Proteomics

Dataset Information

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Global mapping of GalNAc-T isoform-specificities and O-glycosylation site-occupancy in a tissue-forming human cell line


ABSTRACT: Mucin-type-O-glycosylation on proteins is integrally involved in human health and disease and is coordinated by an enzyme family of 20 N-acetylgalactosaminyltransferases (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.

INSTRUMENT(S): Orbitrap Fusion Lumos, Orbitrap Fusion

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Keratinocyte, Skin

SUBMITTER: Mathias Ingemann Nielsen  

LAB HEAD: Hans H. Wandall

PROVIDER: PXD036791 | Pride | 2022-10-22

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
Nielsen_MSraw_Occupancy.zip Other
Nielsen_MSraw_TMT_DifferentialSecretomes.zip Other
Nielsen_MSraw_TMT_Glycoproteome.zip Other
Nielsen_MSraw_TMT_Proteome.zip Other
TableS7_MSdataSupportingTable.dat Other
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