This chapter focuses on less-easily categorized types of glycan linkages that occur on certain proteins or domains. O-linked sugars on epidermal growth factor (EGF)-like repeats (O-fucose, O-glucose, and O-GlcNAc) regulate Notch signaling and the functions of several other proteins. O-Fucosylation of thrombospondin type-1 repeats (TSRs) is required for folding of these domains in a number of secreted matricellular proteins. O-mannosylation of α-dystroglycan is essential for interactions with several extracellular matrix (ECM) proteins. Defects in the glycosyltransferases that add these glycans (O-fucose, O-glucose, O-GlcNAc, and O-mannose) result in human diseases. C-Mannosylation is a unique form of glycosylation in which mannose is linked through a carbon–carbon bond to tryptophan. O-Linked Glc-Gal disaccharides are added to hydroxylysine residues and play an important role in collagen fibril formation. Although the glycans described here are found on relatively few glycoproteins, they play specific and important roles in biology.
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