAS2,^[99][100]
• PRPF6,^[101]
• PTEN,^[102]
• RAD9A,^[103]
• RANBP9,^[104]
• RCHY1,^[105]
• Retinoblastoma protein,^[106][107]
• RNF14,^{[82][85][108][109]}
• RNF4,^{[98][110][111]}
• SART3,^[112]
• SMAD3,^{[113][114][115]}
• Small heterodimer partner,^[116]
• Src,^{[102][117][118]}
• SRY,^[119]
• STAT3,^[120][121]
• SVIL,^[122]
• Testicular receptor 2,^[123]
• Testicular receptor 4,^[124]
• TGFB1I1,^[85][125]
• TMF1,^[126]
• TRIM68,^[127]
• UBE2I,^{[42][43][128][129][130][131]}
• UXT,^[132] and
• ZMIZ1.^[133]

See also

• Androgen
• Discovery and development of antiandrogens

References

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External links

• GeneReviews/NCBI/NIH/UW entry on Androgen Insensitivity Syndrome
• OMIM entries on Androgen Insensitivity Syndrome
• GeneReviews/NIH/NCBI/UW entry on Spinal and Bulbar Muscular Atrophy, Kennedy's Disease, SBMA, X-Linked Spinal and Bulbar Muscular Atrophy
• OMIM entries on Spinal and Bulbar Muscular Atrophy, Kennedy's Disease, SBMA, X-Linked Spinal and Bulbar Muscular Atrophy
• MeSH Androgen+Receptors
• Brinkmann AO. "Androgen physiology: receptor and metabolic disorders". In Robert McLachlan, editor. Endocrinology of Male Reproduction. Endotext.org. http://www.endotext.org/male/male3/male3.pdf. Retrieved 2008-04-29. 
• Gottlieb B (2007-07-24). "The Androgen Receptor Gene Mutations Database Server". McGill University. http://androgendb.mcgill.ca/. Retrieved 2008-04-29. 
• Thompson J (2006-09-30). "Molecular Mechanisms of Androgen Receptor Interactions". Helsinki University Biomedical Dissertations No. 80. University of Helsinki. http://ethesis.helsinki.fi/julkaisut/laa/biola/vk/thompson/molecula.pdf. Retrieved 2008-04-29.