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TIRAP: an adapter molecule in the Toll signaling pathway.

Nature immunology | Sep 29, 2001

Mammalian Toll-like receptors (TLRs) recognize conserved products of microbial metabolism and activate NF-kappa B and other signaling pathways through the adapter protein MyD88. Although some cellular responses are completely abolished in MyD88-deficient mice, TLR4, but not TLR9, can activate NF-kappa B and mitogen-activated protein kinases and induce dendritic cell maturation in the absence of MyD88. These differences suggest that another adapter must exist that can mediate MyD88-independent signaling in response to TLR4 ligation. We have identified and characterized a Toll-interleukin 1 receptor (TIR) domain-containing adapter protein (TIRAP) and have shown that it controls activation of MyD88-independent signaling pathways downstream of TLR4. We have also shown that the double-stranded RNA-binding protein kinase PKR is a component of both the TIRAP- and MyD88-dependent signaling pathways.

Pubmed ID: 11526399 RIS Download

Mesh terms: Adaptor Proteins, Signal Transducing | Amino Acid Sequence | Animals | Antigens, Differentiation | Cell Differentiation | Cell Line | Cloning, Molecular | CpG Islands | Dendritic Cells | Drosophila Proteins | HSP40 Heat-Shock Proteins | Humans | Lipopolysaccharides | Membrane Glycoproteins | Mice | Molecular Sequence Data | Mutation | Myeloid Differentiation Factor 88 | Receptors, Cell Surface | Receptors, Immunologic | Receptors, Interleukin-1 | Sequence Homology, Amino Acid | Signal Transduction | Toll-Like Receptor 4 | Toll-Like Receptor 9 | Toll-Like Receptors | eIF-2 Kinase

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Associated grants

  • Agency: NIAID NIH HHS, Id: AI44220-01

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