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- W2127810225 abstract "Rac1 is a Ρ-family GTP-binding protein that controls lamellipodia formation and membrane ruffling in fibroblasts. Recently, Rac1 and Cdc42, another member of the Ρ-family, have been shown to regulate Fc receptor-mediated phagocytosis in macrophages by controlling different steps of membrane and actin dynamics leading to particle engulfment. Here, we investigated the function of Rac1 using a membrane recruitment system that mimics phagocytosis. Recruitment of an activated Rac1 protein to the cytoplasmic domain of an engineered membrane receptor by using rapamycin as a bridge induces ingestion of latex beads bound to the receptor. Rac1-mediated bead uptake depends on actin polymerisation since actin filaments accumulate at the bead/membrane binding sites and internalisation is inhibited by cytochalasin D. Internalisation is also abolished upon substitution of Phe37 to Leu in the Rac1 effector region. Our results indicate that by promoting actin polymerisation at particle attachment sites, Rac1 by acting through specific downstream effectors induces plasma membrane remodeling that allows particle internalisation in a membrane-enclosed phagosome." @default.
- W2127810225 created "2016-06-24" @default.
- W2127810225 creator A5003805520 @default.
- W2127810225 creator A5058702473 @default.
- W2127810225 creator A5066969008 @default.
- W2127810225 date "2000-09-01" @default.
- W2127810225 modified "2023-10-18" @default.
- W2127810225 title "Membrane recruitment of Rac1 triggers phagocytosis" @default.
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- W2127810225 doi "https://doi.org/10.1242/jcs.113.17.2955" @default.
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