Tyrosine phosphorylation of focal adhesion kinase stimulated by hepatocyte growth factor leads to mitogen-activated protein kinase activation

Hong Chen Chen, Po Chao Chant, Ming Jer Tang, Chi Hung Cheng, Tien Jye Chan

研究成果: Article同行評審

82 引文 斯高帕斯(Scopus)

摘要

Focal adhesion kinase (FAK) is a cytoplasmic tyrosine kinase involved in integrin-mediated signal transduction pathway. In this report, we describe that the treatment of hepatocyte growth factor (HGF) stimulates a significant increase in the tyrosine phosphorylation of FAK in human embryonic kidney 293 cells. This stimulation is independent of cell adhesion or the integrity of the actin cytoskeleton, suggesting potentially different mechanisms by which the HGF receptors and integrins regulate the tyrosine phosphorylation of FAK. Our results also suggest that the activation of Src upon HGF stimulation is likely to be one, if not the only, of the mechanisms responsible for the HGF- induced tyrosine phosphorylation of FAK. Furthermore, we showed that a mutation in the Grb2 binding site Tyr-925 of FAK partially abolishes its increase in HGF-induced phosphorylation. Finally, we demonstrated that HGF stimulates the association of FAK with Grb2 in vitro and in intact cells and provided evidence that FAK might contribute to the activation of mitogen- activated protein kinase through Ras in HGF signaling by functioning as an adapter molecule.

原文English
頁(從 - 到)25777-25782
頁數6
期刊Journal of Biological Chemistry
273
發行號40
DOIs
出版狀態Published - 1998 十月 2

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Cell Biology

指紋 深入研究「Tyrosine phosphorylation of focal adhesion kinase stimulated by hepatocyte growth factor leads to mitogen-activated protein kinase activation」主題。共同形成了獨特的指紋。

引用此