Contents

Search


androgen receptor; dihydrotestosterone receptor; nuclear receptor subfamily 3 group C member 4 (AR, DHTR, NR3C4)

Function: - nuclear hormone receptor - agonist binding is required for dimerization & binding to target DNA - transcription factor activity of the complex formed by ligand-activated AR & DNA is modulated by interactions with coactivator & corepressor proteins - cytoplasmic anchoring &/or assembly associated with heat shock proteins hsp70 & hsp90 & immunophilin p59FKBP - in the absence of ligand, steroid hormone receptors may be weakly associated with nuclear components - hormone binding greatly increases receptor affinity - the hormone-receptor complex appears to recognize discrete DNA sequences upstream of transcriptional start sites - transcriptional activity is enhanced by binding to RANBP9 - transcription activation is down-regulated by NR0B2 - activated, but not phosphorylated, by HIPK3 - binds DNA as a homodimer - part of a ternary complex containing AR, EFCAB6/DJBP & PARK7 - interacts with HIPK3 & NR0B2 in the presence of androgen - the ligand binding domain interacts with MYST2/HBO1 in the presence of dihydrotestosterone - interacts with EFCAB6/DJBP, PELP1, PQBP1, RANBP9, RBAK, SPDEF, SRA1, TGFB1I1, ZNF318 & RREB1 - interacts with ZMIZ1/ZIMP10 & ZMIZ2/ZMIP7 which both enhance its transactivation activity - interacts with SLC30A9 & RAD54L2/ARIP4 (putative) - interacts via the ligand-binding domain with LXXLL & FXXLF motifs from NCOA1, NCOA2, NCOA3, NCOA4 & MAGEA11 - The AR N-terminal poly-Gln region binds Ran resulting in enhancement of AR-mediated transactivation; Ran-binding decreases as the poly-Gln length increases - sumoylated on Lys-386 (major) & Lys-520 - phosphorylated in prostate cancer cells in response to several growth factors including EGF - phosphorylation is induced by c-Src kinase (CSK) - Tyr-534 is one of the major phosphorylation sites & an increase in phosphorylation & Src kinase activity is associated with prostate cancer progression Structure: - composed of three domains: a) modulating N-terminal domain b) DNA-binding domain c) C-terminal steroid-binding domain - in the presence of bound steroid, ligand-binding domain interacts with the N-terminal modulating domain, & thus activates AR transcription factor activity - interaction with RANBP9 is mediated by both the N-terminal domain & the DNA-binding domain - interaction with EFCAB6/DJBP is mediated by the DNA-binding domain - belongs to the nuclear hormone receptor family, NR3 subfamily - contains 1 nuclear receptor DNA-binding domain Compartment: nucleus Polymorphism: - the poly-Gln region of AR is highly polymorphic; the number of Gln varies in the population (17-26); a smaller size of the poly-Gln region may be associated with the development of prostate cancer - the poly-Gly region of AR is polymorphic & ranges from 24-31 gly; a poly-Gly region =< 23 may be associated with development of androgenetic alopecia Pathology: - genetic variation in AR can be responsible of androgenetic alopecia - defects in AR may play a role in prostate cancer a) metastatic prostate cancer b) level of tyrosine phosphorylation may serve as a diagnostic tool to predict patient outcome with hormone-ablation therapy c) inhibition of tyrosine phosphorylation may be an effective intervention target for hormone-refractory prostate cancer - defects in AR are the cause of a) androgen insensibility syndrome b) X-linked bulbospinal muscular atrophy c) infertility male syndrome d) Reifenstein syndrome (partial androgen insensitivity) Laboratory: - androgen receptor Ag in tissue

Related

androgen or anabolic steroid androgen receptor gene prostate cancer X-linked bulbospinal muscular atrophy (Kennedy's disease)

General

nuclear hormone receptor NR3 subfamily steroid receptor

Properties

SIZE: entity length = 919 aa MW = 99 kD COMPARTMENT: cell nucleus MOTIF: Modulating {1-558} MOTIF: glutamine-rich region {58-89} MOTIF: glutamine residue (SEVERAL) glutamine-rich region {58-78} MOTIF: glutamine residue (SEVERAL) glutamine-rich region {84-89} MOTIF: glutamine residue (SEVERAL) glutamine-rich region {193-197} MOTIF: glutamine residue (SEVERAL) Tyr phosphorylation site {Y223} Tyr phosphorylation site {Y267} Tyr phosphorylation site {Y307} Tyr phosphorylation site {Y346} Tyr phosphorylation site {Y357} Tyr phosphorylation site {Y362} Tyr phosphorylation site {Y363} proline-rich region SITE: 372-381 MOTIF: proline residue (SEVERAL) Tyr phosphorylation site {Y393} alanine-rich region {396-402} MOTIF: alanine residue (SEVERAL) glycine-rich region {449-472} Tyr phosphorylation site {Y534} Tyr phosphorylation site {Y551} DNA-binding motif SITE: 559-631 MOTIF: Zn finger C4-type SITE: 559-579 EFFECTOR-BOUND: Zn+2 HIPK3 interaction {571-661} MOTIF: Zn finger C4-type SITE: 595-619 EFFECTOR-BOUND: Zn+2 MYST2 interaction {624-919} MOTIF: binding site SITE: 690-919 FOR-BINDING-OF: ligand binding site SITE: 705-705 FOR-BINDING-OF: androgen lysine residue {720} binding site SITE: 752-752 FOR-BINDING-OF: androgen binding site SITE: 877-877 FOR-BINDING-OF: androgen glutamate residue {897} Tyr phosphorylation site {Y915}

Database Correlations

OMIM correlations MORBIDMAP 313700 UniProt P10275 PFAM correlations Kegg hsa:367

References

  1. Simental JA, Sar M, Lane MV, French FS, Wilson EM. Transcriptional activation and nuclear targeting signals of the human androgen receptor. J Biol Chem. 1991 Jan 5;266(1):510-8. PMID: 1985913
  2. Ross CA, McInnis MG, Margolis RL, Li SH. Genes with triplet repeats: candidate mediators of neuropsychiatric disorders. Trends Neurosci. 1993 Jul;16(7):254-60. Review. PMID: 7689767
  3. Androgen receptor gene mutations database http://www.mcgill.ca/androgendb/
  4. GeneReviews https://www.genecards.org/cgi-bin/carddisp.pl?gene=AR
  5. Wikipedia; Note: androgen receptor entry http://en.wikipedia.org/wiki/androgen_receptor
  6. UniProt :accession P10275