N‐Glycosylation at Asn 402 Stabilizes N‐Cadherin and Promotes Cell–Cell Adhesion of Glioma Cells. Issue 6 (10th January 2017)

• Record Type: Journal Article
• Authors: Xu, Yaolin; Chang, Ruiqi; Xu, Fulin; Gao, Yan; Yang, Fuming; Wang, Can; Xiao, Jin; Su, Zuopeng; Bi, Yongyan; Wang, Liying; Zha, Xiliang
• Is Part Of: Journal of cellular biochemistry. Volume 118:Issue 6(2017)
• Page Start: 1423
• Page End: 1431
• Publication Date: 2017-01-10
• Subjects: N‐CADHERIN -- N‐GLYCOSYLATION -- CELL ADHESION -- GLIOMA -- CELL MIGRATION; Cytochemistry -- Periodicals; 572
• DOI: 10.1002/jcb.25801
• Languages: English
• ISSNs: 0730-2312

Abstract

ABSTRACT: 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. J. Cell. Biochem. 118: 1423–1431, 2017. © 2016 Wiley Periodicals, Inc. Abstract : Elimination of N‐glycans at N402 inhibits cadherin‐mediated cell–cell adhesion and promotes cell migration. Meanwhile, photographs taken by scanning electron microscopy showed that SHG66‐WT cells exhibit more attaching structures among cells.