TRIM52: A nuclear TRIM protein that positively regulates the nuclear factor-kappa B signaling pathway

Emerging evidence suggests that TRIM family proteins play a crucial role in regulating the NF-kappa B signaling pathway. TRIM52 is a novel noncanonical antiviral TRIM gene with a unique expanded RING domain. Information on the biological function of TRIM52 is limited. Herein, we demonstrated TRIM52 involvement in NF-kappa B activation. We found that TRIM52 overexpression specifically activated the NF-kappa B signal. TRIM52 overexpression can significantly induce TNF alpha and IL-6 expression. We also found that the RING domain of TRIM52 was essential for its activation of the NF-kappa B signal. Further study showed that TRIM52 overexpression did not affect the protein level of I kappa B alpha and phosphorylated p65 protein. We found that the pro-inflammatory cytokines TNF alpha and IL-6 could induce TRIM52 expression. Overall, these data suggested that TRIM52 was a positive regulator of the NF-kappa B pathway. (C) 2017 Elsevier Ltd. All rights reserved.