肿瘤坏死受体相关因子(TRAF)最早是通过与TNFR2特异结合而被发现的。在TRAF家族中,只有TRAF1在N端缺失环指结构。TRAF1可以和TNFR超家族中的很多成员相关,并且可以结合多个蛋白激酶以及接头蛋白,因此,TRAF1很有可能在细胞信号网络中发挥重要作用。近些年,在分子、细胞学水平上,我们对TRAF1的功能有许多新的了解,本文就这些研究进展做简要综述。 Tumor necrosis factor receptor (TRAF) was first discovered by its specific binding to TNFR2. In the TRAF family, only TRAF1 lacks the ring finger structure at the N-terminus. TRAF1 is associated with many members of the TNFR superfamily and binds multiple protein kinases and adapter proteins, so TRAF1 is likely to play an important role in cellular signaling networks. In recent years, we have many new understandings on the function of TRAF1 at the molecular and cytological level. This article briefly reviews the progress of these studies.