Mapping Interactions between Glycans and Glycan-Binding Proteins by Live Cell Proximity Tagging.

ABSTRACT: Interactions between glycans and glycan-binding proteins (GBPs) consist of weak, noncovalent, and transient binding events, making them difficult to study in live cells void of a static, isolated system. Furthermore, the glycans are often presented as protein glycoconjugates, but there are limited efforts to identify these proteins. Proximity labeling permits covalent tagging of the glycoprotein interactors to query GBP in live cells. Coupled with high-resolution mass spectrometry, it facilitates determination of the proteins bearing the interacting glycans. In this method, fusion protein constructs of a GBP of interest with a peroxidase enzyme allows for in situ spatiotemporal radical-mediated tagging of interacting glycoproteins in living cells that can be enriched for identification. Us

SUBMITTER: Joeh E 

PROVIDER: S-EPMC8274366 | biostudies-literature | 2021 Apr

REPOSITORIES: biostudies-literature