Skip to main content
. 2016 Oct 17;6:35343. doi: 10.1038/srep35343

Figure 4. The TRIF-dependent phosphorylation of IRF-3 is augmented in Dab2-knockdown cells.

Figure 4

(a–c) The shLuc and shDab2-B cells were treated with LPS (100 ng/ml) for the indicated time. The cell lysates were collected for Western blotting using the antibodies against the indicated proteins to determine the effect of Dab2 knockdown on LPS-stimulated phosphorylation of IRF-3 (panel A), p65-NF-κB (panel B), and MAPKs (p38, ERK1/2, and JNK1/2; panel C), and degradation of IRAK1 and IκBα (panel B). The expression of β-actin was used as a control for equal protein loading. Quantification for the changes of protein phosphorylation and degradation was performed by using the Image J analysis software. The full Western blot and the corresponding positions of the molecular weight protein markers are presented in Supplementary Fig. S3. Data represent the mean ± SEM of three independent experiments. ns, no significance. *P < 0.05; **P < 0.01; and ***P < 0.001.