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Chemical precision tools to dissect protein glycosylation

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Chemical precision tools to dissect protein glycosylation
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28
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CC Attribution 4.0 International:
You are free to use, adapt and copy, distribute and transmit the work or content in adapted or unchanged form for any legal purpose as long as the work is attributed to the author in the manner specified by the author or licensor.
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Release Date2024
LanguageEnglish
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Production Year2024
Production PlaceFrankfurt am Main

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Abstract
The composition of glycoproteins is an undisputed corollary of their function. Understanding the glycoproteome in health and disease is paramount but hampered by the complexity of glycan modifications: hundreds of biosynthetic enzymes in the secretory pathway manifest the cell surface glyco-code. Interdependencies of these enzymes can impact the applicability of classical methods in molecular and cell biology, for instance through compensation or competition events. Here, I describe our work that complements approaches in molecular cell biology by generating chemical “precision tools” to understand the activities of individual glycosyltransferase enzymes. A key technology is the bump-and-hole tactic in which glycosyltransferases are engineered to accept a chemically modified, bulky nucleotide-sugar substrate. The tactic is applicable to living cells, allowing to trace protein glycosylation introduced in the secretory pathway by bioorthogonal chemistry. We have produced precision tools for a variety of glycosyltransferases, glycan subtypes, and cell types to shed light on the complexity of the secretory pathway.
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