Phospholipid Flippases Lem3p-Dnf1p and Lem3p-Dnf2p Are Involved in the Sorting of the Tryptophan Permease Tat2p in Yeast

摘要: The type 4 P-type ATPases are flippases that generate phospholipid asymmetry in membranes. In budding yeast, heteromeric flippases, including Lem3p-Dnf1p and Lem3p-Dnf2p, translocate phospholipids to the cytoplasmic leaflet of Here, we report Lem3p-Dnf1/2p involved transport tryptophan permease Tat2p plasma membrane. lem3Δ mutant exhibited a requirement due mislocalization intracellular was relocalized membrane when trans-Golgi network (TGN)-to-endosome inhibited. Inhibition ubiquitination by mutations machinery also rerouted localized endosomal/TGN membranes addition Endocytosis mutants, which sequestered membrane, ubiquitination-dependent missorting Tat2p. These results suggest is ubiquitinated at TGN missorted vacuolar pathway mutant. NH2-terminal region containing acceptor lysines interacted with liposomes acidic phospholipids, phosphatidylserine. This interaction abrogated alanine substitution basic amino acids downstream sites. Interestingly, these substitutions manner. We propose following model based on results; not bound but if it dissociates from low level phosphatidylserine caused perturbation mutant, then transported vacuole. Background: Lem3p-Dnf2p yeast. Results: vacuole Conclusion: Phospholipid supports inhibiting its improper network. Significance: may be proper sorting proteins.