Ras/mitogen-activated protein kinase signaling activates Ets-1 and Ets-2 by CBP/p300 recruitment

Mol Cell Biol. 2004 Dec;24(24):10954-64. doi: 10.1128/MCB.24.24.10954-10964.2004.

Abstract

Cell signaling affects gene expression by regulating the activity of transcription factors. Here, we report that mitogen-activated protein kinase (MAPK) phosphorylation of Ets-1 and Ets-2, at a conserved site N terminal to their Pointed (PNT) domains, resulted in enhanced transactivation by preferential recruitment of the coactivators CREB binding protein (CBP) and p300. We discovered this phosphorylation-augmented interaction in an unbiased affinity chromatography screen of HeLa nuclear extracts by using either mock-treated or ERK2-phosphorylated ETS proteins as ligands. Binding between purified proteins demonstrated a direct interaction. Both the phosphoacceptor site, which lies in an unstructured region, and the PNT domain were required for the interaction. Minimal regions that were competent for induced CBP/p300 binding in vitro also supported MAPK-enhanced transcription in vivo. CBP coexpression potentiated MEK1-stimulated Ets-2 transactivation of promoters with Ras-responsive elements. Furthermore, CBP and Ets-2 interacted in a phosphorylation-enhanced manner in vivo. This study describes a distinctive interface for a transcription factor-coactivator complex and demonstrates a functional role for inducible CBP/p300 binding. In addition, our findings decipher the mechanistic link between Ras/MAPK signaling and two specific transcription factors that are relevant to both normal development and tumorigenesis.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Acetyltransferases / metabolism
  • Amino Acid Sequence
  • Baculoviridae / genetics
  • Blotting, Western
  • CREB-Binding Protein
  • Cell Cycle Proteins / metabolism
  • Chromatography, Affinity
  • Genes, Reporter
  • Genes, ras*
  • HeLa Cells
  • Histone Acetyltransferases
  • Humans
  • Luciferases / metabolism
  • Mitogen-Activated Protein Kinases / metabolism*
  • Models, Biological
  • Models, Molecular
  • Nuclear Magnetic Resonance, Biomolecular
  • Nuclear Proteins / metabolism*
  • Phosphorylation
  • Protein Structure, Tertiary
  • Proto-Oncogene Protein c-ets-1
  • Proto-Oncogene Protein c-ets-2
  • Proto-Oncogene Proteins / chemistry
  • Proto-Oncogene Proteins / genetics
  • Proto-Oncogene Proteins / metabolism*
  • Proto-Oncogene Proteins c-ets
  • Recombinant Proteins / metabolism
  • Signal Transduction*
  • Silver Staining
  • Trans-Activators / chemistry
  • Trans-Activators / genetics
  • Trans-Activators / metabolism*
  • Transcription Factors / chemistry
  • Transcription Factors / genetics
  • Transcription Factors / metabolism*
  • Transcriptional Activation
  • p300-CBP Transcription Factors

Substances

  • Cell Cycle Proteins
  • ETS1 protein, human
  • ETS2 protein, human
  • Nuclear Proteins
  • Proto-Oncogene Protein c-ets-1
  • Proto-Oncogene Protein c-ets-2
  • Proto-Oncogene Proteins
  • Proto-Oncogene Proteins c-ets
  • Recombinant Proteins
  • Trans-Activators
  • Transcription Factors
  • Luciferases
  • Acetyltransferases
  • CREB-Binding Protein
  • CREBBP protein, human
  • Histone Acetyltransferases
  • p300-CBP Transcription Factors
  • p300-CBP-associated factor
  • Mitogen-Activated Protein Kinases