ArticleScientific reports2019
Ligand induced dissociation of the AR homodimer precedes AR monomer translocation to the nucleus.
Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 16 citations in OpenAlex.
- Targeted proteomics for the detection of androgen receptor variants in preclinical models of castration-resistant prostate cancer.Clinical proteomics · 2026Article
- The Ser434PheThe application of clinical genetics · 2024Article
- Ser815 Phosphorylation stabilizes the androgen receptor homodimer and stimulates ER-stress induced cell death.Biochemical and biophysical research communications · 2023Article
- Non-small molecule PROTACs (NSM-PROTACs): Protein degradation kaleidoscope.Acta pharmaceutica Sinica. B · 2022Review
- FKBP51 and FKBP52 regulate androgen receptor dimerization and proliferation in prostate cancer cells.Molecular oncology · 2022Article
- Combined FCS and PCH Analysis to Quantify Protein Dimerization in Living Cells.International journal of molecular sciences · 2021Article
- Functional Effects In Silico Prediction for Androgen Receptor Ligand-Binding Domain Novel I836S Mutation.Life (Basel, Switzerland) · 2021Article
- Novel missense mutation in ligand binding domain of AR gene identified in patient with androgen insensitivity syndrome from Ukraine.Clinical case reports · 2021Article
- Nuclear receptor phosphorylation in xenobiotic signal transduction.The Journal of biological chemistry · 2020Review
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
The androgen receptor (AR) regulates male sexual development. We have now investigated AR homodimerization, hormone-dependent monomerization and nuclear translocation in PC-3 and COS-1 cells, by utilizing mutations associated with the androgen insensitivity syndrome: Pro767Ala, Phe765Leu, Met743Val and Trp742Arg. AR wild type (WT) was expressed as a homodimer in the cytoplasm, while none of these mutants formed homodimers. Unlike AR WT which responded to 1 nM dihydrotestosterone (DHT) to dissociate and translocate into the nucleus, AR Pro767Ala and Phe765Leu mutants remain as the monomer in the cytoplasm. In the crystal structure of the AR LBD homodimer, Pro767 and Phe765 reside closely on a loop that constitutes the dimer interface; their sidechains interact with the Pro767 of the other monomer and with the DHT molecule in the ligand-binding pocket. These observations place Phe765 at a position to facilitate DHT binding to Pro767 and lead to dissociation of the AR homodimer in the cytoplasm. This Pro-Phe Met relay may constitute a structural switch that mediates androgen signaling and is conserved in other steroid hormone receptors.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.