The membrane proximal segment of the IL-2 receptor beta-chain acidic region is essential for IL2-dependent protein tyrosine kinase activation

Leukemia. 1994 Apr;8 Suppl 1:S186-9.

Abstract

The signal transduction mechanism of the interleukin-2 receptor (IL-2R) remains largely undefined. The cytosolic domain of the IL-2R beta subunit is known to be essential for coupling to intracellular signaling pathways such as protein tyrosine kinase (PTK) and for control of IL-2 dependent cellular proliferation. A panel of cell lines that express IL-2R beta chains that contain sequential truncation mutations within the cytosolic domain were constructed. These cell lines were used to map the interaction of IL-2R with PTK activation, and the linkage of PTK function to activation of the enzyme phosphatidylinositol-3-kinase (Pl3K). The data show that the amino terminal segment of the acidic region (residues 314-350) within IL-2R beta is a critical site for PTK activation, and that activation of Pl3K is linked to IL-2 dependent tyrosine phosphorylation.

MeSH terms

  • Animals
  • Cells, Cultured
  • Enzyme Activation
  • Interleukin-2 / pharmacology*
  • Mice
  • Phosphorylation
  • Protein-Tyrosine Kinases / physiology*
  • Receptors, Interleukin-2 / physiology*

Substances

  • Interleukin-2
  • Receptors, Interleukin-2
  • Protein-Tyrosine Kinases