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Related Experiment Videos

Factor-specific modulation of CREB-binding protein acetyltransferase activity.

V Perissi1, J S Dasen, R Kurokawa

  • 1Howard Hughes Medical Institute, University of California at San Diego, La Jolla, CA 92093-0648, USA.

Proceedings of the National Academy of Sciences of the United States of America
|March 31, 1999
PubMed
Summary
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Adenovirus E1A protein inhibits CBP acetyltransferase activity, while CREB binding does not. The coactivator p/CIP shows variable effects on CBP activity, suggesting differential regulation of transcription factors.

Area of Science:

  • Molecular Biology
  • Epigenetics
  • Gene Regulation

Background:

  • CREB-binding protein (CBP) and p300 are crucial transcriptional coactivators.
  • They facilitate transcription factor assembly and possess intrinsic acetyltransferase activity.
  • Cofactors like p/CIP and p/CAF interact with CBP/p300.

Purpose of the Study:

  • To investigate how adenovirus E1A and coactivator p/CIP modulate CBP/p300 acetyltransferase activity.
  • To understand the differential regulation of CBP/p300 function by distinct protein interactions.

Main Methods:

  • Assaying the effect of adenovirus E1A binding to CBP's C/H3 domain on its acetyltransferase activity.
  • Examining the impact of CREB or CREB/E1A fusion protein binding to CBP's KIX domain.
  • Evaluating the influence of p/CIP on CBP acetyltransferase activity using different substrates and p/CIP functional domains.

Related Experiment Videos

Main Results:

  • Adenovirus E1A inhibits CBP acetyltransferase activity upon binding to the C/H3 domain.
  • CREB binding to the KIX domain does not inhibit CBP acetyltransferase activity.
  • p/CIP exhibits context-dependent effects, inhibiting histone acetylation but enhancing Pit-1 acetylation by CBP.

Conclusions:

  • Distinct regions of CBP/p300 can be differentially modulated by interacting proteins like E1A and p/CIP.
  • Regulation of CBP/p300 acetyltransferase activity by these interactions offers a mechanism for integrating diverse signaling pathways.
  • This differential modulation impacts coactivator functions for various transcription factors.