Current strategies for characterization of mucin- domain glycoproteins

Glycosylation, and especially O-linked glycosylation, remains a critical blind spot in the understanding of post-translational modifications. Due to their nature as proteins defined by a large density and abundance of O-glycosylation, mucins present extra challenges in the analysis of their structure and function. However, recent breakthroughs in multiple areas of research have rendered mucin-domain glycoproteins more accessible to current characterization techniques. In particular, the adaptation of mucinases to glycoproteomic workflows, the manipulation of cellular glycosylation pathways, and the advances in synthetic methods to more closely mimic mucin domains have introduced new and exciting avenues to study mucin glycoproteins. Here, we summarize recent developments in understanding the structure and biological function of mucin domains and their associated glycans, from glycoproteomic tools and visualization methods to synthetic glycopeptide mimetics.

Automated summary

Glycosylation, especially O-linked glycosylation, is still a blind spot in understanding post-translational modifications. Mucins, which are defined by a large density and abundance of O-glycosylation, present extra challenges in their analysis. However, recent breakthroughs in various areas have made mucin-domain glycoproteins more accessible for study. This includes the use of mucinases in glycoproteomic workflows, manipulation of cellular glycosylation pathways, and advances in synthetic methods to mimic mucin domains.