FAK integrates growth-factor and integrin signals to promote cell migration
Author: ["David J. Sieg","Christof R. Hauck","Dusko Ilic","Candice K. Klingbeil","Erik Schaefer","Caroline H. Damsky","David D. Schlaepfer"]
Publication: Nature Cell Biology
CITE.CC academic search helps you expand the influence of your papers.
Abstract
Here we show that cells lacking focal adhesion kinase (FAK) are refractory to motility signals from platelet-derived and epidermal growth factors (PDGF and EGF respectively), and that stable re-expression of FAK rescues these defects. FAK associates with activated PDGF- and EGF-receptor (PDGFR and EGFR) signalling complexes, and expression of the band-4.1-like domain at the FAK amino terminus is sufficient to mediate an interaction with activated EGFR. However, efficient EGF-stimulated cell migration also requires FAK to be targeted, by its carboxy-terminal domain, to sites of integrin-receptor clustering. Although the kinase activity of FAK is not needed to promote PDGF- or EGF-stimulated cell motility, kinase-inactive FAK is transphosphorylated at the indispensable Src-kinase-binding site, FAK Y397, after EGF stimulation of cells. Our results establish that FAK is an important receptor-proximal link between growth-factor-receptor and integrin signalling pathways.
Cite this article
Sieg, D., Hauck, C., Ilic, D. et al. FAK integrates growth-factor and integrin signals to promote cell migration . Nat Cell Biol 2, 249–256 (2000). https://doi.org/10.1038/35010517
