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Ligation of the Fc
Volume 270,
Number 27,
Issue of July 07, pp. 16415-16421, 1995
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
Receptor-initiated Activation of Natural Killer Cells
R on natural killer (NK) cells results in
the tyrosine phosphorylation of multiple substrates critical for
intracellular signaling and activation of NK cell effector functions.
However, it remains unclear which nonreceptor protein-tyrosine kinases
(PTK) participate in this process. In this report we demonstrate that
Fc
R ligation induced the tyrosine phosphorylation and increased
the catalytic activities of both syk family PTKs, ZAP-70, and syk. The
phosphorylation of ZAP-70 and syk was enhanced markedly by
overexpression of wild-type lck but not by a kinase-inactive mutant,
suggesting that early Fc
R-initiated activation of lck results in
the subsequent regulation of syk family PTKs. The regulatory interplay
between src and syk family PTKs was emphasized further by the
observation that lck overexpression enhanced the association of ZAP-70
with the
chain of the Fc
R complex. Additional analyses
indicated that lck induced the subsequent tyrosine phosphorylation of
phospholipase C (PLC)-
2. Interestingly, the regulatory effects of
lck on ZAP-70, syk, and PLC-
2 could not be replaced by
overexpression of either fyn or src, demonstrating a selective role for
lck in effectively coupling Fc
R stimulation to critical downstream
signaling events. Taken together, our results suggest not only that
Fc
R stimulation on NK cells is coupled to the intracellular
activation of both ZAP-70 and syk, but that the src family member, lck,
can selectively regulate this tyrosine kinase cascade.
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