Novel membrane protein complexes for protein glycosylation in the yeast Golgi apparatus

Biochemical and Biophysical Research Communications
H Hashimoto, Koji Yoda

Abstract

Three type II membrane proteins Anp1, Van1 and Mnn9 of Saccharomyces cerevisiae share significant sequence homology. Their precise biochemical activity has long been unknown though the mutant phenotype indicates their participation in protein glycosylation in the Golgi apparatus. To shed light on their molecular characteristics, interactions of these proteins were studied by immunoprecipitation after solubilizing the membrane by nonionic detergent. Our results indicated that there are at least two submembrane complexes containing these proteins: one contains Van1 and Mnn9 proteins and the other contains Anp1 and Mnn9 proteins. In addition, Hoc1 protein which has significant homology to Och1 protein colocalized with Anp1 and Mnn9 proteins. These complexes with similar but partially different constituents may represent essential parts of glycosylation machinery in the yeast Golgi compartments.

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Citations

Oct 20, 2005·Journal of Bioscience and Bioengineering·K Yoda, Y Noda
May 22, 2008·Genetics·Weimin PengSiavash K Kurdistani
Mar 9, 2013·Bioscience, Biotechnology, and Biochemistry·Yoichi Noda, Koji Yoda
Mar 3, 2009·Protein Expression and Purification·Dmitry RodionovAnnette Herscovics
Oct 16, 2013·Molecular Microbiology·Rebecca A Hall, Neil A R Gow
Mar 9, 1999·Neurobiology of Disease·S E Mole
Feb 26, 1999·The Journal of Biological Chemistry·J JungmannS Munro
Feb 1, 2019·The Journal of General and Applied Microbiology·Yuuki TanabeYoichi Noda
Mar 8, 2019·The Journal of General and Applied Microbiology·Yoichi NodaKoji Yoda
May 24, 2006·The Journal of Biological Chemistry·Olga ProtchenkoCaroline C Philpott
Jul 12, 2020·Journal of Bioscience and Bioengineering·Takao OhashiKaoru Takegawa
Jan 8, 1999·Biochimica Et Biophysica Acta·N Dean
Aug 21, 2002·Journal of Cell Science·Yoichi KosodoKoji Yoda

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