In metazoan organisms, apoptotic cells are swiftly engulfed by phagocytes and degraded inside phagosomes through phagosome maturation. Defects in this process can cause inflammatory responses and autoimmune diseases. In the nematode C. elegans, a number of proteins that control the recognition, engulfment, and degradation of apoptotic cells have been identified. In particular, small GTPases known as Rabs, well known for their role in vesicle trafficking, have been implicated in the maturation of developing phagosomes and the degradation of apoptotic cell corpses. To systematically identify all the RAB proteins that play roles in apoptotic cell clearance, we performed an RNAi screen targeting 29 RAB-encoding genes in the C. elegans genome, searching for the presence of extra cell corpses in worm embryos. In addition to rab-2, rab-5, and rab-7, which were previously known to function in phagosome maturation, we discovered that inactivation of rab-35 also results in the ced (cell death abnormal) phenotype indicative of defects in apoptotic cell clearance. RAB-35 is an oncogene that has been implicated in a number of cellular processes such as the termination of cytokinesis and the control of the PI3K/AKT growth pathway. We have observed that RAB-35 localizes to the nascent phagosome in a biphasic manner around the time of phagosomal sealing. Subsequent experiments revealed that a rab-35 loss-of-function causes defects in both the engulfment and subsequent degradation of cell corpses. Moreover, genetic tests indicated that rab-35 acts upstream of rab-7 and may represent a novel cell-corpse removal pathway. We are investigating the molecular function of RAB-35 in this pathway, in particular the functional relationship between RAB-35 and the lipid second messengers PtdIns(4,5)P2 and PtdIns(3)P.