Glycosylation Quality Control by the Golgi Structure.

Glycosylation Quality Control by the Golgi Structure.
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DOI:
10.1016/j.jmb.2016.02.030
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发表时间:
2016-08-14
影响因子:
5.6
通讯作者:
Wang Y
Wang Y
中科院分区:
生物学2区
文献类型:
--
作者:
Zhang X;Wang Y

文献摘要

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糖基化是一种普遍存在的修饰,发生在所有活细胞中的蛋白质和脂质上。与其高度复杂性一致,聚糖在蛋白质质量控制和识别事件中发挥着至关重要的生物学作用。天冬酰胺连接蛋白N-糖基化是最复杂的糖基化,起始于内质网(ER),并在高尔基体中成熟。这一过程不仅需要糖基转移酶、糖苷酶和核苷酸糖转运蛋白等加工机械的准确分布,还需要一个高效、组织良好的工厂负责糖链加工的保真度和质量控制。此外,准确的糖基化必须与蛋白质运输和分选协调进行。这些活动是由高尔基体进行的,高尔基体是分泌途径中心的膜细胞器。为了完成这些任务,高尔基体已经发展成一种独特的堆叠结构,紧密排列的扁平池,高尔基体酶驻留在其中;在哺乳动物细胞中,数十个高尔基体堆叠通常横向连接成带状结构。在这里,我们回顾了我们目前的知识,高尔基体结构是如何形成的,为什么它的形成是需要准确的糖基化,重点是如何的高尔基体堆积因子GRASP 55和GRASP 65产生的高尔基体结构和保守的寡聚体高尔基体(COG)复杂的保持高尔基体酶在不同的高尔基体亚室通过逆行蛋白质运输。
Glycosylation is a ubiquitous modification that occurs on proteins and lipids in all living cells. Consistent with their high complexity, glycans play crucial biological roles in protein quality control and recognition events. Asparagine-linked protein N-glycosylation, the most complex glycosylation, initiates in the endoplasmic reticulum (ER) and matures in the Golgi apparatus. This process not only requires an accurate distribution of processing machineries, such as glycosyltransferases, glycosidases and nucleotide sugar transporters, but also needs an efficient and well-organized factory that is responsible for the fidelity and quality control of sugar chain processing. In addition, accurate glycosylation must occur in coordination with protein trafficking and sorting. These activities are carried out by the Golgi apparatus, a membrane organelle in the center of the secretory pathway. To accomplish these tasks, the Golgi has developed into a unique stacked structure of closely aligned flattened cisternae in which Golgi enzymes reside; in mammalian cells, dozens of Golgi stacks are often laterally linked into a ribbon-like structure. Here, we review our current knowledge of how the Golgi structure is formed and why its formation is required for accurate glycosylation, with the focus of how the Golgi stacking factors GRASP55 and GRASP65 generate the Golgi structure and how the conserved oligomeric Golgi (COG) complex maintains Golgi enzymes in different Golgi subcompartments by retrograde protein trafficking.