| Literature DB >> 28073078 |
Wenchun Fan1, Tingting Liu1, Xiangmin Li2, Yun Zhou1, Mengge Wu1, Xiaofang Cui1, Huanchun Chen2, Ping Qian3.
Abstract
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.Entities:
Keywords: Nuclear factor-kappa B (NF-κB); Pro-inflammatory cytokine; Signaling transduction; TRIM52
Mesh:
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Year: 2017 PMID: 28073078 DOI: 10.1016/j.molimm.2017.01.003
Source DB: PubMed Journal: Mol Immunol ISSN: 0161-5890 Impact factor: 4.407