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Ncr1p, the Yeast Ortholog of Mammalian Niemann Pick C1 Protein, is Dispensable for Endocytic Transport
Author(s) -
Zhang Shaochong,
Ren Jihui,
Li Hongzhe,
Zhang Qian,
Armstrong Jeffery S.,
Munn Alan L.,
Yang Hongyuan
Publication year - 2004
Publication title -
traffic
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.677
H-Index - 130
eISSN - 1600-0854
pISSN - 1398-9219
DOI - 10.1111/j.1600-0854.2004.00241.x
Subject(s) - endosome , endocytic cycle , biology , microbiology and biotechnology , endocytosis , npc1 , transport protein , vacuole , saccharomyces cerevisiae , vacuolar protein sorting , golgi apparatus , protein targeting , escrt , lysosome , vesicular transport proteins , yeast , biochemistry , membrane protein , intracellular , receptor , endoplasmic reticulum , membrane , enzyme , cytoplasm
The Niemann Pick C1 protein localizes to late endosomes and plays a key role in the intracellular transport of cholesterol in mammalian cells. Cholesterol and other lipids accumulate in a lysosomal or late endosomal compartment in cells lacking normal NPC1 function. Other than accumulation of lipids, defects in lysosomal retroendocytosis, sorting of a multifunctional receptor and endosomal movement have also been detected in NPC1 mutant cells. Ncr1p is an ortholog of NPC1 in the budding yeast Saccharomyces cerevisiae . In this study, we show that Ncr1p is a vacuolar membrane protein that transits through the biosynthetic vacuolar protein sorting pathway, and that it can be solubilized by Triton X‐100 at 4 °C. Using well‐established assays, we demonstrate that the absence of Ncr1p had no effect on fluid phase and receptor‐ mediated endocytosis, biosynthetic delivery to the vacuole, retrograde transport from endosome to Golgi and ubiquitin‐ and nonubiquitin‐dependent multivesicular body sorting. We conclude that Ncr1p does not have an essential role in known endocytic transport pathways in yeast.