β1,6 GlcNAc branches-modified protein tyrosine phosphatase alpha enhances its stability and promotes focal adhesion formation in MCF-7 cells

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• 作者：Jin Xiao^a ; ^b ; Yan Gao^a ; ^b ; Fuming Yang^a ; ^b ; Can Wang^d ; Yaolin Xu^a ; ^b ; Ruiqi Chang^a ; ^b ; Xiliang Zha^a ; ^b ; ^c ; Liying Wang^a ; ^b ; ^c ; ^{liying_wang@fudan.edu.cn}
• 关键词：N-Acetylglucosaminyltransferase V ; Receptor-like protein tyrosine phosphatase alpha ; Glycosylation ; Focal adhesion ; Protein stability
• 刊名：Biochemical and Biophysical Research Communications
• 出版年：2017
• 出版时间：22 January 2017
• 年：2017
• 卷：482
• 期：4
• 页码：1455-1461
• 全文大小：1890 K
• 卷排序：482

文摘

Receptor-like protein tyrosine phosphatase alpha (RPTPα or PTPα), a type I transmembrane glycoprotein with complex N-glycans, executes multifunction roles on cell behaviors. However, its effect on tumorigenesis and metastasis remains controversial.In this study, PTPα is identified as a novel substrate of N-Acetylglucosaminyltransferase V (GnT-V). Immunofluorescence results showed that addition of β1,6 GlcNAc branches on PTPα enhanced PTPα’s cytomembrane assemble in GnT-V-MCF-7 compared with Mock-MCF-7 (MCF7 cells transfected with the vector pcDNA3). Then we found the alleviating degradation of PTPα was observed in GnT-V-MCF-7 while PTPα in Mock-MCF-7 was prone to quick degradation. Increased cell-surface retention subsequently enhanced PTPα’s catalytic activity on the dephosphorylation of Src kinase at Tyr529 and promoted focal adhesion formation and mature. Therefore, our findings could provide an insight into the molecular mechanism of how GnT-V promoted cell migration, suggesting that PTPα could be one of factors regulating promote migration of breast cancer cell.