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

Slimane Ait-Si-Ali, Didier Carlisi, Sandra Ramirez, Lia Cristina Upegui-Gonzalez, Arnaud Duquet, Philippe Robin, Brian Rudkin, Annick Harel-Bellan, Didier Trouche

Research output: Contribution to journalArticlepeer-review

117 Scopus citations

Abstract

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.

Original languageEnglish (US)
Pages (from-to)157-162
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume262
Issue number1
DOIs
StatePublished - Aug 19 1999
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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