TRAFs家族是一类多功能蛋白,最初是作为TNFR介导的信号通路中的转导分子而被发现的。TRAFs作为信号接头蛋白和调节分子,参与了TNFR、TLRs、NLRs和RLRs等多种受体介导的信号通路。TRAF7是最新发现的TRAF家族成员,因其保守的RING结构域,而具有E3泛素连接酶活性。此外,TRAF7还以其独特机制参与了MAP激酶、TNFR及TLR2介导的信号通路的转导,以及细胞应激、分化和凋亡等重要生理过程的调控,与乳腺癌、脑膜瘤等多种疾病的发生密切相关。结合最新研究进展对TRAF7的结构、功能及其参与的生物学过程进行综述。
The tumor necrosis factor receptor( TNF-R)-associated factor( TRAF) family was originally identified as signaling adaptors that directly bind to the cytoplasmic regions of receptors of the TNF-R superfamily.TRAFs have also been identified to function in signaling for TLRs,NLRs,RLRs,etc. TRAF7,the most recently identified member,acts as an E3 ubiquitin ligase with its conserved RING finger domain,essential for signal transduction pathways mediated by TNFR and TLR2. In addition, TRAF7 also regulates the activation of cellularstress pathways,as well as unconventional ubiquitination events,the differentiation of muscle tissue and tumorigenesis. The most recent advances in the understanding of TRAF7 function and the biological processes this protein is involved in.