Both Svp 26 and Mnn 6 are required for the efficient ER exit of Mnn 4 in Saccharomyces cerevisiae

N-glycans are important for the folding process of newly synthesized proteins and for their solubility and stability (Aebi et al., 2010). At the cell surface where glycosylated proteins are exposed to the cell exterior, they have a protective function and an important role in recognition by other cells. S. cerevisiae has two types of N-glycans (Munro, 2001). ‘Core type’ is composed of a structure built in the ER and a few mannoses extended at the early Golgi and is found on the proteins destined for the internal organelles. ER type glycan is further elongated with a1,6-linked mannoses by the sequential actions of Och1, mannan-polymerase I (M-Pol I) and mannan-polymerase II (M-Pol II) protein complexes to build a large ‘mannan’ structure (Stolz and Munro, 2002). This long a-1,6-linked backbone is further branched with a-1,2-mannoses by Mnn2 and Mnn5, (Rayner and Munro, 1998) and a-1,3mannoses by Mnn1 (Romero et al., 1999; Wiggins and Munro, 1998). Mannan is usually found in the cell wall proteins and secreted proteins. A mechanism by which one of these two types of glycan is selectively added to a certain protein is not yet fully understood. To some of the Both Svp26 and Mnn6 are required for the efficient ER exit of Mnn4 in Saccharomyces cerevisiae

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