ArticleThe Journal of biological chemistry2010
Site mapping and characterization of O-glycan structures on alpha-dystroglycan isolated from rabbit skeletal muscle.
Article in The Journal of biological chemistry, 2010. 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.
- From Glycocode to Precision Oncology: Therapeutic Strategies Targeting Aberrant O-GalNAc Glycosylation in Cancer.Chemical reviews · 2026Review
- Biosynthesis and Regulation of Laminin-Binding O-Mannosyl Glycans Related to Muscular Dystrophy.Advances in experimental medicine and biology · 2026Review
- LARGE1 processively polymerizes length-controlled matriglycan on prodystroglycan.Nature communications · 2025Article
- Exploring the In situ pairing of human galectins toward synthetic O-mannosylated core M1 glycopeptides of α-dystroglycan.Scientific reports · 2022Article
- Biosynthetic Mechanisms and Biological Significance of Glycerol Phosphate-Containing Glycan in Mammals.Molecules (Basel, Switzerland) · 2021Review
- The structure of POMGNT2 provides new insights into the mechanism to determine the functional O-mannosylation site on α-dystroglycan.Genes to cells : devoted to molecular & cellular mechanisms · 2021Article
- Contrasting the conformational effects of α-O-GalNAc and α-O-Man glycan protein modifications and their impact on the mucin-like region of alpha-dystroglycan.Glycobiology · 2021Article
- Crystal structures of β-1,4-N-acetylglucosaminyltransferase 2: structural basis for inherited muscular dystrophies.Acta crystallographica. Section D, Structural biology · 2021Article
- Separation and Identification of Permethylated Glycan Isomers by Reversed Phase NanoLC-NSI-MSMolecular & cellular proteomics : MCP · 2021Article
- Human UDP-galactose 4'-epimerase (GALE) is required for cell-surface glycome structure and function.The Journal of biological chemistry · 2020Article
- Laminin G-like domains: dystroglycan-specific lectins.Current opinion in structural biology · 2019Review
- Facile Chemoenzymatic Synthesis of O-Mannosyl Glycans.Angewandte Chemie (International ed. in English) · 2018Article
- Expression in retinal neurons of fukutin and FKRP, the protein products of two dystroglycanopathy-causative genes.Molecular vision · 2018Article
- Recent advancements in understanding mammalian O-mannosylation.Glycobiology · 2017Review
- MammalianThe Journal of biological chemistry · 2017Article
- ProteinThe Journal of biological chemistry · 2017Article
- Glycan susceptibility factors in autism spectrum disorders.Molecular aspects of medicine · 2016Review
- Carbohydrate-binding domain of the POMGnT1 stem region modulates O-mannosylation sites of α-dystroglycan.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Article
- Matriglycan: a novel polysaccharide that links dystroglycan to the basement membrane.Glycobiology · 2015Review
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Authors and funding
11 authors.
Funding
Abstract
The main extracellular matrix binding component of the dystrophin-glycoprotein complex, alpha-dystroglycan (alpha-DG), which was originally isolated from rabbit skeletal muscle, is an extensively O-glycosylated protein. Previous studies have shown alpha-DG to be modified by both O-GalNAc- and O-mannose-initiated glycan structures. O-Mannosylation, which accounts for up to 30% of the reported O-linked structures in certain tissues, has been rarely observed on mammalian proteins. Mutations in multiple genes encoding defined or putative glycosyltransferases involved in O-mannosylation are causal for various forms of congenital muscular dystrophy. Here, we explore the glycosylation of purified rabbit skeletal muscle alpha-DG in detail. Using tandem mass spectrometry approaches, we identify 4 O-mannose-initiated and 17 O-GalNAc-initiated structures on alpha-DG isolated from rabbit skeletal muscle. Additionally, we demonstrate the use of tandem mass spectrometry-based workflows to directly analyze glycopeptides generated from the purified protein. By combining glycomics and tandem mass spectrometry analysis of 91 glycopeptides from alpha-DG, we were able to assign 21 different residues as being modified by O-glycosylation with differing degrees of microheterogeneity; 9 sites of O-mannosylation and 14 sites of O-GalNAcylation were observed with only two sites definitively exhibiting occupancy by either type of glycan. The distribution of identified sites of O-mannosylation suggests a limited role for local primary sequence in dictating sites of attachment.
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