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

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. +1 more·1994·Nature

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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Crossref · 10.1038/370223a0

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19 of 19 references verified0 citation errors · 0 not checkable

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  • Once activated by the CaMK cascade, CaMKIV can phosphorylate CREB binding protein/p300 (CBP, gene name CREBBP).

    “Once activated by the CaMK cascade, CaMKIV is able to phosphorylate another important nuclear factor, CREB binding protein/p300 (CBP, gene name CREBBP) (Impey et al., 2002; Kwok et al., 1994).”

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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)
Venue
Nature
Published
1994-07
Volume
370
Issue
6486
Pages
223-226
ISSN
  • 0028-0836 (ISSN-L)
  • 1476-4687
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
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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