The N-Terminus of Vps74p Is Essential for the Retention of Glycosyltransferases in the Golgi but Not for the Modulation of Apical Polarized Growth in Saccharomyces cerevisiae

• Published in: PloS one Vol. 8; no. 9; p. e74715
• Main Authors: Hsu, Jia-Wei, Chang, Lin-Chun, Jang, Li-Ting, Huang, Chun-Fang, Lee, Fang-Jen S.
• Format: Journal Article
• Language: English
• Published: United States Public Library of Science 03.09.2013; Public Library of Science (PLoS)
• Subjects: Amino acids; Analysis; Biosynthesis; Carrier Proteins - chemistry; Carrier Proteins - metabolism; Carrier Proteins - physiology; Cdc34 protein; Cell cycle; Cell walls; Clonal deletion; Coat protein; Cyclin-dependent kinases; Elongation; Enzymes; Genes; Genetic analysis; Glycoproteins; Glycosyltransferase; Glycosyltransferases - metabolism; Golgi apparatus; Golgi Apparatus - enzymology; Homeostasis; Hypersensitivity; Kinases; Localization; Medicine; Modulation; Morphology; Mutation; N-Terminus; Phosphatases; Phosphorylation; Protein binding; Proteins; Rapamycin; Retention; Saccharomyces cerevisiae; Saccharomyces cerevisiae - enzymology; Saccharomyces cerevisiae - growth & development; Saccharomyces cerevisiae - metabolism; Saccharomyces cerevisiae Proteins - chemistry; Saccharomyces cerevisiae Proteins - metabolism; Saccharomyces cerevisiae Proteins - physiology; Sirolimus - pharmacology; Studies; Transferases; Yeast; Taiwan

Vps74p is a member of the PtdIns(4)P-binding protein family. Vps74p interacts with Golgi-resident glycosyltransferases and the coat protein COPI complex to modulate Golgi retention of glycosyltransferases and with the PtdIns(4)P phosphatase Sac1p to modulate PtdIns(4)P homeostasis at the Golgi. Gene...