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

在哺乳动物和酵母细胞中，进入分泌途径的蛋白质在内质网（ER）中采用其最终三级结构。ER是新合成分泌蛋白折叠的主要细胞器。这一过程的主要调节器是质量控制机制，其保留并最终在错误折叠的分泌蛋白可以离开ER之前处理它们。ER质量控制过程在真核细胞中高度保守，并且与哺乳动物细胞中的多种疾病相关。然而，ER质量控制系统所需的蛋白质还没有分析和报告，在裂殖酵母裂殖酵母除了UDP-葡萄糖：糖蛋白葡萄糖基转移酶。本研究对糖蛋白折叠质量控制机制所需的蛋白质进行了研究，并分析了S.粟酒裂殖酵母细胞

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.