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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: Potel, Clément M. (VerfasserIn) , Burtscher, Mira Lea (VerfasserIn) , Garrido-Rodriguez, Martin (VerfasserIn) , Brauer-Nikonow, Amber (VerfasserIn) , Becher, Isabelle (VerfasserIn) , Le Sueur, Cecile (VerfasserIn) , Typas, Athanasios (VerfasserIn) , Zimmermann, Michael (VerfasserIn) , Savitski, Mikhail M. (VerfasserIn)
Dokumenttyp: Article (Journal)
Sprache:Englisch
Veröffentlicht: 10 February 2025
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
Volltext
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
Beschreibung
Zusammenfassung: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.
Beschreibung:Gesehen am 25.07.2025
Beschreibung:Online Resource
ISSN:1545-9985
DOI:10.1038/s41594-025-01485-w

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