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）中采用其最终的三级结构。内质网是折叠新合成的分泌蛋白的主要细胞器。这一过程的主要调节者是质量控制机制，它在错误折叠的分泌蛋白离开内质网之前保留并最终处理掉它们。内质网质量控制过程在真核细胞中高度保守，并与哺乳动物细胞中的多种疾病有关。然而，裂变酵母Schizosaccharomyces pombe中除了糖蛋白葡萄糖基转移酶（UDP-glucose: glycoprotein glucosyltransferase）外，尚未对ER质量控制系统所需的蛋白质进行分析和报道。在本研究中，我们研究了糖蛋白折叠的质量控制机制所需的蛋白质，并分析了S. pombe细胞内质网中低聚糖的糖基化和加工。

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.