Phosphorylation by p44 MAP Kinase/ERK1 stimulates CBP histone acetyl transferase activity in vitro Academic Article


  • Biochemical and Biophysical Research Communications


  • The transcriptional coactivator CBP displays an intrinsic histone acetyl transferase (HAT) activity which seems to participate in transcriptional activation through the destabilization of nucleosome structure. CBP is involved in the activity of several transcription factors that are nuclear endpoints of intracellular signal transduction pathways. In some instances, the transcription factors are phosphorylated upon cell activation, which induces their interaction with CBP. CBP itself is a phosphoprotein and can be phosphorylated by cycle-dependent kinases or by MAP kinases. Here we show that CBP phosphorylation by p44 MAP kinase/ERK1 results in the stimulation of its HAT enzymatic activity. The p44 MAP kinase/ERK1 phosphorylation sites are located in the C-terminal part of the protein, outside of the HAT domain. These sites are required for enzymatic stimulation, suggesting that phosphorylation by p44 MAP kinase/ERK1 induces a conformational change of the CBP molecule. Our data suggest that, in some instances, CBP itself might be a target for signal transduction pathways.

publication date

  • 1999-8-19


  • 262


  • Chemical activation
  • Histones
  • In Vitro Techniques
  • Mitogen-Activated Protein Kinase 3
  • Mitogen-Activated Protein Kinase Kinases
  • Molecules
  • Nucleosomes
  • Phosphoproteins
  • Phosphorylation
  • Phosphotransferases
  • Proteins
  • Signal Transduction
  • Signal transduction
  • Transcription Factors
  • Transcriptional Activation
  • Transferases

International Standard Serial Number (ISSN)

  • 0006-291X

number of pages

  • 6

start page

  • 157

end page

  • 162