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The pro-oncoprotein EWS (Ewing's Sarcoma protein) interacts with the Brn-3a POU transcription factor and inhibits its ability to activate transcription.

The Brn-3a POU family transcription factor is able to induce the expression of a number of neuronally-expressed genes as well as to enhance neuronal differentiation and inhibit apoptosis. Many of these effects are mediated by the C-terminal POU domain of Brn-3a which acts both as a DNA binding domain and a transcriptional activation domain. To identify the mechanisms by which this domain acts, we carried out a yeast two hybrid assay to identify proteins which interact with it. We show that both full length Brn-3a and the isolated POU domain interact with the EWS transcription factor and its oncogenic derivative EWS-Fli1. Moreover, EWS can block Brn-3a-mediated activation of the Bcl-x promoter whereas this effect is lost in EWS-Fli1. The significance of this novel interaction is discussed in terms of the manner in which Brn-3a regulates its target promoters and the mechanism of oncogenic transformation by EWS-Fli1.

Pubmed ID: 12432261


  • Thomas GR
  • Latchman DS


Cancer biology & therapy

Publication Data

November 14, 2002

Associated Grants


Mesh Terms

  • Cell Line
  • Cell Transformation, Neoplastic
  • DNA-Binding Proteins
  • Genes, Reporter
  • Glutathione Transferase
  • Humans
  • Luciferases
  • Protein Binding
  • Protein Biosynthesis
  • Protein Structure, Tertiary
  • RNA-Binding Protein EWS
  • Transcription Factor Brn-3
  • Transcription Factor Brn-3A
  • Transcription Factors
  • Transcription, Genetic
  • Two-Hybrid System Techniques