Uncovering protein glycosylation dynamics and heterogeneity using deep quantitative glycoprofiling (DQGlyco)
Protein glycosylation regulates essential cellular processes such as signaling, adhesion and cell-cell interactions; however, dysregulated glycosylation is associated with diseases such as cancer. Here we introduce deep quantitative glycoprofiling (DQGlyco), a robust method that integrates high-thro...
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| Hauptverfasser: | , , , , , , , , |
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| Dokumenttyp: | Article (Journal) |
| Sprache: | Englisch |
| Veröffentlicht: |
10 February 2025
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| In: |
Nature structural & molecular biology
Year: 2025, Jahrgang: 32, Heft: 6, Pages: 1111-1126 |
| ISSN: | 1545-9985 |
| DOI: | 10.1038/s41594-025-01485-w |
| Online-Zugang: | Verlag, kostenfrei, Volltext: https://doi.org/10.1038/s41594-025-01485-w Verlag, kostenfrei, Volltext: https://www.nature.com/articles/s41594-025-01485-w 
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| Verfasserangaben: | Clément M. Potel, Mira Lea Burtscher, Martin Garrido-Rodriguez, Amber Brauer-Nikonow, Isabelle Becher, Cecile Le Sueur, Athanasios Typas, Michael Zimmermann & Mikhail M. Savitski |
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| 245 | 1 | 0 | |a Uncovering protein glycosylation dynamics and heterogeneity using deep quantitative glycoprofiling (DQGlyco) |c Clément M. Potel, Mira Lea Burtscher, Martin Garrido-Rodriguez, Amber Brauer-Nikonow, Isabelle Becher, Cecile Le Sueur, Athanasios Typas, Michael Zimmermann & Mikhail M. Savitski |
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| 520 | |a Protein glycosylation regulates essential cellular processes such as signaling, adhesion and cell-cell interactions; however, dysregulated glycosylation is associated with diseases such as cancer. Here we introduce deep quantitative glycoprofiling (DQGlyco), a robust method that integrates high-throughput sample preparation, highly sensitive detection and precise multiplexed quantification to investigate protein glycosylation dynamics at an unprecedented depth. Using DQGlyco, we profiled the mouse brain glycoproteome, identifying 177,198 unique N-glycopeptides—25 times more than previous studies. We quantified glycopeptide changes in human cells treated with a fucosylation inhibitor and characterized surface-exposed glycoforms. Furthermore, we analyzed tissue-specific glycosylation patterns in mice and demonstrated that a defined gut microbiota substantially remodels the mouse brain glycoproteome, shedding light on the link between the gut microbiome and brain protein functions. Additionally, we developed a novel strategy to evaluate glycoform solubility, offering new insights into their biophysical properties. Overall, the in-depth profiling offered by DQGlyco uncovered extensive complexity in glycosylation regulation. | ||
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