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TIRAP: an adapter molecule in the Toll signaling pathway.

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


  • Horng T
  • Barton GM
  • Medzhitov R


Nature immunology

Publication Data

September 29, 2001

Associated Grants

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

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