Unglycosylation at Asn-633 made extracellular domain of E-cadherin folded incorrectly and arrested in endoplasmic reticulum, then sequentially degraded by ERAD

@article{Zhou2008UnglycosylationAA,
  title={Unglycosylation at Asn-633 made extracellular domain of E-cadherin folded incorrectly and arrested in endoplasmic reticulum, then sequentially degraded by ERAD},
  author={Feng Zhou and Jianmin Su and Le Fu and Yong Yang and Lineng Zhang and Liying Wang and Hongbo Zhao and Diancai Zhang and Zengxia Li and Xiliang Zha},
  journal={Glycoconjugate Journal},
  year={2008},
  volume={25},
  pages={727-740}
}
The human E-cadherin is a single transmembrane domain protein involved in Ca2+-dependent cell–cell adhesion. In a previous study, we demonstrated that all of four potential N-glycosylation sites in E-cadherin are occupied by N-glycans in human breast carcinoma cells in vivo and the elimination of N-glycan at Asn-633 dramatically affected E-cadherin expression and made it degraded. In this study we investigated the molecular mechanism of E-cadherin, which lacks N-glycosylation at Asn-633 (M4… CONTINUE READING

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ER stress and diseases.

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