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Published online before print May 22, 2003
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receptors FcRIIB and FcRIIA
University of Pennsylvania School of Medicine, Philadelphia
Correspondence: Dr. Alan D. Schreiber, University of Pennsylvania School of Medicine, Hematology/Oncology Division, Biomedical Research Building II/III, Room 705, 421 Curie Blvd., Philadelphia, PA 19104. E-mail: schreibr{at}mail.med.upenn.edu
Inositol and tyrosine phosphatases have been implicated in inhibitory signaling by an Fc receptor for immunoglobulin G, Fc
RIIB, in B cells, mast cells, and monocytes. Here, we propose a role for the Src homology 2 (SH2)-containing tyrosine phosphatase-1 (SHP-1) in FcRIIB-mediated inhibition of FcR signaling. Coexpression of SHP-1 enhances FcRIIB-mediated inhibition of FcRIIA phagocytosis in COS-1 cells. SHP-1 also enhances the reduction in FcRIIA tyrosine phosphorylation that accompanies this inhibition. Significantly, tyrosine phosphorylation of Syk kinase is substantially inhibited by SHP-1. Furthermore, the activation of SHP-1 tyrosine phosphorylation is observed following stimulation of FcRII in COS-1 cells and in human monocytes. The SH2 domain containing inositol phosphatase (SHIP), SHIP-1 also enhances FcRIIB-mediated inhibition of FcRIIA, indicating that FcRIIB can use more than one pathway for its inhibitory action. In addition, SHP-1 and SHIP-1 can inhibit FcRIIA phagocytosis and signal transduction in the absence of FcRIIB. The data support emerging evidence that SH2-containing phosphatases, such as SHP-1 and SHIP-1, can modulate signaling by "activating" receptors.
Key Words: phagocytosis • tyrosine phosphorylation • inhibition
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