Involvement of FAK/Src complex in the processes of Escherichia coli phagocytosis by insect hemocytes

FEBS Letters

Lambropoulou, Maria¹  Metheniti, Aristea¹  Marmaras, Vassilis J¹  Paraskevopoulou, Nikolitsa¹ 

[1] Department of Biology, University of Patras, Patras 265 00, Greece

关键词: Focal adhesion kinase;    Focal adhesion kinase/Src complex;    Phagocytosis;    Hemocyte;    Ceratitis capitata;    LPS;    lipopolysaccharide;    FAK;    focal adhesion kinase;    ERK1;    extracellular signal-regulated protein kinase;    MAP;    mitogen-activated protein;    TBS;    Tris-buffered saline;    Fn;    fibronectin;   

DOI  :  10.1016/S0014-5793(01)02405-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Recently we demonstrated that lipopolysaccharide promotes activation of the Ras/mitogen-activated protein cascade in hemocytes and that phagocytosis of Escherichia coli by insect hemocytes is mediated by an integrin-dependent process [Foukas et al. (1998) J. Biol. Chem. 273, 14813–14818]. Here we report data concerning the focal adhesion kinase (FAK) tyrosine phosphorylation status in hemocytes in response to E. coli. We demonstrate that E. coli-triggering stimulates a significant increase in tyrosine phosphorylation of FAK in hemocytes. Furthermore, immunoblotting analysis using anti-Y397 demonstrated intense FAK activity at the Y397/SH2-binding site in hemocytes treated with E. coli. In addition, antibody-mediated inhibition of FAK and Src-kinase has been shown to abolish FAK phosphorylation and E. coli phagocytosis, indicating a specific role for the FAK/Src complex in the processes of promoting cell phagocytosis. These findings expand the known signaling functions of FAK and provide insight into signal transduction events associated with hemocyte phagocytosis in response to E. coli.

【 授权许可】

Unknown