Journal
NATURE COMMUNICATIONS
Volume 13, Issue 1, Pages -Publisher
NATURE PORTFOLIO
DOI: 10.1038/s41467-022-33806-8
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Funding
- European Research Council (ERC) under the European Union's Horizon 2020 research and innovation programme (GlycoSkin H2020-ERC) [772735]
- European Commission
- Lundbeck Foundation [R313-2019-869]
- Danish National Research Foundation [DNRF107]
- National Science Foundation
- Neye Foundation
- Friis Foundation
- Michelsen Foundation
- A.P. MOller og Hustru Chastine McKinney MOllers Fond til Almene Formaal
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This study systematically analyzed the isoform-specific targets of all GalNAc-Ts expressed in skin cells, revealing the biological effects of O-glycan initiation on epithelial formation. Over 300 unique glycosylation sites were identified on a diverse set of proteins, regulated by specific GalNAc-T isoforms, highlighting their impact on tissue phenotypes. The variability in O-glycosylation site-occupancy of secreted proteins suggests the importance of individual O-glycosylation sites in driving biological functions.
Mucin-type-O-glycosylation on proteins is integrally involved in human health and disease and is coordinated by an enzyme family of 20 N-acetyl-galactosaminyltransferases (GalNAc-Ts). Detailed knowledge on the biological effects of site-specific O-glycosylation is limited due to lack of information on specific glycosylation enzyme activities and O-glycosylation site-occupancies. Here we present a systematic analysis of the isoform-specific targets of all GalNAc-Ts expressed within a tissue-forming human skin cell line, and demonstrate biologically significant effects of O-glycan initiation on epithelial formation. We find over 300 unique glycosylation sites across a diverse set of proteins specifically regulated by one of the GalNAc-T isoforms, consistent with their impact on the tissue phenotypes. Notably, we discover a high variability in the O-glycosylation site-occupancy of 70 glycosylated regions of secreted proteins. These findings revisit the relevance of individual O-glycosylation sites in the proteome, and provide an approach to establish which sites drive biological functions.
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