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The myeloid differentiation protein MyD88 was originally characterized as a protein upregulated in myeloleukemic cells following IL-6-induced growth arrest and terminal differentiation. MyD88 is now known to function as an adaptor protein for the association of IRAK with the IL-1 receptor. It contains an amino-terminal death domain separated from a carboxyl-terminal TIR domain and functions as an adaptor in TLR/IL-1 receptor signaling. The death domain of MyD88 mediates interactions with the IRAK complex triggering a signaling cascade that includes the activation of NF-κB.


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