Phagocytosis is a key process of the innate immune response. It involves highly orchestrated signalling events that drive remodelling of the actin cytoskeleton to form the phagocytic cup, and members of the Rho GTPase family are known to be important for this process. In addition, it has been shown that the small GTPase Rab35 is involved in endocytic processes and localises to phagosomal membranes. However, its precise role in phagocytosis remained unclear. On page 3557, Nobukazu Araki and co-workers now show that Rab35 is recruited to the phagocytic membrane following activation of the Fcγ receptor (FcγR) in macrophages and that it is required for FcγR-mediated phagocytosis. The expression of a dominant-negative Rab35, as well as its depletion by using shRNAs, inhibits FcγR-mediated phagocytosis. Furthermore, GTP-bound Rab35 associates with PtdIns(3,4,5)P3-enriched membrane regions at the base of the phagocytic cup. There, the Ras-related protein is involved in actin disassembly and remodelling, processes that are required for the formation of a fully functional phagosome. In addition Rab35-GTP recruits ACAP2 – a GTPase-activating protein for the ADP-ribosylation factor ARF6 – to the phagocytic cup. Thus, the authors suggest that, following engagement of the FcγR, Rab35 regulates actin remodelling and membrane dynamics through modulating ARF6 activity.