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FEBS J. 2008 May;275(9):1939-48. doi: 10.1111/j.1742-4658.2008.06346.x. Epub 2008 Apr 1.

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

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Department of Biochemistry, Osaka University Graduate School of Medicine, Osaka, Japan.


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, beta-1,6-GlcNAc and core fucose (alpha-1,6-fucose), are enzymatic products of N-acetylglucosaminyltransferase III, N-acetylglucosaminyltransferase V and alpha-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.

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