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

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.

Pubmed ID: 10383400


  • Ron D
  • Napolitano EW
  • Voronova A
  • Vasquez NJ
  • Roberts DN
  • Calio BL
  • Caothien RH
  • Pettiford SM
  • Wellik S
  • Mandac JB
  • Kauvar LM


The Journal of biological chemistry

Publication Data

July 2, 1999

Associated Grants


Mesh Terms

  • Antibodies
  • Electroporation
  • Humans
  • Interleukin-4
  • Isoenzymes
  • Jurkat Cells
  • Protein Kinase C
  • Protein-Tyrosine Kinases
  • Proto-Oncogene Proteins
  • Proto-Oncogene Proteins c-fyn
  • T-Lymphocytes