The addition of bisecting N-acetylglucosamine residues to E-cadherin down-regulates the tyrosine phosphorylation of beta-catenin.

@article{Kitada2001TheAO,
  title={The addition of bisecting N-acetylglucosamine residues to E-cadherin down-regulates the tyrosine phosphorylation of beta-catenin.},
  author={Takuya Kitada and Eiji Miyoshi and Keita Noda and Shigeki Higashiyama and Hideyuki Ihara and Nariaki Matsuura and Nobuki Hayashi and Sumio Kawata and Yuji Matsuzawa and Naoyuki Taniguchi},
  journal={The Journal of biological chemistry},
  year={2001},
  volume={276 1},
  pages={475-80}
}
The enzyme GnT-III (beta 1,4-N-acetylglucosaminyltransferase III) catalyzes the addition of a bisecting N-acetylglucosamine (GlcNAc) residue on glycoproteins. Our previous study described that the transfection of GnT-lll into mouse melanoma cells results in the enhanced expression of E-cadherin, which in turn leads to the suppression of lung metastasis. It has recently been proposed that the phosphorylation of a tyrosine residue of beta-catenin is associated with cell migration. The present… CONTINUE READING