Bridging the Gap between Glycosylation and Vesicle Traffic.
Bridging the Gap between Glycosylation and Vesicle Traffic.
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DOI：
10.3389/fcell.2016.00015
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发表时间：
2016
影响因子：
5.5
通讯作者：
Ungar D
中科院分区：
文献类型：
--
作者：
Fisher P;Ungar D
糖基化被认为是极其重要的翻译后修饰。装饰蛋白质和脂质的聚糖的结构很大程度上取决于高尔基体中发生的生物合成反应。这种生物合成依赖于糖基转移酶和糖苷酶的相对分布，这是由高尔基池之间的逆行囊泡运输维持的。融合前高尔基体上囊泡的束缚由 Rab GTPases、称为高尔金斯的卷曲螺旋束缚体和称为保守寡聚高尔基体 (COG) 复合体的多亚基束缚复合体调节。在这篇综述中，我们讨论了高尔基体囊泡束缚的机制，并强调了束缚在聚糖生物合成和一系列称为先天性糖基化障碍的疾病中的重要性。
Glycosylation is recognized as a vitally important posttranslational modification. The structure of glycans that decorate proteins and lipids is largely dictated by biosynthetic reactions occurring in the Golgi apparatus. This biosynthesis relies on the relative distribution of glycosyltransferases and glycosidases, which is maintained by retrograde vesicle traffic between Golgi cisternae. Tethering of vesicles at the Golgi apparatus prior to fusion is regulated by Rab GTPases, coiled-coil tethers termed golgins and the multisubunit tethering complex known as the conserved oligomeric Golgi (COG) complex. In this review we discuss the mechanisms involved in vesicle tethering at the Golgi apparatus and highlight the importance of tethering in the context of glycan biosynthesis and a set of diseases known as congenital disorders of glycosylation.