ArticleThe Journal of biological chemistry2011
A systematic study of site-specific GalNAc-type O-glycosylation modulating proprotein convertase processing.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 papers.
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Who cites it
59 citing papers in PubMed.
- CCHFV GP38 and GP85 interact with cell-surface glycosaminoglycans.Npj viruses · 2026Article
- Host Cell Proteases Involved in Human Respiratory Viral Infections and Their Inhibitors: A Review.Viruses · 2024Review
- SARS-CoV-2 Syncytium under the Radar: Molecular Insights of the Spike-Induced Syncytia and Potential Strategies to Limit SARS-CoV-2 Replication.Journal of clinical medicine · 2023Review
- Whole Exome-Wide Association Identifies Rare Variants inCancers · 2023Article
- O-Linked Sialoglycans Modulate the Proteolysis of SARS-CoV-2 Spike and Likely Contribute to the Mutational Trajectory in Variants of Concern.ACS central science · 2023Article
- In silico analysis of mutations near S1/S2 cleavage site in SARS-CoV-2 spike protein reveals increased propensity of glycosylation in Omicron strain.Journal of medical virology · 2022Article
- Reg-1α, a New Substrate of Calpain-2 Depending on Its Glycosylation Status.International journal of molecular sciences · 2022Article
- Furin cleavage of the SARS-CoV-2 spike is modulated byProceedings of the National Academy of Sciences of the United States of America · 2021Article
- The glycosylation in SARS-CoV-2 and its receptor ACE2.Signal transduction and targeted therapy · 2021Review
- Sclerostin Directly Stimulates Osteocyte Synthesis of Fibroblast Growth Factor-23.Calcified tissue international · 2021Article
- Furin cleavage of the SARS-CoV-2 spike is modulated by O-glycosylation.bioRxiv : the preprint server for biology · 2021Article
- N- and O-Glycosylation of the SARS-CoV-2 Spike Protein.Analytical chemistry · 2021Article
- Mucin-Type O-GalNAc Glycosylation in Health and Disease.Advances in experimental medicine and biology · 2021Article
- RNAi-Mediated Silencing of Pgants Shows Core 1Frontiers in physiology · 2021Article
- Global view of human protein glycosylation pathways and functions.Nature reviews. Molecular cell biology · 2020Review
- An atlas of O-linked glycosylation on peptide hormones reveals diverse biological roles.Nature communications · 2020Article
- Comparison of Severe Acute Respiratory Syndrome Coronavirus 2 Spike Protein Binding to ACE2 Receptors from Human, Pets, Farm Animals, and Putative Intermediate Hosts.Journal of virology · 2020Article
- O-glycan initiation directs distinct biological pathways and controls epithelial differentiation.EMBO reports · 2020Article
- G Protein-Coupled Receptors in the Sweet Spot: Glycosylation and other Post-translational Modifications.ACS pharmacology & translational science · 2020Review
- Galnt11 regulates kidney function by glycosylating the endocytosis receptor megalin to modulate ligand binding.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
Corrections and comments
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Authors and funding
8 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Site-specific GalNAc-type O-glycosylation is emerging as an important co-regulator of proprotein convertase (PC) processing of proteins. PC processing is crucial in regulating many fundamental biological pathways and O-glycans in or immediately adjacent to processing sites may affect recognition and function of PCs. Thus, we previously demonstrated that deficiency in site-specific O-glycosylation in a PC site of the fibroblast growth factor, FGF23, resulted in marked reduction in secretion of active unprocessed FGF23, which cause familial tumoral calcinosis and hyperostosis hyperphosphatemia. GalNAc-type O-glycosylation is found on serine and threonine amino acids and up to 20 distinct polypeptide GalNAc transferases catalyze the first addition of GalNAc to proteins making this step the most complex and differentially regulated steps in protein glycosylation. There is no reliable prediction model for O-glycosylation especially of isolated sites, but serine and to a lesser extent threonine residues are frequently found adjacent to PC processing sites. In the present study we used in vitro enzyme assays and ex vivo cell models to systematically address the boundaries of the region within site-specific O-glycosylation affect PC processing. The results demonstrate that O-glycans within at least ±3 residues of the RXXR furin cleavage site may affect PC processing suggesting that site-specific O-glycosylation is a major co-regulator of PC processing.
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