Stepwise androgen receptor dimerization

van Royen, Martin E.; van Cappellen, Wiggert A.; de Vos, Carola; Houtsmuller, Adriaan B.; Trapman, Jan

doi:10.1242/jcs.096792

Cited by 144Prostate Cancer Treatment and ResearchEstrogen and related hormone effectsSperm and Testicular Function

Stepwise androgen receptor dimerization

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van Royen, Martin E., van Cappellen, Wiggert A., de Vos, Carola, Houtsmuller, Adriaan B., Trapman, Jan·2012·Journal of Cell Science

DOI 10.1242/jcs.096792

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Abstract

Androgen-regulated gene expression is a highly coordinated dynamic process mediated by androgen receptor (AR) ligand binding and DNA binding, and by specific AR protein-protein interactions. The latter include DNA-binding domain (D-box) interactions in AR homodimers, and the interaction of the FQNLF motif in the AR N-terminal domain and the coactivator groove in the ligand-binding domain (N/C interaction). We have studied these interactions in AR homodimerization using quantitative imaging techniques. We found that the initial cytoplasmic intramolecular AR N/C interaction after ligand binding is followed by a D-box-dimerization-dependent transition to intermolecular N/C interaction in a proportion of nuclear ARs. The consecutive steps leading to homodimerization are initiated prior to DNA binding. Our data indicate the presence of nuclear pools of both AR homodimers and monomers. On the basis of AR-regulated reporter assays we propose specificity in regulation of gene expression by AR homodimers and monomers mediated by AR domain interactions. Moreover, our findings elucidate important steps in the spatiotemporal organization of AR intra- and inter-molecular interactions.

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The NTDs surround the LBDs to make both intra- and inter-molecular N/C interactions.
“Consistent with previous reports (Langley et al., 1998; Langley et al., 1995; van Royen et al., 2012), the NTDs also surround the LBDs to make both intra- and inter-molecular N/C interactions.”
From Structural Insights of Transcriptionally Active, Full-Length Androgen Receptor Coactivator Complexes (2020) · cites this paper as van Royen et al., 2012
An androgen-induced inter-molecular N/C interaction was observed, supporting an anti-parallel dimerization model.
“On the other hand, an androgen-induced inter-molecular N/C interaction was observed, supporting an anti-parallel dimerization model (Langley et al., 1998; Langley et al., 1995; van Royen et al., 2012).”
From Structural Insights of Transcriptionally Active, Full-Length Androgen Receptor Coactivator Complexes (2020) · cites this paper as van Royen et al., 2012

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Authors: van Royen, M. E., van Cappellen, W. A., de Vos, C., Houtsmuller, A. B., & Trapman, J.
Affiliations: Erasmus MC (NL)
Corresponding author: Trapman, Jan
ORCID: Houtsmuller, Adriaan B.
Venue: Journal of Cell Science
Publisher: The Company of Biologists
Published: 2012-01-01
Volume: 125
Issue: Pt 8
Pages: 1970-9
ISSN: 0021-9533 (ISSN-L)
1477-9137
DOI: 10.1242/jcs.096792
OpenAlex: W2133336912
Cited by: 143
References: 46
Citations by year: 2026: 1 · 2025: 5 · 2024: 13 · 2023: 11 · 2022: 11 · 2021: 17 · 2020: 10 · 2019: 13 · 2018: 8 · 2017: 11 · 2016: 9 · 2015: 9 · 2014: 13 · 2013: 8 · 2012: 4
FWCI: 8.77
Type: journal article
Language: en
Open access: green
hdl.handle.net
Licence: other-oa
Locations: Journal of Cell Science (publishedVersion)
PubMed (publishedVersion)
EUR Research Repository (Erasmus University Rotterdam) (publishedVersion)
EUR Research Repository (Erasmus University Rotterdam) (submittedVersion)
RePub (Erasmus University Rotterdam) (submittedVersion, other-oa)
Topics: Health Sciences › Medicine › Pulmonary and Respiratory Medicine › Prostate Cancer Treatment and Research
Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Estrogen and related hormone effects
Health Sciences › Medicine › Reproductive Medicine › Sperm and Testicular Function
Keywords: androgen receptor, homodimerization, protein-protein interaction, DNA-binding domain, ligand binding, receptor monomer, gene expression regulation, nuclear receptor signaling, quantitative imaging
MeSH terms: Amino Acid Sequence, Androgens, Cell Nucleus, Cytoplasm, Gene Expression Regulation, Humans, Ligands, Protein Binding, Receptors, Androgen, Protein Structure, Tertiary, Dimerization, Amino Acid Motifs

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Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

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Stepwise androgen receptor dimerization

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