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, 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.
Zhao
Yanyang
Y
Department of Biochemistry, Osaka University Graduate School of Medicine, Osaka, Japan.
Sato
Yuya
Y
Isaji
Tomoya
T
Fukuda
Tomohiko
T
Matsumoto
Akio
A
Miyoshi
Eiji
E
Gu
Jianguo
J
Taniguchi
Naoyuki
N
D002448:Cell Adhesion; D002450:Cell Communication; D045744:Cell Line, Tumor; D002465:Cell Movement; D005109:Extracellular Matrix; D005544:Forecasting; D006031:Glycosylation; D006801:Humans; D016023:Integrins / Q000737:chemistry / Q000378:metabolism*; D008954:Models, Biological; D017351:N-Acetylglucosaminyltransferases / Q000378:metabolism; D009362:Neoplasm Metastasis; D011134:Polysaccharides / Q000737:chemistry / Q000378:metabolism / Q000502:physiology*
D016023:Integrins; D011134:Polysaccharides; D017351:N-Acetylglucosaminyltransferases