Fine-Tuning Limited Proteolysis: A Major Role for Regulated Site-Specific O-Glycosylation
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Limited proteolytic processing is an essential and ubiquitous post-translational modification (PTM) affecting secreted proteins; failure to regulate the process is often associated with disease. Glycosylation is also a ubiquitous protein PTM and site-specific O-glycosylation in close proximity to sites of proteolysis can regulate and direct the activity of proprotein convertases, a disintegrin and metalloproteinases (ADAMs), and metalloproteinases affecting the activation or inactivation of many classes of proteins, including G-protein-coupled receptors (GPCRs). Here, we summarize the emerging data that suggest O-glycosylation to be a key regulator of limited proteolysis, and highlight the potential for crosstalk between multiple PTMs.
Original language | English |
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Journal | Trends in Biochemical Sciences |
Volume | 43 |
Issue number | 4 |
Pages (from-to) | 269-284 |
Number of pages | 16 |
ISSN | 0968-0004 |
DOIs | |
Publication status | Published - 2018 |
- G-protein-coupled receptors, GalNAc-Ts, O-glycosylation, proteases, proteolytic processing, PTM
Research areas
ID: 195255835