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R1
Department of Cell Biology, Nencki Institute of Experimental Biology, Warsaw, Poland
Recent data indicate that phagocytosis mediated by Fc
Rs is
controlled by the Src and Syk families of protein tyrosine kinases. In
this study, we demonstrate a sequential involvement of Lyn and Syk in
the phagocytosis of IgG-coated particles. The particles isolated at the
stage of their binding to FcRs (4°C) were accompanied by high
amounts of Lyn, in addition to the signaling -chain of FcRs.
Simultaneously, the particle binding induced rapid tyrosine
phosphorylation of numerous proteins. During synchronized
internalization of the particles induced by shifting the cell to
37°C, Syk kinase and Src homology 2-containing tyrosine phosphatase-1
(SHP-1) were associated with the formed phagosomes. At this
step, most of the proteins were dephosphorylated, although some
underwent further tyrosine phosphorylation. Quantitative immunoelectron
microscopy studies confirmed that Lyn accumulated under the plasma
membrane beneath the bound particles. High amounts of the -chain and
tyrosine-phosphorylated proteins were also observed under the bound
particles. When the particles were internalized, the -chain was
still detected in the region of the phagosomes, while amounts of Lyn
were markedly reduced. In contrast, the vicinity of the phagosomes was
heavily decorated with anti-Syk and anti-SHP-1 Abs. The local
level of protein tyrosine phosphorylation was reduced. The data
indicate that the accumulation of Lyn during the binding of IgG-coated
particles to FcRs correlated with strong tyrosine phosphorylation of
numerous proteins, suggesting an initiating role for Lyn in protein
phosphorylation at the onset of the phagocytosis. Syk kinase and
SHP-1 phosphatase are mainly engaged at the stage of particle
internalization.
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