CBP/p300 integrates Raf/Rac-signaling pathways in the transcriptional induction of NF-ATc during T cell activation

Immunity. 1999 May;10(5):515-24. doi: 10.1016/s1074-7613(00)80051-5.


NF-ATc, an inducibly expressed transcription factor, controls gene expression in T lymphocytes and cardiomyocytes. We show here that the transcriptional co-activators CBP/p300 bind to and control the activity of the inducible N-terminal transactivation domain of NF-ATc, TAD-A. Similar to the N terminal transactivation domain of c-Jun, TAD-A is inducibly phosphorylated, but this phosphorylation is dispensable for the interaction with CBP/p300. Constitutive active versions of c-Raf and Rac synergistically enhance the CBP/p300-mediated increase of TAD-A activity, indicating the important role CBP/p300 plays in the integration of T cell activation signals. Since a mutation of CBP abolishing HAT activity is almost as active as wild-type CBP in T cells, functions of CBP/p300 other than histone acetylation appear to control the NF-AT-dependent transcription in T cells.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Calcium-Calmodulin-Dependent Protein Kinases / pharmacology
  • DNA-Binding Proteins / physiology
  • GTP-Binding Proteins / physiology*
  • Humans
  • Lymphocyte Activation / drug effects
  • Nuclear Proteins / physiology*
  • Signal Transduction
  • T-Lymphocytes / immunology*
  • Trans-Activators / physiology*
  • Transcription Factor AP-1 / physiology
  • rac GTP-Binding Proteins


  • DNA-Binding Proteins
  • Nuclear Proteins
  • Trans-Activators
  • Transcription Factor AP-1
  • Calcium-Calmodulin-Dependent Protein Kinases
  • GTP-Binding Proteins
  • rac GTP-Binding Proteins