Phagosome maturation is an important innate defense mechanism of macrophages against pathogen infections. Phagosome-lysosome (P-L) fusion is a highly regulated process. Different RabGTPases are involved in P-L fusion. Rab7l1 is shown to regulate P-L fusion process. In the present study, we demonstrate that Rabaptin5 is a Guanine nucleotide exchange factor (GEF) for Rab7l1. We reveal that Rabaptin5 interacts with Rab7l1-GTP form and promotes its recruitment to phagosome. In the absence of Rabaptin5, localization of P-L markers like EEA1, Rab7, LAMP1 and LAMP2 was found to be poorer. Thus, our data suggest that Rabaptin5 works upstream to Rab7l1 and triggers Rab7l1 activation for further recruitment of P-L markers and downstream regulation of phagosomal maturation process.