Analysis of site-specific N-glycan remodeling in the endoplasmic reticulum and the Golgi
Analysis of site-specific N-glycan remodeling in the endoplasmic reticulum and the Golgi
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DOI：
10.1093/glycob/cwv058
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发表时间：
2015-12-01
期刊：
影响因子：
4.3
通讯作者：
Aebi, Markus
中科院分区：
文献类型：
--
作者：
Hang, Ivan;Lin, Chia-wei;Aebi, Markus
N-连接蛋白糖基化的标志是在分泌途径中产生不同的聚糖结构。内质网和高尔基体中N-聚糖重塑的动态、非模板驱动的过程为结构多样性提供了细胞环境。我们应用新开发的基于质谱的分析来量化昆虫细胞中表达的模型蛋白Pdi 1 p的位点特异性N-聚糖重塑。分子动力学模拟、突变分析、体外加工事件的动力学研究和聚糖通量分析支持蛋白质在N-聚糖加工中的定义作用。
The hallmark of N-linked protein glycosylation is the generation of diverse glycan structures in the secretory pathway. Dynamic, non-template-driven processes of N-glycan remodeling in the endoplasmic reticulum and the Golgi provide the cellular setting for structural diversity. We applied newly developed mass spectrometry-based analytics to quantify site-specific N-glycan remodeling of the model protein Pdi1p expressed in insect cells. Molecular dynamics simulation, mutational analysis, kinetic studies of in vitro processing events and glycan flux analysis supported the defining role of the protein in N-glycan processing.