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"Taken together, these findings establish the TRIM14‐USP14 axis as a crucial checkpoint that controls noncanonical NF‐κB signaling and highlight the crosstalk between autophagy and innate immunity."

"The stabilization of p100/p52 by TRIM14‐USP14 complex subsequently enhances noncanonical NF‐κB signaling (Figure 6 )."

"Thus, the TRIM14‐USP14 complex promotes the activation of noncanonical NF‐κB pathway through the crosstalk with autophagy."

"Thus, the interaction of TRIM14 with USP14 promotes activation of noncanonical NF–κB signaling through interfering with autophagy."

"41 In another study, the ubiquitination–deubiquitination cascade mediated by TRIM27‐USP7 complex plays an essential role in TNFα‐induced apoptosis.42 Collectively, we speculate that TRIM14‐USP14 complex is capable of targeting different proteins in innate immunity."

"Our previous data have also shown that TRIM14 recruits USP14 to accelerate the stabilization of cGAS in response to virus infection, xref as a pair of mutual binding partners, TRIM14‐USP14 in this context has been convinced to regulate noncanonical NF‐κB signaling through the control of selective autophagy."

"Thus, the TRIM14‐USP14 complex promotes the activation of noncanonical NF‐κB pathway through the crosstalk with autophagy.Autophagy is an essential homeostatic process for clearance of intracellular protein aggregates, injured organelles, and invading cytoplasmic microbes.36 Recently, increasing evidence suggests the important regulatory roles of the crosstalk between autophagy and a variety of cellular responses, including immune responses and inflammation.37 For example, selective autophagy plays a pivotal role in regulating type I interferon signaling21, 38 and canonical NF‐κB signaling39 as described by our previous studies."

"Indeed, TRIM14‐USP14 complex is not a unique model in the regulation of innate immune signaling."

"Indeed, TRIM14‐USP14 complex is not a unique model in the regulation of innate immune signaling."

"The stabilization of p100/p52 by TRIM14‐USP14 complex subsequently enhances noncanonical NF‐κB signaling ( Figure xref )."

"It has been reported that FBXW7α (also known as FBW7) targets nuclear p100 for proteasomal degradation, which depends on phosphorylation of p100 by GSK3. xref In our study, we found that TRIM14‐USP14 axis inhibits the degradation of p100/p52 to promote noncanonical NF‐κB signaling."

"These results further support the function of TRIM14‐USP14 complex in noncanonical NF‐κB pathway, by showing that USP14 is also indispensable in regulating p100 or p52 stabilization in noncanonical NF‐κB pathway."

"For example, TRIM27‐USP7 complex inhibited the function of TBK1 in type I interferon signaling by enhancing the ubiquitination of TBK1. xref In another study, the ubiquitination–deubiquitination cascade mediated by TRIM27‐USP7 complex plays an essential role in TNFα‐induced apoptosis. xref Collectively, we speculate that TRIM14‐USP14 complex is capable of targeting different proteins in innate immunity."

"These results further support the function of TRIM14‐USP14 complex in noncanonical NF‐κB pathway, by showing that USP14 is also indispensable in regulating p100 or p52 stabilization in noncanonical NF‐κB pathway."