High-affinity interleukin 2 binding by an oncogenic hybrid interleukin 2-epidermal growth factor receptor molecule

Proc Natl Acad Sci U S A. 1987 Apr;84(8):2125-9. doi: 10.1073/pnas.84.8.2125.


Both interleukin 2 (IL-2) and epidermal growth factor (EGF) receptors exist in two forms that differ with respect to affinity for their ligand. Only the high-affinity receptors appear to be responsible for the proliferation signal delivered upon binding of the growth factor. Fibroblasts transfected with IL-2 receptor cDNA generate only low-affinity receptors for IL-2, but fusion of membranes from these fibroblasts with T-cell membranes converts some receptors to high affinity, indicating the involvement of a T cell-specific factor in the generation of high-affinity receptors. We have constructed a chimeric cDNA molecule containing the extracellular IL-2-binding domain of the IL-2 receptor cDNA and the transmembrane and intracellular tyrosine kinase domains of the EGF receptor cDNA. When transfected into fibroblasts, this IL-2-EGF receptor cDNA generated high-affinity receptors for IL-2. Moreover, fibroblasts transfected with the chimeric molecule were morphologically transformed and produced rapidly growing tumors in nude mice.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Cell Division
  • Cell Transformation, Neoplastic
  • Cells, Cultured
  • Cloning, Molecular
  • DNA / metabolism
  • DNA Replication
  • ErbB Receptors / genetics*
  • ErbB Receptors / metabolism
  • Genes*
  • Interleukin-2 / metabolism*
  • Kinetics
  • Mice
  • Oncogenes*
  • Phosphorylation
  • Receptors, Immunologic / genetics*
  • Receptors, Immunologic / metabolism
  • Receptors, Interleukin-2


  • Interleukin-2
  • Receptors, Immunologic
  • Receptors, Interleukin-2
  • DNA
  • ErbB Receptors