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Molecular characterization of Vig4/Vrg4 GDP‐mannose transporter of the yeast Saccharomyces cerevisiae
Author(s) -
Abe Masato,
Hashimoto Hitoshi,
Yoda Koji
Publication year - 1999
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(99)01177-1
Subject(s) - golgi apparatus , saccharomyces cerevisiae , endoplasmic reticulum , mannose , biochemistry , yeast , secretory pathway , copi , transport protein , transmembrane protein , immunoprecipitation , protein targeting , membrane protein , chemistry , mutant , microbiology and biotechnology , biology , membrane , gene , receptor
Saccharomyces cerevisiae Vig4/Vrg4 protein is a Golgi membrane protein which has multiple transmembrane domains and is essential for transport of GDP‐mannose across the Golgi membrane. By immunoprecipitation of detergent‐solubilized tagged protein, we found that this protein exists as oligomer. Two mutants vig4‐1 and vig4‐2 had amino acid substitutions in the C‐terminal region, Ala286Val and Ser278Cys, respectively. In accord with these mutations, trimming of the C‐terminal hydrophobic part close to the region impaired the function and traffic of the proteins from the endoplasmic reticulum to the Golgi compartments.