Cell-surface complex N-glycan-bearing receptors and adhesion molecules

Cell-surface complex N-glycan-bearing receptors and adhesion molecules represent a functional class of glycoproteins, including EGFR, TGF-beta receptors, and integrins, that are modified with beta-1,6-branched N-glycans by the enzyme MGAT5 (Dennis et al., 2009, Cell). These glycans act as ligands for galectins, particularly Galectin-3, which cross-links them to form a dynamic "galectin-glycan lattice" on the cell surface (Lau et al., 2007, Cell). This lattice is a critical regulator of cell signaling, as it prevents the constitutive endocytosis of the receptors, thereby maintaining their presence and activity at the plasma membrane. In diseases such as cancer and fibrosis, the lattice is often reinforced, leading to aberrant signaling that promotes tumor progression, metastasis, and tissue scarring (Partridge et al., 2004, Science). Therapeutic intervention typically involves small molecules or carbohydrate-based inhibitors that target the galectin's carbohydrate-recognition domain, thereby disrupting the lattice and allowing for the internalization and degradation of the associated receptors (Blanchard et al., 2014, Chem Biol).

Other names

Complex N-glycan-containing glycoproteinsGalectin ligandsMGAT5-modified receptorsN-linked glycoprotein receptorsBeta-1,6-branched N-glycan-bearing receptors

Inhibition of galectin binding to the carbohydrate-recognition domain of complex N-glycan-bearing receptors, which disrupts the galectin-glycan lattice and promotes receptor internalization and degradation.