SWAP70 Organizes the Actin Cytoskeleton and Is Essential for Phagocytosis

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

doi:10.1016/j.celrep.2016.10.021

Cell Reports (Nov 2016)

SWAP70 Organizes the Actin Cytoskeleton and Is Essential for Phagocytosis

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

Affiliations

Maksim V. Baranov: Department of Tumor Immunology, Radboud University Medical Center, Radboud Institute for Molecular Life Sciences, Geert Grooteplein 28, 6525GA Nijmegen, the Netherlands
Natalia H. Revelo: Department of Tumor Immunology, Radboud University Medical Center, Radboud Institute for Molecular Life Sciences, Geert Grooteplein 28, 6525GA Nijmegen, the Netherlands
Ilse Dingjan: Department of Tumor Immunology, Radboud University Medical Center, Radboud Institute for Molecular Life Sciences, Geert Grooteplein 28, 6525GA Nijmegen, the Netherlands
Riccardo Maraspini: Max Planck Institute of Molecular Cell Biology and Genetics, Pfotenhauerstrasse 108, 01307 Dresden, Germany
Martin ter Beest: Department of Tumor Immunology, Radboud University Medical Center, Radboud Institute for Molecular Life Sciences, Geert Grooteplein 28, 6525GA Nijmegen, the Netherlands
Alf Honigmann: Max Planck Institute of Molecular Cell Biology and Genetics, Pfotenhauerstrasse 108, 01307 Dresden, Germany
Geert van den Bogaart: Department of Tumor Immunology, Radboud University Medical Center, Radboud Institute for Molecular Life Sciences, Geert Grooteplein 28, 6525GA Nijmegen, the Netherlands

DOI: https://doi.org/10.1016/j.celrep.2016.10.021
Journal volume & issue: Vol. 17, no. 6
pp. 1518 – 1531

Abstract

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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.

Published in Cell Reports

ISSN: 2211-1247 (Online)
Publisher: Elsevier
Country of publisher: Netherlands
LCC subjects: Science: Biology (General)
Website: http://www.cell.com/cell-reports/home

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