Tewari M, Dixit V M
Department of Pathology, University of Michigan Medical School, Ann Arbor 41809-0602, USA.
Curr Opin Genet Dev. 1996 Feb;6(1):39-44. doi: 10.1016/s0959-437x(96)90008-8.
The past year has witnessed remarkable advances in the understanding of signaling by the two TNF (tumor necrosis factor) receptors, TNFR1 and TNFR2, and the related CD40 receptor. Adaptor molecules (termed TRAFs) have been identified that associate with TNFR2 and CD40 and function to modulate the signaling pathways. Significantly, TRAF2 mediates the activation of NF-kappa B by both receptors. Furthermore, a molecule called TRADD has been identified that associates with the cytoplasmic segment of TNFR1. TRADD, which contains a novel 'death domain' that binds to the corresponding death domain in the cytoplasmic segment of TNFR1, can mediate both activation of NF-kappa B and induction of apoptosis, the two major responses signaled by TNFR1.
过去一年里，在对两种肿瘤坏死因子（TNF）受体TNFR1和TNFR2以及相关CD40受体信号传导的理解方面取得了显著进展。已鉴定出与TNFR2和CD40相关联并调节信号通路功能的衔接分子（称为TRAFs）。值得注意的是，TRAF2介导这两种受体对核因子κB的激活。此外，还鉴定出一种名为TRADD的分子，它与TNFR1的细胞质片段相关联。TRADD含有一个新的“死亡结构域”，可与TNFR1细胞质片段中的相应死亡结构域结合，它既能介导核因子κB的激活，又能诱导细胞凋亡，这是TNFR1发出信号的两种主要反应。
