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Cited by 255Prostate Cancer Treatment and ResearchEstrogen and related hormone effectsGenomics and Chromatin Dynamics

CREB-binding protein in androgen receptor-mediated signaling

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Aarnisalo, Piia, Palvimo, Jorma J., Jänne, Olli A.·1998·Proceedings of the National Academy of Sciences
DOI 10.1073/pnas.95.5.2122PMC PMC19270
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Abstract

CREB-binding protein (CBP) is a transcriptional coregulator that interacts with different DNA binding proteins and components of the general transcription machinery. CBP enhanced androgen receptor (AR)-dependent transcription under transient transfection conditions in CV-1 cells. The ligand binding domain (LBD) and residues 38–296 of the N-terminal region of AR are not required because the activity of a receptor mutant devoid of these domains was augmented by coexpressed CBP. There is physical interaction between AR and CBP in vivo , as judged by coimmunoprecipitation experiments from cell extracts. Consistent with the role of CBP as a coactivator for AR, the 12S E1A adenoviral protein that inactivates CBP function strongly inhibited AR-dependent transactivation. Exogenous CBP was also capable of overcoming the inhibitory effect of AR on AP-1 activity and diminished the mutual transcriptional repression between AR and NF-κB (RelA). Collectively, these data imply that transcriptional interference between AR and AP-1 or NF-κB is mediated, at least in part, through competition for intracellular CBP and that this coactivator serves as an integrator between androgen-mediated and other signaling pathways.

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  • Animal steroid hormones exert their actions via binding to their intracellular nuclear receptors.

    “Animal steroid hormones are known exert their actions via binding to their intracellular nuclear receptors [7], for example, estrogen binds to its nuclear estrogen receptors ERα and ERβ [8], androgens bind to androgen receptors (AR) [9], and glucocorticoids bind to glucocorticoid receptors [10].”

    From G protein-coupled receptors function as cell membrane receptors for the steroid hormone 20-hydroxyecdysone (2020) · cites this paper as [9]

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Authors
Aarnisalo, P., Palvimo, J. J., & Jänne, O. A.
Affiliations
University of Helsinki (FI)
ORCID
Palvimo, Jorma J.
Venue
Proceedings of the National Academy of Sciences
Publisher
National Academy of Sciences
Published
1998-03-03
Volume
95
Issue
5
Pages
2122-2127
ISSN
  • 0027-8424 (ISSN-L)
  • 1091-6490
DOI
10.1073/pnas.95.5.2122
PMC
PMC19270
OpenAlex
W2023929246
Cited by
255
References
56
Citations by year
2026: 1 · 2025: 3 · 2024: 5 · 2023: 3 · 2022: 3 · 2021: 5 · 2020: 3 · 2019: 2 · 2018: 4 · 2017: 3 · 2016: 2 · 2015: 8 · 2014: 3 · 2013: 9 · 2012: 6
FWCI
23.10
Type
journal article
Language
en
Open access
Locations
  • Proceedings of the National Academy of Sciences (publishedVersion)
  • Europe PMC (PubMed Central) (publishedVersion)
  • PubMed Central (publishedVersion)
  • PubMed (publishedVersion)
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
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
Keywords
CREB-binding protein, androgen receptor, transcriptional coactivator, AP-1, NF-κB, RelA, transcriptional repression, transcriptional interference, E1A protein, ligand-binding domain, protein-protein interaction, signaling pathway integration
MeSH terms
Animals, Binding Sites, Cell Line, Humans, Kinetics, Nuclear Proteins, Receptors, Androgen, Receptors, Glucocorticoid, Transcription Factors, Transcription, Genetic, Transfection, Protein Engineering, Signal Transduction, Transcriptional Activation, Trans-Activators, Sequence Deletion, Transcription Factor AP-1, COS Cells, CREB-Binding Protein, Rats

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