The expanding family of MyD88-like adaptors in Toll-like receptor signal transduction

• Published in: Molecular Immunology 2004-07, Vol.41 (6), p.577-582
• Main Authors: McGettrick, Anne F, O’Neill, Luke A.J
• Format: Article
• Language: English
• Subjects: Adaptor Proteins, Vesicular Transport - metabolism; Animals; Armadillo Domain Proteins; Cytoskeletal Proteins; Host defense; Humans; Mal; Membrane Glycoproteins - genetics; Membrane Glycoproteins - metabolism; Multigene Family; MyD88; Receptors, Cell Surface - metabolism; Receptors, Interleukin-1 - genetics; Receptors, Interleukin-1 - metabolism; SARM; Signal transduction; Signal Transduction - genetics; Signal Transduction - physiology; Toll-Like Receptors; TRAM; Trif
• ISSN: 0161-5890; 1872-9142; 1365-2567
• DOI: 10.1016/j.molimm.2004.04.006

Toll-like receptors (TLRs) play an essential role in the detection and elimination of invading microbes. They are type-1 transmembrane receptors, containing extracellular leucine rich repeats and an intracellular Toll/interleukin-1 receptor (TIR) domain. Upon stimulation, these receptors interact with specific TIR domain-containing adaptor proteins. Five such adaptors have been discovered to date, MyD88, Mal (MyD88 adaptor-like)/TIRAP (TIR domain-containing adaptor protein), Trif (TIR-domain-containing adaptor inducing interferon-β), TRAM (Trif-related adaptor molecule) and SARM (SAM and ARM-containing protein). Different TLRs use different combinations of these adaptors, leading to the activation of common and unique pathways involved in the elimination of the invading microbe.