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Receptor IIB That Function in Inhibitory Signaling1
*
Department of Immunology, University of Colorado Health Sciences Center and National Jewish Medical and Research Center, Denver, CO 80262;
Department of Cell Biology, Yale University, New Haven, CT 06510; and
Laboratoire d’Immunologie Cellulaire et Clinique, Institut National de la Santé et de la Recherche Médicale, Unité255, Institut Curie, Paris, France
The low-affinity receptor for IgG, Fc
RIIB, functions broadly in
the immune system, blocking mast cell degranulation, dampening the
humoral immune response, and reducing the risk of autoimmunity.
Previous studies concluded that inhibitory signal transduction by
FcRIIB is mediated solely by its immunoreceptor tyrosine-based
inhibition motif (ITIM) that, when phosphorylated, recruits the
SH2-containing inositol 5'- phosphatase SHIP and the SH2-containing
tyrosine phosphatases SHP-1 and SHP-2. The mutational analysis reported
here reveals that the receptor’s C-terminal 16 residues are also
required for detectable FcRIIB association with SHIP in vivo and for
FcRIIB-mediated phosphatidylinositol 3-kinase hydrolysis by SHIP.
Although the ITIM appears to contain all the structural information
required for receptor-mediated tyrosine phosphorylation of SHIP,
phosphorylation is enhanced when the C-terminal sequence is present.
Additionally, FcRIIB-mediated dephosphorylation of CD19 is
independent of the cytoplasmic tail distal from residue 237, including
the ITIM. Finally, the findings indicate that tyrosines 290, 309, and
326 are all sites of significant FcRIIB1 phosphorylation following
coaggregation with B cell Ag receptor. Thus, we conclude that multiple
sites in FcRIIB contribute uniquely to transduction of
FcRIIB-mediated inhibitory signals.
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