Stimulation of c-Jun activity by CBP: c-Jun residues Ser63/73 are required for CBP induced stimulation in vivo and CBP binding in vitro

Oncogene. 1995 Dec 21;11(12):2509-14.

Abstract

The CBP protein mediates PKA induced transcription by binding to the PKA phosphorylated activation domain of CREB. Here we show that CBP also stimulates the activity of both c-Jun and v-Jun in vivo. The CREB binding domain of CBP is sufficient to contact to c-Jun in vitro. When this domain of CBP is linked to the activation domain of VP16 and expressed in vivo it stimulates c-Jun dependent transcription. Deletion analysis of c-Jun indicate that the CBP binding site is within the N-terminal activation domain. Loss of binding to CBP in vitro correlates with severely reduced transactivation capacity in vivo. Mutation of Ser63/73 in c-Jun, or the corresponding position in v-Jun (Ser36/46) leads to reduced binding to CBP in vitro and abolishes augmentation of transcription in vivo. These data are consistent with a mechanism by which CBP acts as a co-activator protein for Jun dependent transcription by interacting with the Jun N-terminal activation domain.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Binding Sites
  • Humans
  • Phosphorylation
  • Proto-Oncogene Proteins c-jun / metabolism*
  • Transcription Factors / metabolism
  • Transcription Factors / pharmacology*
  • Transcriptional Activation

Substances

  • Proto-Oncogene Proteins c-jun
  • Transcription Factors