ArticleMolecular & cellular proteomics : MCP2016
Mapping the O-Mannose Glycoproteome in Saccharomyces cerevisiae.
Article in Molecular & cellular proteomics : MCP, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.
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46 citing papers in PubMed.
- O-mannosylation of misfolded ER proteins promotes ERAD.The EMBO journal · 2026Article
- Structural characterisation of the fungal Pmt4 homodimer.Nature communications · 2025Article
- Pmt4 recognizes two separate acceptor sites to O-mannosylate in the S/T-rich regions of substrate proteins.Nature communications · 2025Article
- Structural Insights into the Protein Mannosyltransferase from Mycobacterium tuberculosis reveal a WW-Domain-Like Protein Motif in Bacteria.Communications biology · 2025Article
- Development of Supplements of Calcium Microencapsulated with Brewer's Spent Yeast Mannoproteins-Study of Gastrointestinal and Colonic Bioaccessibility.Foods (Basel, Switzerland) · 2025Article
- Proteomic Changes inJournal of proteome research · 2025Article
- Pervasive Divergence in Protein Thermostability is Mediated by Both Structural Changes and Cellular Environments.Molecular biology and evolution · 2025Article
- Potential ER tubular lumen sensing by intrinsically disordered regions.Journal of cell science · 2025Article
- Global View of Domain-Specific O-Linked Mannose Glycosylation in Glycoengineered Cells.Molecular & cellular proteomics : MCP · 2024Article
- A Yeast Modular Cloning (MoClo) Toolkit Expansion for Optimization of Heterologous Protein Secretion and Surface Display inACS synthetic biology · 2024Article
- A role for β-1,6- and β-1,3-glucans in kinetochore function in Saccharomyces cerevisiae.Genetics · 2024Article
- The SHDRA syndrome-associated geneProceedings of the National Academy of Sciences of the United States of America · 2023Article
- Sec16 and Sed4 interdependently function as interaction and localization partners at ER exit sites.Journal of cell science · 2023Article
- Industrial Production of Proteins withBiomolecules · 2023Review
- Article
- Pathway engineering facilitates efficient protein expression in Pichia pastoris.Applied microbiology and biotechnology · 2022Review
- Maximizing Depth of PTM Coverage: Generating Robust MS Datasets for Computational Prediction Modeling.Methods in molecular biology (Clifton, N.J.) · 2022Review
- What makes Komagataella phaffii non-conventional?FEMS yeast research · 2021Review
- Proteome plasticity in response to persistent environmental change.Molecular cell · 2021Article
- Article
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12 authors.
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Abstract
O-Mannosylation is a vital protein modification conserved from fungi to humans. Yeast is a perfect model to study this post-translational modification, because in contrast to mammalsO-mannosylation is the only type ofO-glycosylation. In an essential step toward the full understanding of proteinO-mannosylation we mapped theO-mannose glycoproteome in baker's yeast. Taking advantage of anO-glycan elongation deficient yeast strain to simplify sample complexity, we identified over 500O-glycoproteins from all subcellular compartments for which over 2300O-mannosylation sites were mapped by electron-transfer dissociation (ETD)-based MS/MS. In this study, we focus on the 293O-glycoproteins (over 1900 glycosylation sites identified by ETD-MS/MS) that enter the secretory pathway and are targets of ER-localized proteinO-mannosyltransferases. We find thatO-mannosylation is not only a prominent modification of cell wall and plasma membrane proteins, but also of a large number of proteins from the secretory pathway with crucial functions in protein glycosylation, folding, quality control, and trafficking. The analysis of glycosylation sites revealed thatO-mannosylation is favored in unstructured regions and β-strands. Furthermore,O-mannosylation is impeded in the proximity ofN-glycosylation sites suggesting the interplay of these types of post-translational modifications. The detailed knowledge of the target proteins and theirO-mannosylation sites opens for discovery of new roles of this essential modification in eukaryotes, and for a first glance on the evolution of different types ofO-glycosylation from yeast to mammals.
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