The PI(3,5)P2 regulatory complex regulates both the synthesis and turnover of phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2). Necessary for proper vacuole morphology. Plays an important role in osmotically-induced vacuole fragmentation. Required for cytoplasm to vacuole transport (Cvt) vesicle formation, pexophagy and starvation-induced autophagy. Involved in correct atg9 trafficking to the pre-autophagosomal structure. Might also be involved in premeiotic DNA replication (By similarity). Component of the PI(3,5)P2 regulatory complex. The N-terminus might form a beta-propeller domain involved in specific binding to phosphatidylinositol 3,5-bisphosphate (PIP2), leading to the association of the protein to the membrane. The L/FRRG motif is essential for the cytoplasm to vacuole transport (Cvt) pathway, for the recruitment of atg8 and atg16 to the PAS in nutrient-rich medium, and for its recruitment to and dissociation from the PAS under starvation conditions. Belongs to the WD repeat PROPPIN family.