Department of Biology, University of York York, UK.
Front Cell Dev Biol. 2016 Mar 8;4:15. doi: 10.3389/fcell.2016.00015. eCollection 2016.
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.
糖基化被认为是一种至关重要的翻译后修饰。糖蛋白和糖脂上的聚糖结构在很大程度上由高尔基体中发生的生物合成反应决定。这种生物合成依赖于糖基转移酶和糖苷酶的相对分布，而这种分布是通过高尔基体潴腔之间的逆行囊泡运输来维持的。囊泡在融合前在高尔基体上的附着是由 Rab GTPases、卷曲螺旋 tether 蛋白（称为 golgins）和多亚基 tethering 复合物（即保守寡聚高尔基体（COG）复合物）调节的。在这篇综述中，我们讨论了高尔基体上囊泡附着的机制，并强调了在聚糖生物合成和一组称为先天性糖基化障碍的疾病背景下，附着的重要性。
