N-Glycosylation at Asn 402 Stabilizes N-Cadherin and Promotes Cell-Cell Adhesion of Glioma Cells

被引:18
作者
Xu, Yaolin [1 ,2 ,3 ]
Chang, Ruiqi [2 ,3 ]
Xu, Fulin [1 ]
Gao, Yan [2 ,3 ]
Yang, Fuming [2 ,3 ]
Wang, Can [4 ]
Xiao, Jin [2 ,3 ]
Su, Zuopeng [1 ]
Bi, Yongyan [1 ]
Wang, Liying [2 ,3 ,5 ]
Zha, Xiliang [2 ,3 ,5 ]
机构
[1] Fudan Univ, Cent Hosp Minhang Dist, Shanghai, Peoples R China
[2] Fudan Univ, Dept Biochem & Mol Biol, Sch Basic Med Sci, Shanghai, Peoples R China
[3] Minist Hlth, Key Lab Glycoconjugate Res, Shanghai, Peoples R China
[4] Shanghai Inst Food & Drug Control, Shanghai, Peoples R China
[5] Minist Educ, Key Lab Mol Med, Shanghai, Peoples R China
基金
中国国家自然科学基金;
关键词
N-CADHERIN; N-GLYCOSYLATION; CELL ADHESION; GLIOMA; CELL MIGRATION; CANCER-CELLS; MESENCHYMAL TRANSITION; EXPRESSION; CARCINOMA; GLYCANS; CLASSIFICATION; PROGRESSION; TUMORS; ALPHA;
D O I
10.1002/jcb.25801
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Cadherin is crucial for cell-cell adhesion and N-glycosylation of N-cadherin has been implicated in the process of mammary, renal, and ovarian carcinogenesis. However, whether N-glycosylation of N-cadherin plays a role in glioma remains unknown. Previous studies had indicated that N-glycosylation could occur at three asparagine residues of N-cadherin. By generating and over-expressing N-glycosylation-deficient N-cadherin mutants in the human glioma cell lines SHG66 and U87, we found that mutation of N402 but not of the other potentially N-glycosylated residues destabilized N-cadherin and led to its ubiquitylation and subsequent proteasomal degradation. Furthermore, destabilized N-cadherin inhibited cadherin-mediated cell-cell adhesion and promoted cell migration. Our findings reveal that N-glycosylation controls N-cadherin stability and plays a role in glioma migration. (C) 2016 Wiley Periodicals, Inc.
引用
收藏
页码:1423 / 1431
页数:9
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