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Bridging the Gap between Glycosylation and Vesicle Traffic

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JournalFrontiers in cell and developmental biology
DateAccepted/In press - 22 Feb 2016
DatePublished (current) - 8 Mar 2016
Volume4
Number of pages12
Original languageEnglish

Abstract

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.

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©2016 Fisher and Ungar.

    Research areas

  • Golgi apparatus, glycan processing, COG complex, Congenital disorders of glycosylation, vesicle tethering

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