Identification of tripartite motif-containing 22 (TRIM22) as a novel NF-κB activator.

Increasing evidence suggests that TRIM family proteins may play important roles in the regulation of innate immune signaling pathways. Here we report TRIM22 is involved in the activation of NF-κB. It was found that overexpression of TRIM22 could dose-dependently activate NF-κB as demonstrated by reporter gene assay and electrophoretic mobility shift assay, but had no effect on the activity of other transcription factors, including NF-AT, AP-1, C/EBP and IRFs. Further study showed that both the N-terminal RING domain and C-terminal SPRY domain were crucial for TRIM22-mediated NF-κB activation. Moreover, our results revealed that TRIM22 overexpression could significantly induce the secretion of pro-inflammatory cytokines by human macrophage cell line U937 in an NF-κB-dependent manner. These data suggested that TRIM22 was a positive regulator of NF-κB-mediated transcription.

Yu S ，Gao B ，Duan Z ，Xu W ，Xiong S ... -  《-》

TRIM22 can activate the noncanonical NF-κB pathway by affecting IKKα.

Qiu H ，Huang F ，Gong J ，Xiao H ，Sun BL ，Yang RG ... -  《-》

TRIM22 activates NF-κB signaling in glioblastoma by accelerating the degradation of IκBα.

Ji J ，Ding K ，Luo T ，Zhang X ，Chen A ，Zhang D ，Li G ，Thorsen F ，Huang B ，Li X ，Wang J ... -  《-》

Tripartite motif-containing 22 inhibits the activity of hepatitis B virus core promoter, which is dependent on nuclear-located RING domain.

Gao B ，Duan Z ，Xu W ，Xiong S ... -  《-》

TRIM22 inhibits the TRAF6-stimulated NF-κB pathway by targeting TAB2 for degradation.

Qiu H ，Huang F ，Xiao H ，Sun B ，Yang R ... -  《-》