SWAP70 Organizes the Actin Cytoskeleton and Is Essential for Phagocytosis.

Baranov, Maksim V; Revelo, Natalia H; Dingjan, Ilse; Maraspini, Riccardo; Beest, Martin Ter; Honigmann, Alf; Bogaart, Geert van den

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SWAP70 Organizes the Actin Cytoskeleton and Is Essential for Phagocytosis.

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Maraspini, Riccardo
Max Planck Institute of Molecular Cell Biology and Genetics, Max Planck Society;

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Honigmann, Alf
Max Planck Institute of Molecular Cell Biology and Genetics, Max Planck Society;

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引用

Baranov, M. V., Revelo, N. H., Dingjan, I., Maraspini, R., Beest, M. T., Honigmann, A., & Bogaart, G. v. d. (2016). SWAP70 Organizes the Actin Cytoskeleton and Is Essential for Phagocytosis. Cell Reports, 17(6), 1518-1531.

引用: https://hdl.handle.net/21.11116/0000-0001-037F-E

要旨

Actin plays a critical role during the early stages of pathogenic microbe internalization by immune cells. In this study, we identified a key mechanism of actin filament tethering and stabilization to the surface of phagosomes in human dendritic cells. We found that the actin-binding protein SWAP70 is specifically recruited to nascent phagosomes by binding to the lipid phosphatidylinositol (3,4)-bisphosphate. Multi-color super-resolution stimulated emission depletion (STED) microscopy revealed that the actin cage surrounding early phagosomes is formed by multiple concentric rings containing SWAP70. SWAP70 colocalized with and stimulated activation of RAC1, a known activator of actin polymerization, on phagosomes. Genetic ablation of SWAP70 impaired actin polymerization around phagosomes and resulted in a phagocytic defect. These data show a key role for SWAP70 as a scaffold for tethering the peripheral actin cage to phagosomes.