Takeuchi O, Akira S
Department of Host Defense, Research Institute for Microbial Diseases, Osaka University, 3-1 Yamadaoka, Suita, Osaka 565-0871, Japan.
Curr Top Microbiol Immunol. 2002;270:155-67. doi: 10.1007/978-3-642-59430-4_10.
Myeloid differentiation factor 88 (MyD88) is an adaptor molecule composed of an N-terminal death domain and a C-terminal Toll/interleukin (IL)-1R homology domain. Ligand binding to Toll-like receptor (TLR)/IL-1R family members results in the association of MyD88 to the cytoplasmic tail of receptors; this then initiates the signaling cascade that leads to the activation of nuclear factor-kappa B and mitogen-activated protein kinases. Analysis of MyD88-deficient mice revealed its essential role in TLR/IL-1R signaling as well as in both the innate and the adaptive immune response.
髓样分化因子88（MyD88）是一种衔接分子，由N端死亡结构域和C端Toll样受体/白细胞介素（IL）-1受体同源结构域组成。配体与Toll样受体（TLR）/IL-1受体家族成员结合会导致MyD88与受体的胞质尾部结合；随后启动信号级联反应，导致核因子-κB和丝裂原活化蛋白激酶的激活。对MyD88缺陷小鼠的分析揭示了其在TLR/IL-1R信号传导以及先天性和适应性免疫反应中的重要作用。
