Direct interaction in T-cells between thetaPKC and the tyrosine kinase p59fyn

J Biol Chem. 1999 Jul 2;274(27):19003-10. doi: 10.1074/jbc.274.27.19003.

Abstract

The protein kinase C (PKC) family has been clearly implicated in T-cell activation as have several nonreceptor protein-tyrosine kinases associated with the T-cell receptor, including p59fyn. This report demonstrates that thetaPKC and p59fyn specifically interact in vitro, in the yeast two-hybrid system, and in T-cells. Further indications of direct interaction are that p59fyn potentiates thetaPKC catalytic activity and that thetaPKC is a substrate for tyrosine phosphorylation by p59fyn. This interaction may account for the localization of thetaPKC following T-cell activation, pharmacological disruption of which results in specific cell-signaling defects. The demonstration of a physical interaction between a PKC and a protein-tyrosine kinase expands the class of PKC-anchoring proteins (receptors for activated C kinases (RACKs)) and demonstrates a direct connection between these two major T-cell-signaling pathways.

MeSH terms

  • Antibodies / administration & dosage
  • Antibodies / pharmacology
  • Electroporation
  • Humans
  • Interleukin-4 / metabolism
  • Isoenzymes / immunology
  • Isoenzymes / metabolism*
  • Jurkat Cells
  • Protein Kinase C / immunology
  • Protein Kinase C / metabolism*
  • Protein Kinase C-theta
  • Protein-Tyrosine Kinases / metabolism*
  • Proto-Oncogene Proteins / immunology
  • Proto-Oncogene Proteins / metabolism*
  • Proto-Oncogene Proteins c-fyn
  • T-Lymphocytes / enzymology*

Substances

  • Antibodies
  • Isoenzymes
  • Proto-Oncogene Proteins
  • Interleukin-4
  • Protein-Tyrosine Kinases
  • FYN protein, human
  • Proto-Oncogene Proteins c-fyn
  • PRKCQ protein, human
  • Protein Kinase C
  • Protein Kinase C-theta