Table 1. Mutational study of the EGFR feedback monomerization at the PLCγ binding sites.
| Construct | Mutation a | Negative feedback b | EGF - | EGF + | ||||
|---|---|---|---|---|---|---|---|---|
| Y992 | Y1148 | Y1173 | D (μm2/s) | Dmin c | Dmax d | Davg e | ||
| (μm2/s) | (μm2/s) | (μm2/s) | ||||||
| EGFRwt | + + | 0.24 ± 0.02 | 0.11 ± 0.03 | 0.22 ± 0.03 | 0.17 ± 0.06 | |||
| EGFRY992F | F | + + | 0.24 ± 0.03 | 0.11 ± 0.03 | 0.21 ± 0.03 | 0.16 ± 0.05 | ||
| EGFRY1148F | F | + + | 0.24 ± 0.03 | 0.08 ± 0.04 | 0.21 ± 0.03 | 0.14 ± 0.07 | ||
| EGFRY1173F | F | + + | 0.24 ± 0.03 | 0.10 ± 0.04 | 0.22 ± 0.04 | 0.17 ± 0.07 | ||
| EGFRY992/1148F | F | F | + | 0.22 ± 0.03 | 0.11 ± 0.02 | 0.19 ± 0.04 | 0.13 ± 0.05 | |
| EGFRY992/1173F | F | F | + | 0.24 ± 0.03 | 0.10 ± 0.02 | 0.19 ± 0.03 | 0.13 ± 0.04 | |
| EGFRY1148/1173F | F | F | + + | 0.23 ± 0.03 | 0.11 ± 0.03 | 0.20 ± 0.03 | 0.15 ± 0.05 | |
| EGFRY992/1148/1173F | F | F | F | - | 0.22 ± 0.02 | 0.07 ± 0.02 | ND f | 0.07 ± 0.02 |
a F stands for the phosphodeficient mutation (phenylalanine substitution).
b The strength of negative feedback scaled from as strong as for the EGFRwt (+ +) to none (—).
c, d Minimum (Dmin) and maximum (Dmax) level of the diffusion coefficient.
e The diffusion coefficient averaged over the whole measurement time after EGF addition (Davg).
f Not determinable.