Modulation of focal adhesion constituents and their down-stream events by EGF: On the cross-talk of integrins and growth factor receptors

摘要: Within the concept of integrin growth factor receptor (GFR) cross-talk, little is known about effects GFRs on focal adhesions (FAs). Therefore, we tested hypothesis whether EGF can modulate constituents FAs and subsequent down-stream events. To this end, EGF-treated keratinocytes were subjected to combined fluorescence imaging western blotting, quantify expression and/or activation molecules, involved in GFR proximal distal signaling Generally, response revealed an amplified redistribution or molecules under study, which will be explained detail from plasma membrane cell interior. In addition significant (EGFR) at tyrosine Tyr845, a remarkable was detectable for adhesion constituents, s1 s3, zyxin. Increased also applied kinase (FAK) by phosphorylation Tyr397, Tyr576, Src Tyr418, while total FAK remained unchanged. Risen activity seen as well analyzed events, p190RhoGAP MAP kinases p42/44. Intriguingly, Src-specific inhibitor Herbimycin A abrogated entire except Tyr397 phosphorylation, independent presence. Mechanistically, our results show that modulates dual fashion, firstly redistributing sites, but amplifying levels activated RhoA antagonist p190RhoGAP, important motility. Further, findings suggest observed underlies EGFR cross-talk recruitment Src,