期刊
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS
卷 502, 期 2, 页码 89-95出版社
ELSEVIER SCIENCE INC
DOI: 10.1016/j.abb.2010.07.014
关键词
EGFRvIII; FAK; ERK1/2; Tyrosine phosphorylation; Cell migration
资金
- National Natural Science Foundation of China [30600336]
- National Key Sci-Tech Special Project of China [2008ZX10002-018, 2008ZX10002-019]
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 U87 Delta EGFR 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 U87 Delta EGFR cells. (C) 2010 Elsevier Inc. All rights reserved.
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