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The recognition of microbial pathogens by the innate immune system involves Toll-like receptors (TLRs), which recognize pathogen-associated molecular patterns^,,,,,,,,. Different TLRs recognize different pathogen-associated molecular patterns, with TLR-4 mediating the response to lipopolysaccharide from Gram-negative bacteria^,,. All TLRs have a Toll/IL-1 receptor (TIR) domain, which is responsible for signal transduction^,. MyD88 is one such protein that contains a TIR domain^,. It acts as an adapter, being involved in TLR-2, TLR-4 and TLR-9 signalling^,,,; however, our understanding of how TLR-4 signals is incomplete^,. Here we describe a protein, Mal (MyD88-adapter-like), which joins MyD88 as a cytoplasmic TIR-domain-containing protein in the human genome. Mal activates NF-κB, Jun amino-terminal kinase and extracellular signal-regulated kinase-1 and -2. Mal can form homodimers and can also form …