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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Article Synopsis
- Glycosyltransferases are primarily type II membrane proteins with a small cytosolic tail that need proper localization to the Golgi apparatus, and in S. cerevisiae, Gpp74p helps facilitate this.
- In the study with S. pombe, researchers found that the gpp74 gene is crucial for the localization of some glycosyltransferases to the Golgi, as its deletion led to these proteins being incorrectly sorted to vacuoles.
- The research also showed that the localization of Gpp74p to the Golgi relies on the SpPik1p protein, and that the cytosolic tails of certain glycosyltransferases play a significant role in their proper targeting.
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