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RIIa Involves Three Distinct Cytoplasmic Kinase Families Leading to Phagocytosis1
*
Immunobiology and Cancer Program, Oklahoma Medical Research Foundation, Oklahoma City, OK 73104;
Molecular, Cellular and Developmental Biology Program and Departments of
Biochemistry and
Microbiology, Ohio State University, Columbus, OH 43210
Recent experiments indicate an important role for Src family and
Syk protein tyrosine kinases and phosphatidylinositol 3-kinase in the
signal transduction process initiated by mouse receptors for IgG and
leading to phagocytosis. Considerably less is known regarding signal
transduction by the human-restricted IgG receptor, Fc
RIIa.
Furthermore, the relationship among the Src family, Syk, and
phosphatidylinositol 3-kinase in phagocytosis is not understood. Here,
we show that FcRIIa is phosphorylated by an Src family member, which
results in recruitment and concomitant activation of the distal enzymes
Syk and phosphatidylinositol 3-kinase. Using a FcRI-p85 receptor
chimera cotransfected with kinase-inactive mutants of Syk or
application of a pharmacological inhibitor of Syk, we show that Syk
acts in parallel with phosphatidylinositol 3-kinase. Our results
indicate that FcRIIa-initiated monocyte or neutrophil phagocytosis
proceeds from the clustered IgG receptor to Src to phosphatidylinositol
3-kinase and Syk.
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