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Receptor-Mediated Phagocytosis1
*
Department of Allergy and Rheumatology, Faculty of Medicine, University of Tokyo, Tokyo, Japan;
Division of Protein Metabolism, Institute for Protein Research, Osaka University, Osaka, Japan; and
Department of Oncology, Institute of Medical Science, University of Tokyo, Tokyo, Japan
The tyrosine phosphorylation cascade originated from Fc
receptors (FcRs) is essential for macrophage functions including
phagocytosis. Although the initial step is ascribed to Src family
tyrosine kinases, the role of individual kinases in phagocytosis
signaling is still to be determined. In reconstitution experiments, we
first showed that expression in the RAW 264.7 cell line of C-terminal
Src kinase (Csk) inhibited and that of a membrane-anchored,
gain-of-function Csk abolished the FcR-mediated signaling that leads
to phagocytosis in a kinase-dependent manner. We next tested
reconstruction of the signaling in the membrane-anchored,
gain-of-function Csk-expressing cells by introducing Src family kinases
the C-terminal negative regulatory sequence of which was replaced with
a c-myc epitope. Those constructs derived from Lyn and Hck (a-Lyn and
a-Hck) that associated with detergent-resistant membranes successfully
reconstructed FcR-mediated Syk activation, filamentous actin
rearrangement, and phagocytosis. In contrast, c-Src-derived construct
(a-Src), that was excluded from detergent-resistant membranes, could
not restore the series of phagocytosis signaling. Tyrosine
phosphorylation of Vav and c-Cbl was restored in common by a-Lyn,
a-Hck, and a-Src, but FcRIIB tyrosine phosphorylation, which is
implicated in negative signaling, was reconstituted solely by a-Lyn and
a-Hck. These findings suggest that Src family kinases are
differentially involved in FcR-signaling and that selective kinases
including Lyn and Hck are able to fully transduce phagocytotic
signaling.
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