Heregulin and HER2 signaling selectively activates c-Src phosphorylation at tyrosine 215

被引：70

作者：

Vadlamudi, RK

Sahin, AA

Adam, L

Wang, RA

Kumar, R

机构：

[1] Univ Texas, MD Anderson Canc Ctr, Dept Mol & Cellular Oncol, Houston, TX 77030 USA

[2] Univ Texas, MD Anderson Canc Ctr, Dept Pathol, Houston, TX 77030 USA

来源：

FEBS LETTERS | 2003年 / 543卷 / 1-3期

关键词：

receptor tyrosine kinase; cytoplasmic tyrosine kinase; growth factor signaling;

D O I：

10.1016/S0014-5793(03)00404-6

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

To elucidate the molecular mechanisms by which human epidermal growth factor receptor/heregulin (HER2/HRG) influence the migratory potential of breast cancer cells, we have used phospho-specific antibodies against c-Src kinase and focal adhesion kinase (FAK). This study establishes that HER2/HRG-signaling selectively upregulates Tyr phosphorylation of c-Src at Tyr-215 located within the SH2 domain, increases c-Src kinase activity and selectively upregulates Tyr phosphorylation of FAK at Tyr-861. HER2-overexpressing tumors showed increased levels of c-Src phosphorylation at Tyr-215. These findings suggest that HER2/HRG influence metastasis of breast cancer cells through a novel signaling pathway involving phosphorylation of FAK tyrosine 861 via activation of c-Src tyrosine 215. (C) 2003 Published by Elsevier Science B.V. on behalf of the Federation of European Biochemical Societies.

引用

页码：76 / 80

页数：5

共 24 条

[1] Src mediates stimulation by vascular endothelial growth factor of the phosphorylation of focal adhesion kinase at tyrosine 861, and migration and anti-apoptosis in endothelial cells [J].