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Citation
Zhang, L., Ten Hagen, K.G. (2019). O-Linked glycosylation in Drosophila melanogaster.  Curr. Opin. Struct. Biol. 56(): 139--145.
FlyBase ID
FBrf0243014
Publication Type
Review
Abstract

Glycosylation, or the addition of sugars to proteins, is a highly conserved protein modification defined by both the monosaccharide initially added as well as the amino acid to which it is attached. O-Linked glycosylation represents a diverse group of protein modifications occurring on the hydroxyl groups of serine and/or threonine residues. O-Glycosylation can have wide-ranging effects on protein stability and function, which translate into crucial consequences at the organismal level. This review will summarize structural and biological insights into the major O-glycans formed within the secretory apparatus (O-GalNAc, O-Man, O-Fuc, O-Glc and extracellular O-GlcNAc) from studies in the fruit fly Drosophila melanogaster. Drosophila has many advantages for investigating these complex modifications, boasting reduced functional redundancy within gene families, reduced length/complexity of glycan chains and sophisticated genetic tools. Gaining an understanding of the normal cellular and developmental roles of these conserved modifications in Drosophila will provide insight into how changes in O-glycans are involved in human disease and disease susceptibilities.

PubMed ID
PubMed Central ID
PMC6656608 (PMC) (EuropePMC)
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Secondary IDs
    Language of Publication
    English
    Additional Languages of Abstract
    Parent Publication
    Publication Type
    Compendium
    Abbreviation
    Curr. Opin. Struct. Biol.
    Title
    Current Opinion in Structural Biology
    Publication Year
    1991-
    ISBN/ISSN
    0959-440X
    Data From Reference