ArticleProceedings of the National Academy of Sciences of the United States of America2015
Discovery of a nucleocytoplasmic O-mannose glycoproteome in yeast.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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Who cites it
35 citing papers in PubMed, 64 citations in OpenAlex.
- Mass Spectrometry-Based Proteomics Methods for Systematic Identification and Quantification of Protein O-Glycosylation in Complex Biological Samples.Journal of the American Society for Mass Spectrometry · 2026Review
- Computational origins of cortical brain circuits for social cognition.Nature reviews. Neuroscience · 2026Review
- Production Technologies for Recombinant Antibodies: Insights into Eukaryotic, Prokaryotic, and Transgenic Expression Systems.Biochemical genetics · 2025Review
- A role for β-1,6- and β-1,3-glucans in kinetochore function in Saccharomyces cerevisiae.Genetics · 2024Article
- Molecular-level architecture of Chlamydomonas reinhardtii's glycoprotein-rich cell wall.Nature communications · 2024Article
- Silencing GMPPB Inhibits the Proliferation and Invasion of GBM via Hippo/MMP3 Pathways.International journal of molecular sciences · 2023Article
- Protein O-GlcNAcylation and the regulation of energy homeostasis: lessons from knock-out mouse models.Journal of biomedical science · 2022Review
- O-GlcNAc modification of nuclear pore complexes accelerates bidirectional transport.The Journal of cell biology · 2021Article
- Detection and Analysis of Proteins Modified by O-Linked N-Acetylglucosamine.Current protocols · 2021Article
- DrosophilaCells · 2021Article
- Role ofPhysiological reviews · 2021Review
- Comparison ofACS chemical biology · 2021Article
- Glycomics, Glycoproteomics, and Glycogenomics: An Inter-Taxa Evolutionary Perspective.Molecular & cellular proteomics : MCP · 2021Review
- Meta-heterogeneity: Evaluating and Describing the Diversity in Glycosylation Between Sites on the Same Glycoprotein.Molecular & cellular proteomics : MCP · 2021Review
- The O-GlcNAc Modification on Kinases.ACS chemical biology · 2020Article
- The formation of hybrid complexes between isoenzymes of glyceraldehyde-3-phosphate dehydrogenase regulates its aggregation state, the glycolytic activity and sphingolipid status in Saccharomyces cerevisiae.Microbial biotechnology · 2020Article
- ProteinParasitology · 2019Review
- Recent advances in mass spectrometry (MS)-based glycoproteomics in complex biological samples.Trends in analytical chemistry : TRAC · 2019Article
- Global and site-specific analysis of protein glycosylation in complex biological systems with Mass Spectrometry.Mass spectrometry reviews · 2019Review
- Nucleocytoplasmic O-glycosylation in protists.Current opinion in structural biology · 2019Review
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Dynamic cycling of N-Acetylglucosamine (GlcNAc) on serine and threonine residues (O-GlcNAcylation) is an essential process in all eukaryotic cells except yeast, including Saccharomyces cerevisiae and Schizosaccharomyces pombe. O-GlcNAcylation modulates signaling and cellular processes in an intricate interplay with protein phosphorylation and serves as a key sensor of nutrients by linking the hexosamine biosynthetic pathway to cellular signaling. A longstanding conundrum has been how yeast survives without O-GlcNAcylation in light of its similar phosphorylation signaling system. We previously developed a sensitive lectin enrichment and mass spectrometry workflow for identification of the human O-linked mannose (O-Man) glycoproteome and used this to identify a pleothora of O-Man glycoproteins in human cell lines including the large family of cadherins and protocadherins. Here, we applied the workflow to yeast with the aim to characterize the yeast O-Man glycoproteome, and in doing so, we discovered hitherto unknown O-Man glycosites on nuclear, cytoplasmic, and mitochondrial proteins in S. cerevisiae and S. pombe. Such O-Man glycoproteins were not found in our analysis of human cell lines. However, the type of yeast O-Man nucleocytoplasmic proteins and the localization of identified O-Man residues mirror that of the O-GlcNAc glycoproteome found in other eukaryotic cells, indicating that the two different types of O-glycosylations serve the same important biological functions. The discovery opens for exploration of the enzymatic machinery that is predicted to regulate the nucleocytoplasmic O-Man glycosylations. It is likely that manipulation of this type of O-Man glycosylation will have wide applications for yeast bioprocessing.
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