Branched N-glycans regulate the biological functions of integrins and cadherins.

Glycosylation is one of the most common post-translational modifications, and approximately 50% of all proteins are presumed to be glycosylated in eukaryotes. Branched N-glycans, such as bisecting GlcNAc, β-1,6-GlcNAc and core fucose (α-1,6-fucose), are enzymatic products of N-acetylglucosaminyltransferase III, N-acetylglucosaminyltransferase V and α-1,6-fucosyltransferase, respectively. These branched structures are highly associated with various biological functions of cell adhesion molecules, including cell adhesion and cancer metastasis. E-cadherin and integrins, bearing N-glycans, are representative adhesion molecules. Typically, both are glycosylated by N-acetylglucosaminyltransferase III, which inhibits cell migration. In contrast, integrins glycosylated by N-acetylglucosaminyltransferase V promote cell migration. Core fucosylation is essential for integrin-mediated cell migration and signal transduction. Collectively, N-glycans on adhesion molecules, especially those on E-cadherin and integrins, play key roles in cell–cell and cell–extracellular matrix interactions, thereby affecting cancer metastasis. [ABSTRACT FROM AUTHOR]