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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 Toll/Interleukin-1 receptor (TIR) domain. Upon activation, TLRs associate with a number of cytoplasmic adaptor proteins containing TIR domains, including myeloid differentiation factor 88 (MyD88), MyD88-adaptor-like/TIR-associated protein (MAL/TIRAP), Toll-receptor-associated activator of interferon (TRIF), and Toll-receptor-associated molecule (TRAM). 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, which normally maintains NF-kappaB in an inactive state by sequestering it in the cytoplasm. Tollip (Toll interacting protein) is an adaptor protein discovered to be associated with the IRAK complex and recruited to IL1-R following IL-1 stimulation . Overexpression of Tollip results in impaired NF-kappaB signaling . Tollip also associates directly with TLR2 and TLR4 and inhibits TLR-mediated signaling through inhibition of IRAK . Studies of Tollip deficient mice suggest that it plays a role in the regulation of inflammatory cytokines in response to IL-1 and LPS . Synonyms: FLJ33531, IL-1RAcPIP,