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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Citation

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

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

Abstract

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.