scholarly journals Bombesin, Lysophosphatidic Acid, and Epidermal Growth Factor Rapidly Stimulate Focal Adhesion Kinase Phosphorylation at Ser-910

2003 ◽  
Vol 278 (25) ◽  
pp. 22631-22643 ◽  
Author(s):  
Isabel Hunger-Glaser ◽  
Eduardo Perez Salazar ◽  
James Sinnett-Smith ◽  
Enrique Rozengurt
Keyword(s):  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Focal Adhesion Kinase ◽  
Focal Adhesion ◽  
Lysophosphatidic Acid ◽  
Epidermal Growth ◽  
Focal Adhesion Kinase Phosphorylation ◽  
Kinase Phosphorylation

scholarly journals Spatial activation of ezrin by epidermal growth factor receptor and focal adhesion kinase co-ordinates epithelial cell migration

Open Biology ◽  
2021 ◽  
Vol 11 (8) ◽  
pp. 210166
Author(s):  
Grace K. Chan ◽  
John A. McGrath ◽  
Maddy Parsons
Keyword(s):  
Epidermal Growth Factor Receptor ◽  
Growth Factor ◽  
Epithelial Cell ◽  
Epidermal Growth Factor ◽  
Focal Adhesion Kinase ◽  
Focal Adhesion ◽  
Growth Factor Receptor ◽  
Adaptor Protein ◽  
Epidermal Growth ◽  
And Migration

Epidermal growth factor receptor (EGFR) plays a critical role in the promotion of epithelial cell proliferation and migration. Previous studies have suggested a cooperative role between EGFR and integrin signalling pathways that enable efficient adhesion and migration but the mechanisms controlling this remain poorly defined. Here, we show that EGFR forms a complex with focal adhesion kinase in epithelial cells. Surprisingly, this complex enhances local Src activity at focal adhesions to promote phosphorylation of the cytoskeletal adaptor protein ezrin at Y478, leading to actomyosin contractility, suppression of focal adhesion dynamics and slower migration. We further demonstrate this regulation of Src is due to the suppression of PTP1B activity. Our data provide new insight into EGF-independent cooperation between EGFR and integrins and suggest transient interactions between these kinases at the leading edge of cells act to spatially control signalling to permit efficient motility.

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