Modulating Cell-Surface Receptor Signaling and Ion Channel Functions by In Situ Glycan Editing

Angew Chem Int Ed Engl. 2018 Jan 22;57(4):967-971. doi: 10.1002/anie.201706535. Epub 2018 Jan 2.


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.

Keywords: click chemistry; fucosylation; in situ glycan editing; sialylation.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • A549 Cells
  • Animals
  • CHO Cells
  • Click Chemistry
  • Cricetinae
  • Cricetulus
  • Cycloaddition Reaction
  • ERG1 Potassium Channel / chemistry
  • ERG1 Potassium Channel / metabolism*
  • ErbB Receptors / chemistry
  • ErbB Receptors / metabolism
  • Evoked Potentials / physiology*
  • Fucose / chemistry
  • Glycosylation
  • Humans
  • Microscopy, Fluorescence
  • Monosaccharides / chemistry*
  • N-Acetylneuraminic Acid / chemistry
  • Receptors, Cell Surface / chemistry
  • Receptors, Cell Surface / metabolism*
  • Sialyltransferases / metabolism
  • Signal Transduction / physiology*
  • beta-Galactoside alpha-2,3-Sialyltransferase


  • ERG1 Potassium Channel
  • KCNH2 protein, human
  • Monosaccharides
  • Receptors, Cell Surface
  • Fucose
  • Sialyltransferases
  • EGFR protein, human
  • ErbB Receptors
  • N-Acetylneuraminic Acid
  • beta-Galactoside alpha-2,3-Sialyltransferase