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(Received for publication, July 17,
1995; and in revised form, September 25, 1995) FcR
Volume 270,
Number 50,
Issue of December 15, 1995 pp. 29781-29787
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
Chain
MOLECULAR BASIS FOR CD89/FcR CHAIN ASSOCIATION
chain has previously been shown to interact with the
TCR-CD3 complex, the IgE Fc receptor I (Fc
RI), and the class I and
IIIA IgG receptors (Fc
RI and Fc
RIIIa). Here, we demonstrate
that the Fc receptor
chain associates with Fc
R in
transfected IIA1.6 B lymphocytes. FcR could be expressed at the
surface of IIA1.6 B cells by itself, but was devoid of signaling
capacity. Upon co-expression of FcR chain, a physical interaction
with Fc
R could be demonstrated. This association proved crucial
for the triggering of both proximal (intracellular calcium increase and
tyrosine phosphorylation), as well as distal (IL-2 release), signal
transduction responses. We next tested the hypothesis that a positively
charged arginine residue (Arg) within the transmembrane
domain of Fc
R promotes association with FcR chain. We
therefore constructed Fc
R molecules where Arg was
mutated to either a positively charged histidine, a negatively charged
aspartic acid, or an uncharged leucine. A functional association
between Fc
R and FcR chain was observed only with a
positively charged residue (Arg
or His
)
present within the Fc
R transmembrane domain. These data show that
transmembrane signal transduction by the FcR is mediated via FcR
chain, and that Fc
R requires a positively charged residue
within the transmembrane domain to promote functional association.
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