Cited by 1,443Genomics and Chromatin DynamicsProtein Kinase Regulation and GTPase SignalingSignaling Pathways in Disease

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Nuclear protein CBP is a coactivator for the transcription factor CREB

Kwok, Roland P. S., Lundblad, James R., Chrivia, John C., Richards, Jane P., Bächinger, Hans Peter, Brennan, Richard G., Roberts, Stefan G. E., Green, Michael R., Goodman, Richard H.·1994·Nature

DOI 10.1038/370223a0

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Abstract

The transcription factor CREB binds to a DNA element known as the cAMP-regulated enhancer (CRE). CREB is activated through phosphorylation by protein kinase A (PKA), but precisely how phosphorylation stimulates CREB function is unknown. One model is that phosphorylation may allow the recruitment of coactivators which then interact with basal transcription factors. We have previously identified a nuclear protein of M(r)265K, CBP, that binds specifically to the PKA-phosphorylated form of CREB. We have used fluorescence anisotropy measurements to define the equilibrium binding parameters of the phosphoCREB:CBP interaction and report here that CBP can activate transcription through a region in its carboxy terminus. The activation domain of CBP interacts with the basal transcription factor TFIIB through a domain that is conserved in the yeast coactivator ADA-1 (ref. 8). Consistent with its role as a coactivator, CBP augments the activity of phosphorylated CREB to activate transcription of cAMP-responsive genes.

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The TRAP220 component of a thyroid hormone receptor- associated protein (TRAP) coactivator complex interacts directly with nuclear receptors in a ligand-dependent fashion
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Everything you have ever wanted to know about Yin Yang 1......
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Authors: Kwok, R. P. S., Lundblad, J. R., Chrivia, J. C., Richards, J. P., Bächinger, H. P., Brennan, R. G., Roberts, S. G. E., Green, M. R., & Goodman, R. H.
Affiliations: Oregon Health & Science University (US)
ORCID: Brennan, Richard G.
Roberts, Stefan G. E.
Green, Michael R.
Venue: Nature
Publisher: Springer Science and Business Media LLC
Published: 1994-07
Volume: 370
Issue: 6486
Pages: 223-226
ISSN: 0028-0836 (ISSN-L)
1476-4687
DOI: 10.1038/370223a0
OpenAlex: W1964337986
Cited by: 1,443
References: 19
Citations by year: 2026: 3 · 2025: 10 · 2024: 15 · 2023: 10 · 2022: 16 · 2021: 15 · 2020: 15 · 2019: 7 · 2018: 18 · 2017: 21 · 2016: 22 · 2015: 13 · 2014: 21 · 2013: 29 · 2012: 36
FWCI: 30.10
Type: journal article
Language: en
Open access: closed
Licence: www.springer.com/tdm (tdm)
Locations: Nature (publishedVersion)
PubMed (publishedVersion)
Research Explorer (The University of Manchester) (submittedVersion)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Signaling Pathways in Disease
Keywords: CBP, CREB, transcriptional coactivator, transcriptional activation, protein kinase A phosphorylation, TFIIB, protein-protein interaction
MeSH terms: Animals, Base Sequence, Binding Sites, DNA, Enhancer Elements, Genetic, Fluorescence Polarization, Molecular Sequence Data, Nuclear Proteins, Phosphorylation, Protein Binding, Recombinant Fusion Proteins, Somatostatin, Transcription Factors, Transcription, Genetic, Tumor Cells, Cultured, Trans-Activators, Zinc Fingers, PC12 Cells, Cyclic AMP Response Element-Binding Protein, Transcription Factor TFIIB, CREB-Binding Protein, Mice

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Nuclear protein CBP is a coactivator for the transcription factor CREB

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