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Related Experiment Videos

Phosphorylated CREB binds specifically to the nuclear protein CBP

J C Chrivia1, R P Kwok, N Lamb

  • 1Vollum Institute, Oregon Health Sciences University, Portland 97201.

Nature
|October 28, 1993
PubMed
Summary

Cyclic AMP-regulated gene expression involves CREB binding protein (CBP). Phosphorylated CREB binds to CBP, which acts as a transcriptional activator, mediating cAMP-regulated gene expression.

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Area of Science:

  • Molecular Biology
  • Gene Regulation
  • Signal Transduction

Background:

  • Cyclic AMP (cAMP)-regulated gene expression often utilizes cAMP-response elements (CREs).
  • CREB (cAMP-response element-binding protein) is a key transcription factor activated by protein kinase A-mediated phosphorylation.
  • Phosphorylated CREB interacts with general transcription factors or co-activators to modulate gene expression.

Purpose of the Study:

  • To identify nuclear proteins that interact with phosphorylated CREB.
  • To characterize the function of CREB-binding protein (CBP) in cAMP-regulated transcription.

Main Methods:

  • Co-immunoprecipitation to identify CREB-binding proteins.
  • Expression of chimeric proteins to assess transcriptional activity.

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Main Results:

  • A 265 kDa nuclear protein, termed CBP (CREB-binding protein), was identified as a specific binding partner for phosphorylated CREB.
  • A fusion protein consisting of CBP and a heterologous DNA-binding domain demonstrated protein kinase A-regulated transcriptional activation.

Conclusions:

  • CBP is a nuclear protein that specifically binds to the phosphorylated, activated form of CREB.
  • CBP likely functions as a co-activator in cAMP-regulated gene expression by interacting with phosphorylated CREB.