(Glycan Binding) Activity-Based Protein Profiling in Cells Enabled by Mass Spectrometry-Based Proteomics

The presence of glycan modifications at the cell surface and other locales positions them as key regulators of cell recognition and function. However, due to the complexity of glycosylation, the annotation of which proteins bear glycan modifications, which glycan patterns are present, and which proteins are capable of binding glycans is incomplete. Inspired by activity-based protein profiling to enrich for proteins in cells based on select characteristics, these endeavors have been greatly advanced by the development of appropriate glycan-binding and glycan-based probes. Here, we provide context for these three problems and describe how the capability of molecules to interact with glycans has enabled the assignment of proteins with specific glycan modifications or of proteins that bind glycans. Furthermore, we discuss how the integration of these probes with high resolution mass spectrometry-based technologies has greatly advanced glycoscience.

Automated summary

The presence of glycan modifications on cell surface and other locations is important for cell recognition and function. But due to the complexity of glycosylation, the annotation of which proteins have glycan modifications, which glycan patterns are present, and which proteins can bind glycans is incomplete. The development of glycan-binding and glycan-based probes, along with high resolution mass spectrometry-based technologies, has greatly advanced the understanding of these problems and glycoscience as a whole.