Fig. 5: Activation of c-MET in infected erythrocytes.

a c-MET phosphorylation sites covered by the antibody microarray, with the fold change from uRBC control values for the three time points (ring, trophozoite and schizont). Signals that were significantly different during infection are marked by an asterisks (p < 0.05, unpaired two-tailed T-test). b Schematic of the c-MET protein. The juxtamembrane sequence contains both S975 and Y1003, which represent c-CBL-binding sites that target the receptor for degradation (red circles)^73,74. The catalytic domain contains Y1230, Y1234, Y1235, S1236 and T1241. All activating tyrosine phosphorylations (green circles) occur through receptor homodimerization^42,45,75. The function of S1236 and T1241 (black circles) is uncharacterized. The multifunctional docking site contains two phosphosites, Y1349 and Y1356, which aid in the binding of adapter molecules such as grb2 and GAB1⁴⁵. c Western blotting validation of c-MET phosphorylation across asexual development. A phospho-specific antibody to c-MET (Y1234 + Y1235) detected phosphorylated c-MET at the ring and trophozoite stages (upper panel), n = 2 independent experiments. A pan c-MET antibody detected c-MET across all four samples, with a double band in the uninfected, ring and trophozoite samples (middle panel). An antibody against Glycophorin-C was used as a loading control (lower panel). Source data are provided as a Source Data file.