The DOI matches its Crossref record; 56 of the 56 references it cites were found in a registry or an index.
CREB-binding protein in androgen receptor-mediated signaling
Open accessAbstract
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 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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Metadata
- 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
- 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
- green
- europepmc.org
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Prostate Cancer Treatment and Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Endocrinology › 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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