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48887BiochemicalReaction2564

Source:http://www.reactome.org/biopax/48887BiochemicalReaction2564

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Authored: Shamovsky, V, 2012-04-19, Edited: Shamovsky, V, 2011-08-12, Reviewed: D'Eustachio, P, 2012-05-25, TIRAP/Mal-deficient mice showed normal responses to the TLR3, TLR5, TLR7, and TLR9 ligands, but were defective in TLR4 and TLR2 ligand-induced proinflammatory cytokine production (Horng et al. 2002,Yamamoto et al. 2002). In contrast, TLR4 ligand-induced activation of IRF-3 and expression of IFN-inducible genes were not impaired in TIRAP/Mal knockout macrophages or in mice lacking both MyD88 and TIRAP/Mal (Horng et al. 2002,Yamamoto et al. 2002). Thus, TIRAP/Mal is an essential adapter that is involved in the MyD88-dependent pathway via TLR4 and TLR2, but not in the MyD88-independent pathway. Mal contains a phosphatidylinositol 4,5-bisphosphate-binding domain required for retention in the plasma membrane. TLR2 or 4 associates with Mal on the cell surface, which in turn facilitates the binding of MyD88 to the activated TLR, leading to NF-kB and MAPK activation [Nunez Miguel et al 2007].<p>Bruton's tyrosine kinase (BTK) is a cytoplasmic tyrosine kinase, which plays an essential role in B cell receptor (BCR) signaling [Brunner C et al 2005]. BTK has been also implicated in TLR signaling [Lee KG et al 2012, Jefferies CA et al 2003]. Interaction studies revealed that BTK can associate with intracellular TIR-domains of TLRs 4, 6, 8 and 9. Furthermore, BTK was found to interact with other proteins involved in TLR2|4 signaling - MyD88, MAL and IRAK-1 [Jefferies CA et al 2003].
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MAL(TIRAP) and BTK bind to the activated TLR2|4
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