Helicobacter pylori regulates TIFA turnover in gastric epithelial cells.

被引:4
|
作者
Sokolova, Olga [1 ]
Maubach, Gunter [1 ]
Naumann, Michael [1 ]
机构
[1] Otto Von Guericke Univ, Inst Expt Internal Med, Med Fac, D-39120 Magdeburg, Germany
关键词
ADP-heptose; Bacteria; Inflammation; NF-?B; Proteasome; Lysosome; Ubiquitin; NF-KAPPA-B; TRAF2; BINDING-PROTEIN; ACTIVATION; OLIGOMERIZATION; INFLAMMATION; DEGRADATION; EXPRESSION; INHIBITORS; CANCER; ALPHA;
D O I
10.1016/j.ejcb.2023.151307
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
The human pathogen Helicobacter pylori induces a strong inflammatory response in gastric mucosa manifested by the recruitment of neutrophils and macrophages to the places of infection, and by changes in epithelial integrity and function. At the molecular level, this innate immune response is essentially dependent on the activation of NF-?B transcription factors regulating the expression of chemotactic factors, e.g., IL-8. Recently, it has been demonstrated that the NF-?B signaling pathway is triggered by the bacterial heptose metabolites, which activate the host ALPK1-TIFA axis. TIFA has been suggested to promote oligomerization and activity of the E3 ubiquitin ligase TRAF6, which further stimulates TAK1-IKK signaling. Here, we demonstrate that ALPK1-dependent TIFA activation in H. pylori-infected gastric epithelial cells is followed in time by a decline in TIFA levels, and that this process is impeded by inhibitors of the proteasomal and lysosomal degradation. According to our data, TRAF2, TRAF6, TAK1 or NEMO are not required for TIFA degradation. Additionally, H. pylori promotes the interaction of TIFA with free polyubiquitin as well as with optineurin, TAX1BP1 and LAMP1, which are known protein adaptors involved in intracellular trafficking to lysosomes.
引用
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页数:14
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