{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["110(52)"],"submitter":["Vester-Christensen MB"],"pubmed_abstract":["The metazoan O-mannose (O-Man) glycoproteome is largely unknown. It has been shown that up to 30% of brain O-glycans are of the O-Man type, but essentially only alpha-dystroglycan (α-DG) of the dystrophin-glycoprotein complex is well characterized as an O-Man glycoprotein. Defects in O-Man glycosylation underlie congenital muscular dystrophies and considerable efforts have been devoted to explore this O-glycoproteome without much success. Here, we used our SimpleCell strategy using nuclease-mediated gene editing of a human cell line (MDA-MB-231) to reduce the structural heterogeneity of O-Man glycans and to probe the O-Man glycoproteome. In this breast cancer cell line we found that O-Man glycosylation is primarily found on cadherins and plexins on β-strands in extracellular cadherin and Ig-like, plexin and transcription factor domains. The positions and evolutionary conservation of O-Man glycans in cadherins suggest that they play important functional roles for this large group of cell adhesion glycoproteins, which can now be addressed. The developed O-Man SimpleCell strategy is applicable to most types of cell lines and enables proteome-wide discovery of O-Man protein glycosylation."],"journal":["Proceedings of the National Academy of Sciences of the United States of America"],"pagination":["21018-23"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC3876253"],"repository":["biostudies-literature"],"pubmed_title":["Mining the O-mannose glycoproteome reveals cadherins as major O-mannosylated glycoproteins."],"pmcid":["PMC3876253"],"pubmed_authors":["Vester-Christensen MB","Halim A","Joshi HJ","Steentoft C","Bennett EP","Vakhrushev SY","Clausen H","Levery SB"],"additional_accession":[]},"is_claimable":false,"name":"Mining the O-mannose glycoproteome reveals cadherins as major O-mannosylated glycoproteins.","description":"The metazoan O-mannose (O-Man) glycoproteome is largely unknown. It has been shown that up to 30% of brain O-glycans are of the O-Man type, but essentially only alpha-dystroglycan (α-DG) of the dystrophin-glycoprotein complex is well characterized as an O-Man glycoprotein. Defects in O-Man glycosylation underlie congenital muscular dystrophies and considerable efforts have been devoted to explore this O-glycoproteome without much success. Here, we used our SimpleCell strategy using nuclease-mediated gene editing of a human cell line (MDA-MB-231) to reduce the structural heterogeneity of O-Man glycans and to probe the O-Man glycoproteome. In this breast cancer cell line we found that O-Man glycosylation is primarily found on cadherins and plexins on β-strands in extracellular cadherin and Ig-like, plexin and transcription factor domains. The positions and evolutionary conservation of O-Man glycans in cadherins suggest that they play important functional roles for this large group of cell adhesion glycoproteins, which can now be addressed. The developed O-Man SimpleCell strategy is applicable to most types of cell lines and enables proteome-wide discovery of O-Man protein glycosylation.","dates":{"release":"2013-01-01T00:00:00Z","publication":"2013 Dec","modification":"2026-05-03T23:34:36.631Z","creation":"2026-04-07T19:50:21.367Z"},"accession":"S-EPMC3876253","cross_references":{"pubmed":["24101494"],"doi":["10.1073/pnas.1313446110"]}}