Most Toll-like receptors (TLRs) are believed to act as homodimers, although heterodimers do exist. The Toll interleukin-1 receptor (TIR) domain adaptors, MyD88, MAL/TIRAP, TRAM, and TRIF, also associate with one another as they induce translocation of transcription factors like NF-κB and IRF-3 into the nucleus (Adapted from B. Beutler,
Innate immunity, the first line of defense against infection, has revealed surprising complexity for what is considered a relatively primitive and conserved function. A diverse array of Toll-like receptors (TLRs) serves to recognize specific components of foreign invaders. Each TLR contains a Toll interleukin-1 receptor (TIR) domain that recruits IL-1R-associated kinases via adaptor molecules. These adaptors induce nuclear translocation of transcription factors like NF-κB or IRF-3, which turn on a variety of cytokines, including IFN-β and IFN-α, and subsequently a large number of interferon-stimulated genes. Most TLRs have been shown to signal through the adaptor protein myeloid differentiation ...
