A CBP Integrator Complex Mediates Transcriptional Activation and AP-1 Inhibition by Nuclear Receptors
Open accessAbstract
Nuclear receptors regulate gene expression by direct activation of target genes and inhibition of AP-1. Here we report that, unexpectedly, activation by nuclear receptors requires the actions of CREB-binding protein (CBP) and that inhibition of AP-1 activity is the apparent result of competition for limiting amounts of CBP/p300 in cells. Utilizing distinct domains, CBP directly interacts with the ligand-binding domain of multiple nuclear receptors and with the p160 nuclear receptor coactivators, which upon cloning have proven to be variants of the SRC-1 protein. Because CBP represents a common factor, required in addition to distinct coactivators for function of nuclear receptors, CREB, and AP-1, we suggest that CBP/p300 serves as an integrator of multiple signal transduction pathways within the nucleus.
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Kamei et al. proposed the term integrator for CBP, suggesting it integrates cellular signals that assemble transcription factors and coactivators and converts them into transcriptional activation.
“Kamei et al. have coined the term “integrator,” postulating that CBP integrates diverse signals within the cell which culminate in the assembly of transcription factors and coactivators and translates them into transcriptional activation (26).”
From Multiple Functional Domains of AML1: PU.1 and C/EBPα Synergize with Different Regions of AML1 (1998) · cites this paper as [26]
CBP is a ubiquitous adapter protein that links transcription factors to the basal transcription machinery and is thought to stimulate transcription through contact with RNA polymerase II and histone acetylation.
“CBP is a ubiquitous adapter protein that mediates contacts between transcription factors and the basal transcription machinery (1,26,33) and is thought to stimulate transcription both by physical contact with the RNA polymerase II complex and through intrinsic histone acetylation activity (4, 33, 52).”
From Multiple Functional Domains of AML1: PU.1 and C/EBPα Synergize with Different Regions of AML1 (1998) · cites this paper as [26]
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- Authors
- Kamei, Y., Xu, L., Heinzel, T., Torchia, J., Kurokawa, R., Gloss, B., Lin, S.-C., Heyman, R. A., Rose, D. W., Glass, C. K., & Rosenfeld, M. G.
- Affiliations
- Howard Hughes Medical Institute (US)
- University of California San Diego (US)
- Ligand Pharmaceuticals (United States) (US)
- Corresponding author
- Rosenfeld, Michael G
- ORCID
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 1996-05
- Volume
- 85
- Issue
- 3
- Pages
- 403-414
- ISSN
- 0092-8674 (ISSN-L)
- OpenAlex
- W2143241514
- Cited by
- 2,150
- References
- 64
- Citations by year
- 2026: 8 · 2025: 6 · 2024: 8 · 2023: 9 · 2022: 12 · 2021: 17 · 2020: 12 · 2019: 16 · 2018: 21 · 2017: 17 · 2016: 22 · 2015: 20 · 2014: 26 · 2013: 31 · 2012: 18
- FWCI
- 145.30
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Cell (publishedVersion)
- PubMed (publishedVersion)
- National University of Singapore (submittedVersion)
- eScholarship (California Digital Library) (submittedVersion)
- Topics
- 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
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Nuclear Receptors and Signaling
- Keywords
- CREB-binding protein, P300, nuclear receptors, transcriptional activation, p160 coactivators, SRC-1, ligand-binding domain, CREB
- MeSH terms
- Animals, Base Sequence, Binding Sites, Binding, Competitive, Cloning, Molecular, Fibroblasts, Gene Expression Regulation, Ligands, Molecular Sequence Data, Molecular Weight, Nuclear Proteins, Transcription Factors, Transcriptional Activation, Trans-Activators, Conserved Sequence, Sequence Homology, Amino Acid, DNA, Complementary, Receptors, Cytoplasmic and Nuclear, Transcription Factor AP-1, CREB-Binding Protein, Rats, Histone Acetyltransferases, Nuclear Receptor Coactivator 1
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