ArticleMolecular and cellular biology1999
The androgen receptor amino-terminal domain plays a key role in p160 coactivator-stimulated gene transcription.
Article in Molecular and cellular biology, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 67 papers.
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Who cites it
67 citing papers in PubMed, 267 citations in OpenAlex.
- Coregulators determine androgen receptor activity in prostate cancer.Bioscience reports · 2025Review
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- N/C Interactions Are Dispensable for Normal In Vivo Functioning of the Androgen Receptor in Male Mice.Endocrinology · 2022Article
- The T850D Phosphomimetic Mutation in the Androgen Receptor Ligand Binding Domain Enhances Recruitment at Activation Function 2.International journal of molecular sciences · 2022Article
- The androgen receptor depends on ligand-binding domain dimerization for transcriptional activation.EMBO reports · 2021Article
- Roles of Key Epigenetic Regulators in the Gene Transcription and Progression of Prostate Cancer.Frontiers in molecular biosciences · 2021Review
- Clinical Actionability of the Genomic Landscape of Metastatic Castration Resistant Prostate Cancer.Cells · 2020Review
- Structural Insights of Transcriptionally Active, Full-Length Androgen Receptor Coactivator Complexes.Molecular cell · 2020Article
- Therapies Targeted to Androgen Receptor Signaling Axis in Prostate Cancer: Progress, Challenges, and Hope.Cancers · 2019Review
- AR variants: lost in translation to clinical practice?Nature reviews. Urology · 2019Article
- Development of selective androgen receptor modulators (SARMs).Molecular and cellular endocrinology · 2018Review
- Therapeutic Rationales, Progresses, Failures, and Future Directions for Advanced Prostate Cancer.International journal of biological sciences · 2016Review
- The promise and perils of HDAC inhibitors in neurodegeneration.Annals of clinical and translational neurology · 2015Review
- Coactivator recruitment of AhR/ARNT1.International journal of molecular sciences · 2014Review
- Coregulator control of androgen receptor action by a novel nuclear receptor-binding motif.The Journal of biological chemistry · 2014Article
- The transcription intermediary factor 1β coactivates the androgen receptor.Journal of endocrinological investigation · 2013Article
- Androgen receptor gene rearrangements: new perspectives on prostate cancer progression.Current drug targets · 2013Review
- The CXCL12/CXCR4 axis promotes ligand-independent activation of the androgen receptor.Molecular and cellular endocrinology · 2012Article
7 more citing papers are in PubMed but not listed here.
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Steroid receptors are conditional transcription factors that, upon binding to their response elements, regulate the expression of target genes via direct protein interactions with transcriptional coactivators. We have analyzed the functional interactions between the androgen receptor (AR) and 160-kDa nuclear receptor coactivators. Upon overexpression in mammalian cells, these coactivators enhance the transcriptional activity of both the amino-terminal domain (NTD) and the ligand-binding domain (LBD) of the AR. The coactivator activity for the LBD is strictly ligand-controlled and depends on the nature of the DNA-binding domain to which it is fused. We demonstrate that the NTD physically interacts with coactivators and with the LBD and that this interaction, like the functional interaction between the LBD and p160 coactivators, relies on the activation function 2 (AF2) core domain. The mutation of a highly conserved lysine residue in the predicted helix 3 of the LBD (K720A), however, blunts the functional interaction with coactivators but not with the NTD. Moreover, this mutation does not affect the transcriptional activity of the full-size AR. A mutation in the NTD of activation function AF1a (I182A/L183A), which dramatically impairs the activity of the AR, has no effect on the intrinsic transcriptional activity of the NTD but interferes with the cooperation between the NTD and the LBD. Finally, p160 proteins in which the three LXXLL motifs are mutated retain most of their coactivator activity for the full-size AR, although they are no longer functional for the isolated LBD. Together, these data suggest that in the native AR the efficient recruitment of coactivators requires a functional association of the NTD with the LBD and that the binding of coactivators occurs primarily through the NTD.
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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.