The VPS8 gene is required for localization and trafficking of the CPY sorting receptor in Saccharomyces cerevisiae.
AuthorsChen YJ, Stevens TH
JournalEur J Cell Biol
PubMed ID8864656
To better understand the process of protein sorting to the yeast vacuole, the VPS8 gene was identified and characterized. VPS8 encodes a membrane-associated hydrophilic protein of 135 kDa (Vps8p), which is required for the accurate sorting of the vacuolar hydrolase, carboxypeptidase Y (CPY). vps8 mutant cells missort and secrete CPY ... More
Cell growth-dependent coordination of lipid signaling and glycosylation is mediated by interactions between Sac1p and Dpm1p.
AuthorsFaulhammer F, Konrad G, Brankatschk B, Tahirovic S, Knödler A, Mayinger P
JournalJ Cell Biol
PubMed ID15657391
The integral membrane lipid phosphatase Sac1p regulates local pools of phosphatidylinositol-4-phosphate (PtdIns(4)P) at endoplasmic reticulum (ER) and Golgi membranes. PtdIns(4)P is important for Golgi trafficking, yet the significance of PtdIns(4)P for ER function is unknown. It also remains unknown how localization of Sac1p to distinct organellar membranes is mediated. Here, ... More
Ligand recognition and domain structure of Vps10p, a vacuolar protein sorting receptor in Saccharomyces cerevisiae.
AuthorsJørgensen MU, Emr SD, Winther JR
JournalEur J Biochem
PubMed ID10095782
Vp10p is a receptor that sorts several different vacuolar proteins by cycling between a late Golgi compartment and the endosome. The cytoplasmic tail of Vps10p is necessary for the recycling, whereas the lumenal domain is predicted to interact with the soluble ligands. We have studied ligand binding to Vps10p by ... More
Vps10p cycles between the late-Golgi and prevacuolar compartments in its function as the sorting receptor for multiple yeast vacuolar hydrolases.
AuthorsCooper AA, Stevens TH
JournalJ Cell Biol
PubMed ID8636229
VPS10 (Vacuolar Protein Sorting) encodes a large type I transmembrane protein (Vps10p), involved in the sorting of the soluble vacuolar hydrolase carboxypeptidase Y (CPY) to the Saccharomyces cerevisiae lysosome-like vacuole. Cells lacking Vps10p missorted greater than 90% CPY and 50% of another vacuolar hydrolase, PrA, to the cell surface. In ... More
Retrieval of resident late-Golgi membrane proteins from the prevacuolar compartment of Saccharomyces cerevisiae is dependent on the function of Grd19p.
AuthorsVoos W, Stevens TH
JournalJ Cell Biol
PubMed ID9456318
The dynamic vesicle transport processes at the late-Golgi compartment of Saccharomyces cerevisiae (TGN) require dedicated mechanisms for correct localization of resident membrane proteins. In this study, we report the identification of a new gene, GRD19, involved in the localization of the model late-Golgi membrane protein A-ALP (consisting of the cytosolic ... More
A membrane coat complex essential for endosome-to-Golgi retrograde transport in yeast.
AuthorsSeaman MN, McCaffery JM, Emr SD
JournalJ Cell Biol
PubMed ID9700157
We have recently characterized three yeast gene products (Vps35p, Vps29p, and Vps30p) as candidate components of the sorting machinery required for the endosome-to-Golgi retrieval of the vacuolar protein sorting receptor Vps10p (Seaman, M.N.J., E.G. Marcusson, J.-L. Cereghino, and S.D. Emr. 1997. J. Cell Biol. 137:79-92). By genetic and biochemical means ... More
A screen for genes of heme uptake identifies the FLC family required for import of FAD into the endoplasmic reticulum.
AuthorsProtchenko O, Rodriguez-Suarez R, Androphy R, Bussey H, Philpott CC
JournalJ Biol Chem
PubMed ID16717099
Although Candida albicans and Saccharomyces cerevisiae express very similar systems of iron uptake, these species differ in their capacity to use heme as a nutritional iron source. Whereas C. albicans efficiently takes up heme, S. cerevisiae grows poorly on media containing heme as the sole source of iron. We identified ... More