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- W2751041246 abstract "The Arp2/3 complex nucleates branched actin, forming networks involved in lamellipodial protrusion, phagocytosis, and cell adhesion. We derived primary bone marrow macrophages lacking Arp2/3 complex (Arpc2-/-) and directly tested its role in macrophage functions. Despite protrusion and actin assembly defects, Arpc2-/- macrophages competently phagocytose via FcR and chemotax toward CSF and CX3CL1. However, CR3 phagocytosis and fibronectin haptotaxis, both integrin-dependent processes, are disrupted. Integrin-responsive actin assembly and αM/β2 integrin localization are compromised in Arpc2-/- cells. Using an in vivo system to observe endogenous monocytes migrating toward full-thickness ear wounds we found that Arpc2-/- monocytes maintain cell speeds and directionality similar to control. Our work reveals that the Arp2/3 complex is not a general requirement for phagocytosis or chemotaxis but is a critical driver of integrin-dependent processes. We demonstrate further that cells lacking Arp2/3 complex function in vivo remain capable of executing important physiological responses that require rapid directional motility." @default.
- W2751041246 created "2017-09-15" @default.
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- W2751041246 date "2017-09-01" @default.
- W2751041246 modified "2023-10-15" @default.
- W2751041246 title "Arp2/3 Complex Is Required for Macrophage Integrin Functions but Is Dispensable for FcR Phagocytosis and In Vivo Motility" @default.
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- W2751041246 doi "https://doi.org/10.1016/j.devcel.2017.08.003" @default.
- W2751041246 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/5601320" @default.
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- W2751041246 hasPublicationYear "2017" @default.
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