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Receptor I-Associated lyn-Dependent Phosphorylation of Fc
Receptor IIB During Negative Regulation of Mast Cell Activation1
*
Laboratoire d’Immunologie Cellulaire et Clinique, INSERM U.255, Institut Curie, Paris, France;
Department of Pediatrics, National Jewish Center for Immunology and Respiratory Medicine, Denver, CO 80206; and
Division of Cellular Immunology, National Institute for Medical Research, London, United Kingdom
Fc
RIIB are low-affinity receptors for IgG whose intracytoplasmic
domain contains an immunoreceptor tyrosine-based inhibition motif
(ITIM). FcRIIB inhibit cell activation triggered by receptors that
signal via immunoreceptor tyrosine-based activation motifs. This
inhibition requires ITIM tyrosyl phosphorylation and is correlated with
the binding of SH2 domain-containing phosphatases that may mediate the
inhibitory signal. In the present work, we investigated the mechanism
of FcRIIB phosphorylation and its consequences in mast cells. We
demonstrate that the phosphorylation of FcRIIB requires
coaggregation with Fc
RI and that, once phosphorylated, FcRIIB
selectively recruit the inositol polyphosphate 5 phosphatase SHIP, in
vivo. In vitro, however, the phosphorylated FcRIIB ITIM binds not
only SHIP, but also the two protein tyrosine phosphatases, SHP-1 and
SHP-2. We show that the coaggregation of FcRIIB with FcRI does
not prevent FcRI-mediated activation of lyn and
syk. Both kinases can phosphorylate FcRIIB in vitro.
However, when coaggregated with FcRI, FcRIIB was in vivo
phosphorylated in syk-deficient mast cells, but not in
lyn-deficient mast cells. When FcRI are coaggregated
with FcRIIB by immune complexes, FcRI-associated lyn
may thus phosphorylate FcRIIB. By this mechanism, FcRI initiate
ITIM-dependent inhibition of intracellular propagation of their own
signals.
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