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Heterodimerization of the transcription factors E2F-1 and DP-1 leads to cooperative trans-activation.

The E2F transcription factor has been implicated in the regulation of genes whose products are involved in cell proliferation. Two proteins have recently been identified with E2F-like properties. One of these proteins, E2F-1, has been shown to mediate E2F-dependent trans-activation and to bind the hypophosphorylated form of the retinoblastoma protein (pRB). The other protein, murine DP-1, was purified from an E2F DNA-affinity column, and it was subsequently shown to bind the consensus E2F DNA-binding site. To study a possible interaction between E2F-1 and DP-1, we have now isolated a cDNA for the human homolog of DP-1. Human DP-1 and E2F-1 associate both in vivo and in vitro, and this interaction leads to enhanced binding to E2F DNA-binding sites. The association of E2F-1 and DP-1 leads to cooperative activation of an E2F-responsive promoter. Finally, we demonstrate that E2F-1 and DP-1 association is required for stable interaction with pRB in vivo and that trans-activation by E2F-1/DP-1 heterodimers is inhibited by pRB. We suggest that "E2F" is the activity that is formed when an E2F-1-related protein and a DP-1-related protein dimerize.

Pubmed ID: 8405995


  • Helin K
  • Wu CL
  • Fattaey AR
  • Lees JA
  • Dynlacht BD
  • Ngwu C
  • Harlow E


Genes & development

Publication Data

October 19, 1993

Associated Grants


Mesh Terms

  • Adenovirus E2 Proteins
  • Amino Acid Sequence
  • Cell Cycle Proteins
  • Cloning, Molecular
  • DNA, Complementary
  • Genes, Reporter
  • Humans
  • Models, Genetic
  • Molecular Sequence Data
  • Protein Conformation
  • Recombinant Fusion Proteins
  • Retinoblastoma Protein
  • Sequence Analysis
  • Sequence Homology, Amino Acid
  • Transcription Factor DP1
  • Transcription Factors
  • Transcription, Genetic
  • Transcriptional Activation
  • Transfection
  • Tumor Cells, Cultured