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Membrane glycoproteins get another go: the GlycoSwitch
Ludger Johannes1, Roberto Weigert2, Christian Wunder1
1Institut Curie, Université PSL, U1143 INSERM, UMR3666 CNRS, Cellular and Chemical Biology unit, Paris, France; Inria Center at University of Rennes, SAIRPICO Team, U1143 INSERM, Institut Curie, Cellular and Chemical Biology Unit, Paris, France.
Trends in Cell Biology
|October 31, 2025
Summary
Cell surface glycans are dynamic, not static. A newly discovered GlycoSwitch pathway uses sialic acid removal to send membrane proteins back to the Golgi, regulating cellular functions.
Area of Science:
- Cell Biology
- Glycobiology
- Molecular Biology
Background:
- Cell surface glycans on glycoproteins and lipids were traditionally considered static.
- Recent research indicates dynamic glycan remodeling can occur.
Purpose of the Study:
- To review glycosylation processes, focusing on terminal sialic acid-capped glycans.
- To discuss the role of galectin family proteins in glycan binding.
- To highlight the GlycoSwitch pathway's impact on cellular regulation.
Main Methods:
- Review of recent studies on cell surface glycosylation.
- Analysis of growth factor-induced sialic acid removal.
- Investigation of galectin-mediated endocytosis and retrograde transport.
Main Results:
- Selective glycan remodeling can redirect membrane glycoproteins to the Golgi.
- Growth factors trigger sialic acid removal by neuraminidases.
- This process, the GlycoSwitch, involves glycolipid-lectin interactions and retrograde transport.
Conclusions:
- The cell surface glycan landscape is dynamic and subject to remodeling.
- The GlycoSwitch pathway offers a novel mechanism for glycan-mediated cellular regulation.
- This highlights new perspectives on the functional roles of cell surface glycans.
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