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- _6 value "Upon binding of IL-1 to IL-1RI, an IL-1RAcP is recruited to form a high affinity IL-1R1-IL-1RAcP heterodimeric receptor, which initiates the downstream signaling cascade. The trimeric complex rapidly assembles MyD88 and IRAK4 and forms a stable IL-1-induced first signaling module, which subsequently phosphorylates IRAK1 and IRAK2, and recruits TRAF6. Complexes of IRAK1, IRAK2 and TRAF6 dissociate from the initial receptor complex and promote TGF?-activated protein kinase (TAK)1/TAK-binding protein (TAB)1 association, which is followed by the activation of NF?B, JNK and p38 MAPK pathways. Activation of the IKK complex by IL-1 promotes I?B? ubiquitination. The nuclear translocation of NF?B with the nuclear translocation of c-JUN, induced by the activation of JNK and p38 MAPK, modulates the gene expression of IL-6, TNF?, IL-1?, IFN?, IFN? and TGF?. Multiple negative regulators of this pathway, including inhibitory IL-RII, secreted soluble (s)IL-1RI and sIL-RII, regulatory IL-1R1a and SIGIRR provide a negative feedback control of this pathway and suppress excessive IL-1 signaling." provenance.
- _6 wasQuotedFrom 21776333 provenance.