Interleukin 2 (IL-2)-induced tyrosine phosphorylation of IL-2 receptor p75

J Exp Med. 1990 Mar 1;171(3):637-44. doi: 10.1084/jem.171.3.637.

Abstract

We have recently established a mAb named TU11 mAb specific for the p75 subunit of human IL-2 receptor (IL-2R). The present study using TU11 mAb demonstrates the IL-2-induced phosphorylation of IL-2Rp75 on tyrosine residues in IL-2-dependent T cells. The tyrosine phosphorylation is mediated by the high affinity IL-2R, correlates with the IL-2-induced cell growth, and rapidly increases during the first 5 min of IL-2 stimulation. Phosphorylation of serine and threonine residues of IL-2Rp75 is also detected, but its IL-2 dependency is not significant during at least the first 5 min. These results suggest some roles of a tyrosine kinase associated with IL-2Rp75 in the IL-2-induced signal-transducing pathway.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Humans
  • Interleukin-2 / pharmacology*
  • Phosphorylation
  • Protein-Tyrosine Kinases / physiology
  • Receptors, Interleukin-2 / metabolism*
  • Threonine / metabolism
  • Tyrosine / metabolism*

Substances

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