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The ubiquitin-modifying enzyme A20 is required for termination of Toll-like receptor responses.

Nature immunology | Oct 29, 2004

http://www.ncbi.nlm.nih.gov/pubmed/15334086

A20 is a cytoplasmic protein required for the termination of tumor necrosis factor (TNF)-induced signals. We show here that mice doubly deficient in either A20 and TNF or A20 and TNF receptor 1 developed spontaneous inflammation, indicating that A20 is also critical for the regulation of TNF-independent signals in vivo. A20 was required for the termination of Toll-like receptor-induced activity of the transcription factor NF-kappaB and proinflammatory gene expression in macrophages, and this function protected mice from endotoxic shock. A20 accomplished this biochemically by directly removing ubiquitin moieties from the signaling molecule TRAF6. The critical function of this deubiquitinating enzyme in the restriction of TLR signals emphasizes the importance of the regulation of ubiquitin conjugation in innate immune cells.

Pubmed ID: 15334086 RIS Download

Mesh terms: Animals | Antigens, CD | Cysteine Endopeptidases | Intracellular Signaling Peptides and Proteins | Lipopolysaccharides | Macrophages | Membrane Glycoproteins | Mice | Mice, Inbred C57BL | NF-kappa B | Nuclear Proteins | Proteins | Receptors, Cell Surface | Receptors, Tumor Necrosis Factor | Receptors, Tumor Necrosis Factor, Type I | Shock, Septic | Signal Transduction | TNF Receptor-Associated Factor 6 | Toll-Like Receptors | Tumor Necrosis Factor-alpha | Ubiquitin

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Associated grants

  • Agency: NIDDK NIH HHS, Id: DK42086
  • Agency: NIGMS NIH HHS, Id: GM07281
  • Agency: NIAID NIH HHS, Id: R01AI53224
  • Agency: NIDDK NIH HHS, Id: R01DK52751

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