Journal
TRENDS IN BIOCHEMICAL SCIENCES
Volume 43, Issue 4, Pages 269-284Publisher
ELSEVIER SCIENCE LONDON
DOI: 10.1016/j.tibs.2018.02.005
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Funding
- Neye Foundation
- Laege Sofus Carl Emil Friis og hustru Olga Doris Friis' Legat
- Lundbeck Foundation
- Independent Research Fund Denmark
- Novo Nordisk Foundation
- Danish National Research Foundation [DNRF107]
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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.
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