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.
J A Johnston  1 ,  M Kawamura ,  R A Kirken ,  Y Q Chen ,  T B Blake ,  K Shibuya ,  J R Ortaldo ,  D W McVicar ,  J J O'Shea
Affiliations
  • 1. Leukocyte Cell Biology Section, PRI/DynCorp, Frederick, Maryland.
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.