Epidermal growth factor receptor and signal transduction: potential targets for anti-cancer therapy

2005 ◽  
Vol 16 (5) ◽  
pp. 483-494 ◽  
Author(s):  
Sumanta Kumar Pal ◽  
Mark Pegram
Keyword(s):  
Signal Transduction ◽  
Epidermal Growth Factor Receptor ◽  
Growth Factor ◽  
Cancer Therapy ◽  
Epidermal Growth Factor ◽  
Growth Factor Receptor ◽  
Anti Cancer ◽  
Epidermal Growth

scholarly journals Single molecule analysis of signal transduction through epidermal growth factor receptor

2001 ◽  
Vol 41 (supplement) ◽  
pp. S29
Author(s):  
M. Morimatsu ◽  
K. Ota ◽  
K. Hibino ◽  
T. Miyauchi ◽  
T. Uyemura ◽  
...  
Keyword(s):  
Signal Transduction ◽  
Epidermal Growth Factor Receptor ◽  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Single Molecule ◽  
Growth Factor Receptor ◽  
Epidermal Growth ◽  
Single Molecule Analysis

scholarly journals The juxtamembrane regions of the epidermal growth factor receptor and gp185erbB-2 determine the specificity of signal transduction.

1991 ◽  
Vol 11 (6) ◽  
pp. 3191-3202 ◽  
Author(s):  
O Segatto ◽  
F Lonardo ◽  
D Wexler ◽  
F Fazioli ◽  
J H Pierce ◽  
...  
Keyword(s):  
Signal Transduction ◽  
Epidermal Growth Factor Receptor ◽  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Tyrosine Kinase ◽  
Mutational Analysis ◽  
Growth Factor Receptor ◽  
Tyrosine Kinase Domain ◽  
Amino Terminal ◽  
Epidermal Growth

The epidermal growth factor receptor (EGFR) and gp185erbB-2 are closely related tyrosine kinases. Despite extensive sequence and structural homology, these two receptors display quantitative and qualitative differences in their ability to couple with mitogenic signalling pathways. By using chimeric molecules between EGFR and erbB-2, we found that the determinants responsible for the specificity of mitogenic signal transduction are located in the amino-terminal half of the tyrosine kinase domain of either receptor. In the EGFR, mutational analysis within this subdomain revealed that deletion of residues 660 to 667 impaired receptor mitogenic activity without affecting its tyrosine kinase properties. This sequence is therefore likely to contribute to the specificity of substrate recognition by the EGFR kinase.

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