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N ‐Glycosylation affects the adhesive function of E‐Cadherin through modifying the composition of adherens junctions (AJs) in human breast carcinoma cell line MDA‐MB‐435
Author(s) -
Zhao Hongbo,
Liang Yulong,
Xu Zhibin,
Wang Liying,
Zhou Feng,
Li Zengxia,
Jin Jiawei,
Yang Yong,
Fang Zhengyu,
Hu Yali,
Zhang Lineng,
Su Jianmin,
Zha Xiliang
Publication year - 2007
Publication title -
journal of cellular biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.028
H-Index - 165
eISSN - 1097-4644
pISSN - 0730-2312
DOI - 10.1002/jcb.21608
Subject(s) - adherens junction , cadherin , ectodomain , cell adhesion , glycosylation , microbiology and biotechnology , n linked glycosylation , adhesion , chemistry , biology , cell , glycan , biochemistry , glycoprotein , receptor , organic chemistry
E‐cadherin mediates calcium‐dependent cell–cell adhesion between epithelial cells. The ectodomain of human E‐cadherin contains four potential N ‐glycosylation sites at Asn residues 554, 566, 618, and 633. In this study, the role of N ‐glycosylation in E‐cadherin‐mediated cell–cell adhesion was investigated by site‐directed mutagenesis. In MDA‐MB‐435 cells, all four potential N ‐glycosylation sites of human E‐cadherin were N ‐glycosylated. Removal of N ‐glycan at Asn‐633 dramatically affected E‐cadherin stability. In contrast, mutant E‐cadherin lacking the other three N ‐glycans showed similar protein stability in comparison with wild‐type E‐cadherin. Moreover, N ‐glycans at Asn‐554 and Asn‐566 were found to affect E‐cadherin‐mediated calcium‐dependent cell–cell adhesion, and removal of either of the two N ‐glycans caused a significant decrease in calcium‐dependent cell–cell adhesion accompanied with elevated cell migration. Analysis of the composition of adherens junctions (AJs) revealed that removal of N ‐glycans on E‐cadherin resulted in elevated tyrosine phosphorylation level of β‐catenin and reduced β‐ and α‐catenins at AJs. These findings demonstrate that N ‐glycosylation may affect the adhesive function of E‐cadherin through modifying the composition of AJs. J. Cell. Biochem. 104: 162–175, 2008. © 2007 Wiley‐Liss, Inc.