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Protein glycosylation, the covalent attachment of carbohydrates to amino acid side chains of proteins, is a ubiquitous post-translational modification across all branches of life. Due to many factors, including the vast structural complexity of glycans and the convoluted processes regulating their construction, protein glycosylation is a significantly understudied phenomenon. In particular, the study of protein O-glycosylation is limited because there exists no well-defined consensus sequence for its occurrence and the construction of O-glycosylated proteins in a controlled manner is often difficult. Recent years have seen many advances incorporating an interdisciplinary approach to this problem, and new chemical biology technologies have revealed many important discoveries. This review covers these recent advances with a focus on biosynthetic pathways, in vivo functions and the role of chemical biology in advancing our understanding of this important post-translational modification.

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