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Modulation of ETS-1 transcriptional activity by huUBC9, a ubiquitin-conjugating enzyme.

Ets transcription factors have Ets DNA binding domains, that have a winged helix-turn-helix structure. ETS-1, the founding member of the family, is regulated by the Ras and Ca2+ signaling pathways and is implicated in various physiological processes leading to cell growth, differentiation and apoptosis. We have identified ETS-1 interacting factors with a yeast two-hybrid screen. The majority of the positive clones turned out to encode the human homologue of the yeast ubiquitin-conjugating enzymes UBC9 and Hus5. In two different yeast assays, ETS-1 interacted with huUBC9. In an in vitro GST 'pull-down' assay, ETS-1 and several other Ets family members complexed with huUBC9. Interestingly, in mammalian cells, coexpression of huUBC9 resulted in a substantial increase in the transcriptional activity of ETS-1. Coexpressed huUBC9 did not affect the ETS-1 protein level, and moreover, a point mutation at Cys93, an amino acid known to be essential for ubiquitination, did not abolish the stimulation of the ETS-1 transcriptional activity. Our results indicate that the modulation of ETS-1 activity by huUBC9 results from processes other than ubiquitination and ETS-1 stabilization.

Pubmed ID: 9333025


  • Hahn SL
  • Wasylyk B
  • Criqui-Filipe P
  • Criqui P



Publication Data

September 18, 1997

Associated Grants


Mesh Terms

  • Amino Acid Sequence
  • Base Sequence
  • Binding Sites
  • Cloning, Molecular
  • Humans
  • Ligases
  • Molecular Sequence Data
  • Protein-Tyrosine Kinases
  • Proto-Oncogene Protein c-ets-1
  • Proto-Oncogene Proteins
  • Proto-Oncogene Proteins c-ets
  • Recombinant Fusion Proteins
  • Sequence Alignment
  • Sequence Homology, Amino Acid
  • Transcription Factors
  • Transcription, Genetic
  • Ubiquitin-Conjugating Enzymes