The Multifaceted Protein O-Glycosylation in Health and Disease

Dear Colleagues,

The scope of this Special Issue refers to the O-glycosylation of proteins in the broadest sense by including all structural and functional aspects of this multifaceted protein modification. About 10% of all proteins are reported to be modified by any of the various types of O-glycosidically linked chains. Accordingly, the term protein O-glycosylation covers not only the more abundant mucin-type O-glycosylation (O-GalNAc core-based), which is found on proteins following the secretory pathway, but also rare types, including other extracellular O-glycosylation types—such as O-fucosylation (O-Fuc), O-glucosylation (O-Glc), and O-mannosylation (O-Man)—and the unique nuclear–cytosolic O-glycosylation-type referred to as O-N-acetylglucosaminylation (O-GlcNAc). All types have in common that their core sugars are linked to the hydroxyl groups of serine or threonine; in rare cases, tyrosine is also known to be modified O-glycosidically. While mucin-type O-glycosylation is characterized by high structural complexity (at least six core structures are known) and oligosaccharide sizes can reach more than ten monosaccharide units, the other types are restricted in size and complexity or even confined to the level of a single sugar (O-GlcNAc). The structural heterogeneity of this type of protein modification is reflected through a multitude of functional aspects ranging from cellular functions (O-GalNAc glycans in sorting for targeted trafficking; O-Man glycans in cell–cell adhesion) to functions in innate immunity (O-GalNAc glycans or “blood group antigens” in the interaction of viral and bacterial pathogens with host epithelia and mucins) or to the regulation of protein activity (O-Fuc, O-Glc, and O-GlcNAc).

All contributions related to structural or functional aspects of this highly complex and heterogenous group of protein modifications are welcome, with particular emphasis on the pathways underlying cellular homeostasis under physiological conditions and those affected in disease.

Prof. Franz-Georg Hanisch
Guest Editor

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