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Interaction and functional collaboration of p300/CBP and bHLH proteins in muscle and B-cell differentiation

R Eckner1, T P Yao, E Oldread

  • 1Dana-Farber Cancer Institute and Harvard Medical School, Boston, Massachusetts 02115, USA.

Genes & Development
|October 1, 1996
PubMed

Insights

Cellular differentiation of muscle and B cells relies on basic helix-loop-helix (bHLH) proteins. The study reveals that p300/CBP coactivators are essential for bHLH-mediated transcription and cellular differentiation.

Area of Science:

  • Molecular Biology
  • Cell Biology
  • Biochemistry

Background:

  • Basic helix-loop-helix (bHLH) proteins regulate skeletal muscle and B lymphocyte differentiation.
  • Adenovirus E1A oncoprotein inhibits these differentiation processes.
  • Cellular-binding proteins p300 and CBP are implicated in differentiation control.

Purpose of the Study:

  • To investigate the role of p300/CBP in bHLH protein-mediated transcriptional activation.
  • To determine the necessity of p300/CBP for cellular differentiation processes.

Main Methods:

  • Analysis of adenovirus E1A mutants.
  • Cooperation assays between p300 and tissue-specific bHLH proteins.
  • Microinjection of p300/CBP antibodies into myoblasts.

Main Results:

  • p300 cooperates with bHLH proteins to activate target genes, requiring only the bHLH domain.
  • Transcriptional activation by bHLH proteins correlates with p300/CBP presence in DNA-binding complexes, dependent on E-box motifs.
  • Antibodies against p300/CBP inhibit myoblast differentiation, cell fusion, and myogenic bHLH transcriptional activity.

Conclusions:

  • p300/CBP are essential coactivators for bHLH proteins in gene activation.
  • The function of p300/CBP is critical for key aspects of skeletal muscle and B lymphocyte differentiation.

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