| Literature DB >> 20650261 |
Mingzhu Liu1, Yong Yang, Can Wang, Lidong Sun, Chuanzhong Mei, Wantong Yao, Yonglei Liu, Yinghong Shi, Shuangjian Qiu, Jia Fan, Xiumei Cai, Xiliang Zha.
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. 2010 Elsevier Inc. All rights reserved.Entities:
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Year: 2010 PMID： 20650261 DOI： 10.1016/j.abb.2010.07.014
Source DB: PubMed Journal: Arch Biochem Biophys ISSN： 0003-9861 Impact factor: 4.013