XXXX and @entity10255 kinases are sequentially engaged in phagocytosis mediated by Fc gamma R.

@entity18226 @entity7242 @entity46999 @entity10255 @entity669
Recent data indicate that phagocytosis mediated by FcgammaRs is controlled by the @entity7242 and @entity10255 families of protein @entity669 kinases. In this study, we demonstrate a sequential involvement of @entity18226 and @entity10255 in the phagocytosis of IgG-coated particles. The particles isolated at the stage of their binding to FcgammaRs (4 degrees C) were accompanied by high amounts of @entity18226 , in addition to the signaling gamma-chain of FcgammaRs. Simultaneously, the particle binding induced rapid @entity669 phosphorylation of numerous proteins. During synchronized internalization of the particles induced by shifting the cell to 37 degrees C, @entity10255 kinase and @entity7242 homology 2-containing @entity669 phosphatase-1 ( @entity46999 ) were associated with the formed phagosomes. At this step, most of the proteins were dephosphorylated, although some underwent further @entity669 phosphorylation. Quantitative immunoelectron microscopy studies confirmed that @entity18226 accumulated under the plasma membrane beneath the bound particles. High amounts of the gamma-chain and @entity669 -phosphorylated proteins were also observed under the bound particles. When the particles were internalized, the gamma-chain was still detected in the region of the phagosomes, while amounts of @entity18226 were markedly reduced. In contrast, the vicinity of the phagosomes was heavily decorated with anti- @entity10255 and anti- @entity46999 Abs. The local level of protein @entity669 phosphorylation was reduced. The data indicate that the accumulation of @entity18226 during the binding of IgG-coated particles to FcgammaRs correlated with strong @entity669 phosphorylation of numerous proteins, suggesting an initiating role for @entity18226 in protein phosphorylation at the onset of the phagocytosis. @entity10255 kinase and @entity46999 phosphatase are mainly engaged at the stage of particle internalization.
