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RIIB1 Activates Src Homology 2-Containing Protein Tyrosine Phosphatase-11
The John P. Robarts Research Institute and Department of Microbiology and Immunology, University of Western Ontario, London, Ontario, Canada
Fc
RIIB1 (CD32) is a receptor that binds the Fc domain of
Ag-complexed IgG. Coaggregation of B cell receptor (BCR) and Fc
RIIB1
generates a dominant negative signal that inhibits B cell activation.
In Ag-specific Id-positive B cells, the co-cross-linking of BCR and
Fc
RIIB1 by anti-Id Ab resulted in the association of both Src
homology 2-containing protein tyrosine phosphatase (SHP-1) and Src
homology 2-containing inositol phosphatase (SHIP) with the Fc
RIIB1;
however, only SHIP activity was detected. "Superclustering" of the
BCR and Fc
RIIB1 complex induced by stimulation with anti-Id Ab
plus polyvalent Ag synergistically activated SHP-1. The degree of
co-cross-linking between BCR and Fc
RIIB1 may determine the
activation status of SHP-1 and SHIP.
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