2. Academic Validation
  3. TRIM52: A nuclear TRIM protein that positively regulates the nuclear factor-kappa B signaling pathway

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

  • Mol Immunol. 2017 Feb;82:114-122. doi: 10.1016/j.molimm.2017.01.003.
Wenchun Fan 1,  Tingting Liu 1,  Xiangmin Li 2,  Yun Zhou 1,  Mengge Wu 1,  Xiaofang Cui 1,  Huanchun Chen 2,  Ping Qian 3
Affiliations

Affiliations

  • 1 State Key Laboratory of Agricultural Microbiology, Huazhong Agricultural University, Wuhan 430070, China; Division of Animal Infectious Diseases, College of Veterinary Medicine, Huazhong Agricultural University, Wuhan 430070, China.
  • 2 State Key Laboratory of Agricultural Microbiology, Huazhong Agricultural University, Wuhan 430070, China; Division of Animal Infectious Diseases, College of Veterinary Medicine, Huazhong Agricultural University, Wuhan 430070, China; The Cooperative Innovation Center for Sustainable Pig Production, Huazhong Agricultural University, Wuhan 430070, China.
  • 3 State Key Laboratory of Agricultural Microbiology, Huazhong Agricultural University, Wuhan 430070, China; Division of Animal Infectious Diseases, College of Veterinary Medicine, Huazhong Agricultural University, Wuhan 430070, China; The Cooperative Innovation Center for Sustainable Pig Production, Huazhong Agricultural University, Wuhan 430070, China. Electronic address: [email protected].
PMID: 28073078 DOI: 10.1016/j.molimm.2017.01.003
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.

Keywords

Nuclear factor-kappa B (NF-κB); Pro-inflammatory cytokine; Signaling transduction; TRIM52.

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