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Papers In Press, published online ahead of print November 29, 2005
J. Biol. Chem, 10.1074/jbc.M510893200
Submitted on October 5, 2005
Revised on November 2, 2005
Accepted on November 29, 2005

Core fucosylation regulates EGF receptor-mediated intracellular signaling

Xiangchun Wang, Hideyuki Ihara, Eiji Miyoshi, Koichi Honke, Naoyuki Taniguchi, and Jianguo Gu

Department of Biochemistry, Osaka University Graduate School of Medicine, Suita, Osaka 565-0871

Corresponding Author: jgu{at}biochem.med.osaka-u.ac.jp

alpha1,6-Fucosyltransferase (Fut8) catalyzes the transfer of a fucose residue to N-linked oligosaccharides on glycoproteins via an alpha1,6-linkage to form core fucosylation in mammals. We recently found that disruption of the Fut8 gene induces severe growth retardation and early postnatal death. In order to investigate the molecular mechanism involved, we established embryonic fibroblasts of Fut8+/+ and Fut8-/-, derived from wild-type and Fut8-null mice, respectively. Interestingly, the epidermal growth factor (EGF)-induced phosphorylation levels of the EGF receptor (EGFR) were substantially blocked in Fut8-/-cells, compared with Fut8+/+cells, while there are no significant changes in the total activities of tyrosine phosphatase for phosphorylated EGFR between two cells. The inhibition of EGFR phosphorylation was completely restored by re-introduction of the Fut8 gene to Fut8-/-cells. Consistent with this, EGFR-mediated JNK or ERK activation was significantly suppressed in Fut8-/- cells. Finally, we found that the core fucosylation of N-glycans is required for the binding of the EGF to its receptor, whereas no effect was observed for the expression levels of EGFR on the cell surface. Collectively, these results strongly suggest that core fucosylation is essential for EGF receptor-mediated biological functions.


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