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

Dorit Ron, Eugene W. Napolitano, Anna Voronova, Nicki J. Vasquez, Doug N. Roberts, Brenda L. Calio, Roger H. Caothien, Sherrie M. Pettiford, Sarah Wellik, Janis B. Mandac, Lawrence M. Kauvar

Research output: Contribution to journalArticlepeer-review

36 Scopus citations


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 θPKC 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 θPKC catalytic activity and that θPKC is a substrate for tyrosine phosphorylation by p59fyn. This interaction may account for the localization of θPKC 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.

Original languageEnglish (US)
Pages (from-to)19003-19010
Number of pages8
JournalJournal of Biological Chemistry
Issue number27
StatePublished - Jul 2 1999
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology


Dive into the research topics of 'Direct interaction in T-cells between θPKC and the tyrosine kinase p59fyn'. Together they form a unique fingerprint.

Cite this