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Pep12p is a Multifunctional Yeast Syntaxin that Controls Entry of Biosynthetic, Endocytic and Retrograde Traffic into the Prevacuolar Compartment
Author(s) -
Gerrard Sonja R.,
Levi Boaz P.,
Stevens Tom H.
Publication year - 2000
Publication title -
traffic
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.677
H-Index - 130
eISSN - 1600-0854
pISSN - 1398-9219
DOI - 10.1034/j.1600-0854.2000.010308.x
Subject(s) - syntaxin , vacuole , endocytic cycle , endosome , biology , microbiology and biotechnology , saccharomyces cerevisiae , retromer , yeast , compartment (ship) , biochemistry , endocytosis , membrane protein , cytoplasm , receptor , membrane , oceanography , geology , intracellular
Delivery of proteins to the vacuole of the yeast Saccharomyces cerevisiae requires the function of the endosomal syntaxin, Pep12p. Many vacuolar proteins, such as the soluble vacuolar hydrolase, carboxypeptidase Y (CPY), traverse the prevacuolar compartment (PVC) en route to the vacuole. Here we show that deletion of the carboxy‐terminal transmembrane domain of Pep12p results in a temperature‐conditional block in transport of CPY to the PVC. The PVC also receives traffic from the early endosome and the vacuole, and mutation in PEP12 also blocks these other trafficking pathways into the PVC. Therefore, Pep12p is a multifunctional syntaxin that is required for all known trafficking pathways into the yeast PVC. Finally, we found that the internalized pheromone receptor, Ste3p, can cycle out of the PVC in a VPS27 ‐independent fashion.