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(Received for publication, April 21, 1997, and in revised form, July 15, 1997)
From the Arthritis and Rheumatism Branch, NIAMS, National
Institutes of Health, Bethesda, Maryland 20892-1820
Aggregation of the high affinity receptor for IgE
(Fc
Volume 272, Number 38,
Issue of September 19, 1997
pp. 24072-24080
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
RI) leads to the phosphorylation of tyrosines on the 
and 
chains of the receptor by the Src family kinase Lyn. We have studied the interaction between Lyn and the FcRI in vivo using a
transfection-based approach. FcRI were stably transfected into
Chinese hamster ovary cells. The small amount of endogenous Src family
kinase was sufficient to phosphorylate receptor tyrosines upon
extensive aggregation of FcRI but not after addition of dimers of
IgE. Upon stable co-transfection of Lyn kinase into the cells, dimers
were now able to stimulate receptor phosphorylation and the response to more extensive aggregation was enhanced. In contrast, co-transfection with catalytically inactive Lyn inhibited the aggregation-induced phosphorylation by the endogenous kinase, and a quantitatively similar
inhibition was observed in cells transfected with the SH4-containing
unique domain of Lyn. Consistent with the results of others using
alternative approaches, our additional studies using a yeast two-hybrid
system detected a direct interaction between intact Lyn or its unique
domain and the C-terminal cytoplasmic domain of the chain but not
with the receptor's other cytoplasmic domains.
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