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A dileucine‐like sorting signal directs transport into an AP‐3‐dependent, clathrin‐independent pathway to the yeast vacuole

Transport of yeast alkaline phosphatase (ALP) to the vacuole depends on the clathrin adaptor‐like complex AP‐3, but does not depend on proteins necessary for transport through pre‐vacuolar endosomes. We have identified ALP sequences that direct sorting into the AP‐3‐dependent pathway using chimeric proteins containing residues from the ALP cytoplasmic domain fused to sequences from a Golgi‐localized membrane protein, guanosine diphosphatase (GDPase). The full‐length ALP cytoplasmic domain, or ALP amino acids 1–16 separated from the transmembrane domain by a spacer, directed GDPase chimeric proteins from the Golgi complex to the vacuole via the AP‐3 pathway. Mutation of residues Leu13 and Val14 within the ALP cytoplasmic domain prevented AP‐3‐dependent vacuolar transport of both chimeric proteins and full‐length ALP. This Leucine–Valine (LV)‐based sorting signal targeted chimeric proteins and native ALP to the vacuole in cells lacking clathrin function. These results identify an LV‐based sorting signal in the ALP cytoplasmic domain that directs transport into a clathrin‐independent, AP‐3‐dependent pathway to the vacuole. The similarity of the ALP sorting signal to mammalian dileucine sorting motifs, and the evolutionary conservation of AP‐3 subunits, suggests that dileucine‐like signals constitute a core element for AP‐3‐dependent transport to lysosomal compartments in all eukaryotic cells.