Tyrosyl phosphorylation and activation of a type II phosphatidylinositol 4-kinase by p56(lck) in concanavalin A stimulated rat splenic lymphocytes

Mol Immunol. 2000 Apr;37(6):273-80. doi: 10.1016/s0161-5890(00)00053-5.

Abstract

Recent evidence suggests that concanavalin A modulates tyrosyl phosphorylation and activation of a type II PtdIns 4-kinase in rat splenic lymphocytes. However, the regulatory protein tyrosine kinase(s) remain to be elusive. The present manuscript provides evidence that a type II PtdIns 4-kinase associates with p56(lck) in Con A stimulated rat splenic lymphocytes. In vitro phosphorylation studies suggest that p56(lck) regulates phosphorylation and activation of type II PtdIns 4-kinase. Inhibition of p56(lck) activity in vivo has shown to reduce tyrosyl phosphorylation and activation of PtdIns 4-kinase by Con A. These results suggest that p56(lck) may be the physiological regulator of type II PtdIns 4-kinase.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • 1-Phosphatidylinositol 4-Kinase / classification
  • 1-Phosphatidylinositol 4-Kinase / metabolism*
  • Animals
  • Concanavalin A / pharmacology
  • Enzyme Activation
  • In Vitro Techniques
  • Kinetics
  • Lymphocyte Activation
  • Lymphocyte Specific Protein Tyrosine Kinase p56(lck) / metabolism*
  • Lymphocytes / drug effects
  • Lymphocytes / enzymology*
  • Lymphocytes / immunology*
  • Nocodazole / pharmacology
  • Phosphorylation
  • Rats
  • Rats, Wistar
  • Signal Transduction
  • Tyrosine / metabolism

Substances

  • Concanavalin A
  • Tyrosine
  • 1-Phosphatidylinositol 4-Kinase
  • Lymphocyte Specific Protein Tyrosine Kinase p56(lck)
  • Nocodazole