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Description
Members of the Toll-like receptor (TLR) family, named for the closely related Toll receptor in Drosophila, play a pivotal role in innate immune responses . TLRs recognize conserved motifs found in various pathogens and mediate defense responses. Triggering of the TLR pathway leads to the activation of NF-kappaB and subsequent regulation of immune and inflammatory genes. The TLRs and members of the IL-1 receptor family share a conserved stretch of approximately 200 amino acids known as the TIR domain. Upon activation, TLRs associate with a number of cytoplasmic adaptor proteins containing TIR domains including MyD88 (myeloid differentiation factor), MAL/TIRAP (MyD88-adaptor-like/TIR-associated protein), TRIF (Toll-receptor-associated activator of interferon), and TRAM (Toll-receptor-associated molecule). This association leads to the recruitment and activation of IRAK1 and IRAK4, which form a complex with TRAF6 to activate TAK1 and IKK. Activation of IKK leads to the degradation of IkappaB that normally maintains NF-kappaB inactivity by sequestering it in the cytoplasm. TLR3 functions as a receptor for double-stranded (ds)RNA typically associated with viral infection . It was originally shown to be specifically expressed in dendritic cells of the leukocyte family . TLR3 has also been found in placenta and lung, and can be induced by LPS in a variety of tissues . TLR3 is predominantly localized to early endosomes . Binding of dsRNA, or the analog polyinosine-polycytidylic acid (pIpC), to TLR3 triggers activation of transcription factors NF-kappaB and IRF3 through the adaptor protein TICAM-1/TRIF . TRIF associates with members of the TRAF family and with RIP that combine to activate NF-kappaB and IRF3 . Synonyms: TLR3,CD283 ,