Analysis of glycoprotein quality control in the secretory pathway of fission yeast cells

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In both mammalian and yeast cells, proteins entering the secretory pathway adopt their final tertiary structure in the endoplasmic reticulum (ER). ER is the major organelle for folding of newly synthesized secretory proteins. A major regulator of this process is the quality control machinery, which retains and finally disposes of misfolded secretory proteins before they can exit the ER. The ER quality control process is highly conserved in eukaryotic cells, and are linked to a variety of diseases in mammalian cells. However, proteins required for the ER quality control system has not been analyzed and reported in the fission yeast Schizosaccharomyces pombe except UDP-glucose : glycoprotein glucosyltransferase. In this study, we studied proteins required for quality control mechanism of glycoprotein folding, and analyzed the glycosylation and processing of oligosaccharides in the ER in S. pombe cells.