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The Journal of Immunology, 1998, 161: 2716-2722.
Copyright © 1998 by The American Association of Immunologists

Superclustering of B Cell Receptor and Fc{gamma}RIIB1 Activates Src Homology 2-Containing Protein Tyrosine Phosphatase-11

Katsuaki Sato and Atsuo Ochi2

The John P. Robarts Research Institute and Department of Microbiology and Immunology, University of Western Ontario, London, Ontario, Canada

Fc{gamma}RIIB1 (CD32) is a receptor that binds the Fc domain of Ag-complexed IgG. Coaggregation of B cell receptor (BCR) and Fc{gamma}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{gamma}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{gamma}RIIB1; however, only SHIP activity was detected. "Superclustering" of the BCR and Fc{gamma}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{gamma}RIIB1 may determine the activation status of SHP-1 and SHIP.




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