Author/Authors :
Liu، نويسنده , , Mingzhu and Yang، نويسنده , , Yong and Wang، نويسنده , , Can and Sun، نويسنده , , Lidong and Mei، نويسنده , , Chuanzhong and Yao، نويسنده , , Wantong and Liu، نويسنده , , Yonglei and Shi، نويسنده , , Yinghong and Qiu، نويسنده , , Shuangjian and Fan، نويسنده , , Jia and Cai، نويسنده , , Xiumei and Zha، نويسنده , , Xiliang، نويسنده ,
Abstract :
Epidermal growth factor receptor variant III (EGFRvIII), the most common EGFR mutation, is associated with cell migration of glioblastoma multiforme (GBM) cases; however, the mechanism has not been elucidated. In this study, we found that the EGFRvIII-promoted glioma cell migration was closely linked to high levels of tyrosine phosphorylation in focal adhesion kinase (FAK) Y397. We also demonstrated that EGFRvIII formed a complex with FAK, resulting in enhanced tyrosine phosphorylation levels of FAK Y397 and EGFR Y1068. After knockdown of FAK expression via anti-FAK shRNA, the U87ΔEGFR cell migration was significantly inhibited, accompanying with the reduced phosphorylation levels of extracellular signal-regulated kinase (ERK1/2). Furthermore, the role of ERK1/2 in FAK-regulated cell migration was confirmed. Taken together, our results suggest that FAK and its downstream molecule ERK were involved in EGFRvIII-promoted glioma cell migration in U87ΔEGFR cells.
Keywords :
FAK , EGFRvIII , tyrosine phosphorylation , Cell migration , ERK1/2
