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J Biol Chem, Vol. 274, Issue 31, 21519-21527, July 30, 1999
From the Department of Microbiology and Immunology, Faculty of
Health Sciences, and the Cancer Research Center, Ben Gurion
University of the Negev, Beer Sheva 84105, Israel
Engagement of the T cell antigen receptor
initiates signal transduction involving tyrosine phosphorylation of
multiple effector molecules and the formation of multimolecular
complexes at the receptor site. Adapter proteins that possess SH2 and
SH3 protein-protein interaction domains are implicated in the assembly
of cell activation-induced signaling complexes. We found that Crk
adapter proteins undergo activation-induced interaction with the
-chain associated protein (ZAP-70) tyrosine kinase in the human T
cell line, Jurkat. Incubation of various glutathione
S-transferase fusion proteins with a lysate of activated
Jurkat cells resulted in selective association of ZAP-70 with Crk, but
not Grb2 or Nck, adapter proteins. In addition, tyrosine-phosphorylated
ZAP-70 co-immunoprecipitated with Crk from a lysate of activated Jurkat
cells, and ZAP-70 association with GST-Crk was observed in a lysate of
activated human peripheral blood T cells. Association between the two
molecules was mediated by direct physical interaction and involved the
Crk-SH2 domain and phosphotyrosyl-containing sequences on ZAP-70. The
association required intact Lck, considered to be an upstream regulator
of ZAP-70, because it could not take place in activated JCaM1 cells, which express normal levels of ZAP-70 but are devoid of Lck. Finally, glutathione S-transferase-Crk fusion proteins were found to
interact predominantly with membrane-residing tyrosine-phosphorylated
ZAP-70 that exhibited autophosphorylation activity as well as
phosphorylation of an exogenous substrate, CFB3. These findings suggest
that Crk adapter proteins play a role in the early activation events of T lymphocytes, apparently, by direct interaction with, and regulation of, the membrane-residing ZAP-70 protein tyrosine kinase.
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