Glycan regulation of cell-cell junction dynamics and architecture

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Glycosylation is a common posttranslational modification of glycoproteins, glycolipids and proteoglycans that generates extracellular binding sites for galactose-specific lectins or galectins. Cadherins are glycoproteins involved in cell-cell contacts whose extracellular domain mediates homotypic interactions with adjacent cells and cytoplasmic domain interacts through catenins with the underlying actin cytoskeleton. We have shown that galectin-3 destabilizes cell-cell junctions and increases mobility of N-cadherin and the lipid raft-associated glycosphingolipid GM1 ganglioside within cell-cell junctions. We hypothesize that galectin-3 regulation of glycoprotein and glycolipid residency and dynamics in cell-cell junctions drives local endocytosis impacting the underlying actin cytoskeleton and junctional stability. In this proposal, we will study the role of galectin-3 and lipid rafts in the regulation of N-cadherin dynamics and cell-cell junction architecture.