Molecular characterization of Vig4/Vrg4 GDP-mannose transporter of the yeast Saccharomyces cerevisiae

Abstract

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.