It was known that the uptake of @entity2340 is reduced in the @entity375 @entity46120 mutant, which is defective in a late step of @entity12364 biosynthesis. Here, we show that this is because the high affinity @entity2340 permease @entity53241 is not targeted to the plasma membrane. In wild-type cells, the plasma membrane localization of @entity53241 is regulated by the external @entity2340 concentration. @entity53241 is transported from the Golgi apparatus to the vacuole at high @entity2340 , and to the plasma membrane at low @entity2340 . However, in the @entity46120 mutant, @entity53241 is missorted to the vacuole at low @entity2340 . The plasma membrane targeting of @entity53241 is dependent on detergent-insoluble membrane domains, suggesting that @entity5068 affects the sorting through the organization of lipid rafts. The @entity46120 mutation also caused missorting to the multivesicular body pathway in late endosomes. Thus, @entity5068 composition is crucial for protein sorting late in the secretory pathway. @entity53241 is subject to polyubiquitination, which acts as a vacuolar-targeting signal, and the inhibition of this process suppresses the @entity53241 sorting defects of the @entity46120 mutant. The sorting mechanisms of @entity53241 that depend on both @entity5068 and ubiquitin will be discussed.

XXXX is required for targeting of @entity2340 permease to the @entity375 plasma membrane.

@entity12364 :: ('MESH:D004875', 'Chemical') :: ['ergosterol'] @entity46120 :: ('855003(Tax:4932)', 'Gene') :: ['erg6'] @entity2340 :: ('CHEBI:27897', 'Chemical') :: ['tryptophan'] @entity5068 :: ('CHEBI:15889', 'Chemical') :: ['sterol'] @entity375 :: ('4932', 'Species') :: ['yeast'] @entity53241 :: ('854139(Tax:4932)', 'Gene') :: ['Tat2p']
@entity12364 :: (MESH:D004875,Chemical) :: ['Ergosterol']
