In our hypothetical model, Rab10 is initially recruited to PI(3,4) P2 /PI(3,4,5) P3 positive membrane ruffles at the early stage of macropinosome formation. The factors that underlie Rab10-patched recruitment to these initial membranes are not known. During the process of full ruffle closure, PI(3,4,5) P3 is concentrated on macropinosomes, with Rab10 now recruited at much higher levels to facilitate early trafficking of macropinosomes. Now distinct form the plasma membrane, without LRRK2 phosphorylation, Rab10 binds EHBP1L1 to facilitate the formation of tubular endosomes which mediate fast recycling of surface receptors. Our antibody staining demonstrates that virtually all macropinosomes (defined by 70 kDa dextran positivity) in the cells studied here included the GPCR CCR5 and integrins (CD11b). The fate of recycling-tubular endosomes is likely dictated by EHBP1L1 effectors and the local microcytoskeleton network. On the other hand, if LRRK2 phosphorylation of Rab10 occurs on Thr73, EHBP1L1 interaction is weakened and instead RILPL2 interaction is promoted. The net effect may be to inhibit EHBP1L1-mediated fast recycling of CCR5 to retain an endosome-localized activated receptor complex. In vesicle maturation, the former macropinosomes assume early and then late endosome markers. These endosomes, if loaded with CCL5-bound CCR5, appear to potently activate Akt signaling pathways using these PI(3,4,5) P3 enriched vesicles as a platform. Through this signaling axis, critical pathways that mediate chemotaxis, as well as other possible pathways not studied here including cell survival in tissues and respiratory bursts, may be promoted (through LRRK2 phosphorylation of Rab10). 