Your browser doesn't support javascript.
loading
Direct interaction in T-cells between thetaPKC and the tyrosine kinase p59fyn.
Ron, D; Napolitano, E W; Voronova, A; Vasquez, N J; Roberts, D N; Calio, B L; Caothien, R H; Pettiford, S M; Wellik, S; Mandac, J B; Kauvar, L M.
Affiliation
  • Ron D; Telik, Inc., South San Francisco, California 94080, USA.
J Biol Chem ; 274(27): 19003-10, 1999 Jul 02.
Article in En | MEDLINE | ID: mdl-10383400
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.
Subject(s)
Search on Google
Collection: 01-internacional Database: MEDLINE Main subject: Protein Kinase C / Protein-Tyrosine Kinases / T-Lymphocytes / Proto-Oncogene Proteins / Isoenzymes Limits: Humans Language: En Journal: J Biol Chem Year: 1999 Type: Article Affiliation country: United States
Search on Google
Collection: 01-internacional Database: MEDLINE Main subject: Protein Kinase C / Protein-Tyrosine Kinases / T-Lymphocytes / Proto-Oncogene Proteins / Isoenzymes Limits: Humans Language: En Journal: J Biol Chem Year: 1999 Type: Article Affiliation country: United States