Author:
Higuchi Maiko,Kihara Rina,Okazaki Tomohiko,Aoki Ichiro,Suetsugu Shiro,Gotoh Yukiko
Abstract
The crosstalk between spatial adhesion signals and temporal soluble signals is key in regulating cellular responses such as cell migration. Here we show that soluble growth factors (GFs) enhance integrin signaling through Akt phosphorylation of FAK at Ser695 and Thr700. PDGF treatment or overexpression of active Akt1 in fibroblasts increased autophosphorylation of FAK at Tyr397, an essential event for integrin turnover and cell migration. Phosphorylation-defective mutants of FAK (S695A and T700A) underwent autophosphorylation at Tyr397 and promoted cell migration in response to the integrin ligand fibronectin (FN), but importantly, not in response to PDGF. This study has unveiled a novel function of Akt as an “ignition kinase” of FAK in GF signaling and may shed light on the mechanism by which GFs regulate integrin signaling.
Publisher
The Company of Biologists
Cited by
31 articles.
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