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

Publication date: February 2017
Source:Molecular Immunology, Volume 82
Author(s): Wenchun Fan, Tingting Liu, Xiangmin Li, Yun Zhou, Mengge Wu, Xiaofang Cui, Huanchun Chen, Ping Qian
Emerging evidence suggests that TRIM family proteins play a crucial role in regulating the NF-κB 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-κB activation. We found that TRIM52 overexpression specifically activated the NF-κB signal. TRIM52 overexpression can significantly induce TNFα and IL-6 expression. We also found that the RING domain of TRIM52 was essential for its activation of the NF-κB signal. Further study showed that TRIM52 overexpression did not affect the protein level of IκBα and phosphorylated p65 protein. We found that the pro-inflammatory cytokines TNFα and IL-6 could induce TRIM52 expression. Overall, these data suggested that TRIM52 was a positive regulator of the NF-κB pathway.



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