Epidermal growth factor stimulates matrix metalloproteinase-9 expression and invasion in human follicular thyroid carcinoma cells through Focal adhesion kinase

Biochimie ◽  
2007 ◽  
Vol 89 (5) ◽  
pp. 613-624 ◽  
Author(s):  
B ROTHHUT ◽  
C GHONEIM ◽  
F ANTONICELLI ◽  
M SOULAROTHHUT
Open Biology ◽  
2021 ◽  
Vol 11 (8) ◽  
pp. 210166
Author(s):  
Grace K. Chan ◽  
John A. McGrath ◽  
Maddy Parsons

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.


Sign in / Sign up

Export Citation Format

Share Document