Fig. 5

The D domain of LRRC4 abolished the activation and nuclear translocation of ERK1/2. a Western blot analysis showed that LRRC4 inhibited the phosphorylation of ERK1/2. After deletion of the D domain, the inhibitory effect of LRRC4 was weakened. b Western blot analysis showed that LRRC4 inhibited the phosphorylation of ERK1/2 both in the cytoplasm and nucleus. Deletion of the D domain in LRRC4 increased the phosphorylation level of ERK1/2 both in the cytoplasm and in the nucleus. c Confocal fluorescence microscopy of HEK293 cells co-transfected with different plasmids to assess the effect on localization of ERK1 and LRRC4 (LRRC4-ΔD) after EGF stimuli. The merged image shows that the translocation of active ERK1 to the nucleus was more significant after deletion of the D domain. The signals were measured by ImageJ software. (Scale bars, 50 μm.). The data represent the mean±SD of three replicates. Bar in the graph represents the s.e.m. One-way ANOVA, *p < 0.05; **p < 0.01; ***p < 0.001