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Cyclophilin J limits inflammation through the blockage of ubiquitin chain sensing

Author

Listed:
  • Chunjie Sheng

    (Collaborative Innovation Center of Cancer Medicine)

  • Chen Yao

    (Collaborative Innovation Center of Cancer Medicine)

  • Ziyang Wang

    (Collaborative Innovation Center of Cancer Medicine)

  • Hongyuan Chen

    (Guangdong Pharmaceutical University)

  • Yu Zhao

    (Mayo Clinic College of Medicine)

  • Dazhi Xu

    (Collaborative Innovation Center of Cancer Medicine)

  • Haojie Huang

    (Mayo Clinic College of Medicine)

  • Wenlin Huang

    (Collaborative Innovation Center of Cancer Medicine)

  • Shuai Chen

    (Collaborative Innovation Center of Cancer Medicine)

Abstract

Maintaining innate immune homeostasis is important for individual health. Npl4 zinc finger (NZF) domain-mediated ubiquitin chain sensing is reported to function in the nuclear factor-kappa B (NF-κB) signal pathway, but the regulatory mechanism remains elusive. Here we show that cyclophilin J (CYPJ), a member of the peptidylprolyl isomerase family, is induced by inflammation. CYPJ interacts with the NZF domain of transform growth factor-β activated kinase 1 binding protein 2 and 3 as well as components of the linear ubiquitin chain assembly complex to block the binding of ubiquitin-chain and negatively regulates NF-κB signaling. Mice with Cypj deficiency are susceptible to lipopolysaccharide and heat-killed Listeria monocytogenes-induced sepsis and dextran sulfate sodium-induced colitis. These findings identify CYPJ as a negative feedback regulator of the NF-κB signaling pathway, and provide insights for understanding the homeostasis of innate immunity.

Suggested Citation

  • Chunjie Sheng & Chen Yao & Ziyang Wang & Hongyuan Chen & Yu Zhao & Dazhi Xu & Haojie Huang & Wenlin Huang & Shuai Chen, 2018. "Cyclophilin J limits inflammation through the blockage of ubiquitin chain sensing," Nature Communications, Nature, vol. 9(1), pages 1-13, December.
    • Handle: RePEc:nat:natcom:v:9:y:2018:i:1:d:10.1038_s41467-018-06756-3
    DOI: 10.1038/s41467-018-06756-3
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