Glycans anchored on cell-surface receptors are active modulators of receptor signaling. A strategy is presented that enforces transient changes to cell-surface glycosylation patterns to tune receptor signaling. This approach, termed in situ glycan editing, exploits recombinant glycosyltransferases to incorporate monosaccharides with linkage specificity onto receptors in situ. α2,3-linked sialic acid or α1,3-linked fucose added in situ suppresses signaling through epidermal growth factor receptor and fibroblast growth factor receptor. We also applied the same strategy to regulate the electrical signaling of a potassium ion channel-human ether-à-go-go-related gene channel. Compared to gene editing, no long-term perturbations are introduced to the treated cells. In situ glycan editing therefore offers a promising approach for studying the dynamic role of specific glycans in membrane receptor signaling and ion channel functions.
Keyphrases
- cell surface
- crispr cas
- epidermal growth factor receptor
- signaling pathway
- endothelial cells
- induced apoptosis
- tyrosine kinase
- small molecule
- advanced non small cell lung cancer
- genome wide
- copy number
- gene expression
- oxidative stress
- transcription factor
- brain injury
- subarachnoid hemorrhage
- newly diagnosed
- genome wide analysis