A single amino acid substitution in the v-Eyk intracellular domain results in activation of Stat3 and enhances cellular transformation Academic Article uri icon


MeSH Major

  • Cell Transformation, Neoplastic
  • DNA-Binding Proteins
  • Mitogen-Activated Protein Kinases
  • Receptor Protein-Tyrosine Kinases
  • Receptors, Cell Surface
  • Trans-Activators


  • The receptor tyrosine kinase Eyk, a member of the Axl/Tyro3 subfamily, activates the STAT pathway and transforms cells when constitutively activated. Here, we compared the potentials of the intracellular domains of Eyk molecules derived from c-Eyk and v-Eyk to transform rat 3Y1 fibroblasts. The v-Eyk molecule induced higher numbers of transformants in soft agar and stronger activation of Stat3; levels of Stat1 activation by the two Eyk molecules were similar. A mutation in the sequence Y933VPL, present in c-Eyk, to the v-Eyk sequence Y933VPQ led to increased activation of Stat3 and increased transformation efficiency. However, altering another sequence, Y862VNT, present in both Eyk molecules to F862VNT markedly decreased transformation without impairing Stat3 activation. These results indicate that activation of Stat3 enhances transformation efficiency and cooperates with another pathway to induce transformation.

publication date

  • February 1999



  • Academic Article



  • eng

PubMed Central ID

  • PMC116068

PubMed ID

  • 9891073

Additional Document Info

start page

  • 1401

end page

  • 9


  • 19


  • 2