Phosphorylation and Activation of the Jak-3 Janus Kinase in Response to interleukin-2

Nature. 1994 Jul 14;370(6485):151-3. doi: 10.1038/370151a0.

Abstract

Interleukin-2 is an autocrine growth factor for T cells which also activates other cells including B cells and natural killer cells. The subunits of the interleukin-2 receptor (IL-2R) lack intrinsic enzymatic activity, but protein tyrosine phosphorylation is a critical event following ligand binding and src family kinases, such as Lck, are known to be activated by IL-2 (refs 5-9). However, IL-2 signalling can occur in the absence of receptor interaction with Lck, suggesting that other protein tyrosine kinases might be important. Here we report that a new member of the Janus family of kinases (Jak-3) is coupled to the IL-2R in human peripheral blood T cells and natural killer cells.

MeSH terms

  • Cell Line
  • Cytokines / physiology
  • Enzyme Activation
  • Growth Hormone / physiology
  • Humans
  • In Vitro Techniques
  • Interleukin-2 / physiology*
  • Janus Kinase 3
  • Leukocytes, Mononuclear / enzymology
  • Phosphorylation
  • Protein-Tyrosine Kinases / metabolism*
  • Signal Transduction / physiology
  • Tumor Cells, Cultured

Substances

  • Cytokines
  • Interleukin-2
  • Growth Hormone
  • Protein-Tyrosine Kinases
  • JAK3 protein, human
  • Janus Kinase 3