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Abstract
Glycosylation, or the addition of sugars to proteins, is a highly conserved protein
modification defined by both the monosaccharide initially attached to the protein
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.