Figure 5.
The regulation of JunB by TLR/MYD88 signaling and the impact of JunB on HCK transcription. The phosphorylation of JunB (Ser79) and c-Jun (Ser63) was assessed following TLR4 (by LPS-EB) and TLR9 (by ODN-2006) stimulation (A) as well as the lentiviral cells (C). HCK overexpression of MYD88 L265P mutant vs MYD88 WT (B) in both MYD88-mutated BCWM.1 cells and MYD88 wild-type Ramos cells. The phosphorylation of JunB (Ser79) and c-Jun (Ser63) was determined following MYD88 knockdown in MYD88-mutated BCWM.1 protein levels detected following lentiviral mediated knockdown of JunB in MYD88-mutated BCWM.1 and TMD-8 cells using 2 distinct shRNAs and compared with scrambled control vector (D). Protein levels of MYD88, JunB, c-Jun, and GADPH served as protein expression, knockdown efficiency, and loading controls.

The regulation of JunB by TLR/MYD88 signaling and the impact of JunB on HCK transcription. The phosphorylation of JunB (Ser79) and c-Jun (Ser63) was assessed following TLR4 (by LPS-EB) and TLR9 (by ODN-2006) stimulation (A) as well as the lentiviral cells (C). HCK overexpression of MYD88 L265P mutant vs MYD88 WT (B) in both MYD88-mutated BCWM.1 cells and MYD88 wild-type Ramos cells. The phosphorylation of JunB (Ser79) and c-Jun (Ser63) was determined following MYD88 knockdown in MYD88-mutated BCWM.1 protein levels detected following lentiviral mediated knockdown of JunB in MYD88-mutated BCWM.1 and TMD-8 cells using 2 distinct shRNAs and compared with scrambled control vector (D). Protein levels of MYD88, JunB, c-Jun, and GADPH served as protein expression, knockdown efficiency, and loading controls.

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