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- Title
FAK integrates growth-factor and integrin signals to promote cell migration.
- Authors
Sieg, D J; Hauck, C R; Ilic, D; Klingbeil, C K; Schaefer, E; Damsky, C H; Schlaepfer, D D
- 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.
- Publication
Nature cell biology, 2000, Vol 2, Issue 5, p249
- ISSN
1465-7392
- Publication type
Journal Article
- DOI
10.1038/35010517