去泛素化酶7与髓样分化因子88蛋白相互作用的研究

摘要

The toll like receptor (TLR) plays central roles in recognizing microbial molecules and actives the innate immune response. Here, we applied co-immunoprecipitation, co-locolization and indirect co-locolization to identify the interaction of ubiquitin-specific-processing protease 7CUSP7) with myeloid differentiation primary response gene (MyD88) which is the critical adaptor in TLR signal pathway. The results showed that the two proteins could co-locate in the same cytoplasm and interacted with each other. The research can enrich the knowledge of TLR pathway and may play a theorical and practical value on the treatment of TLR pathway related diseases.%Toll-like受体(TLRs)介导的信号途径不仅参与机体识别病原微生物入侵、诱导免疫应答,而且还可诱导机体产生破坏性炎症反应.通过免疫共沉淀、免疫荧光共定位、间接免疫荧光等实验方法鉴定去泛素化酶7 (USP7)和TLR信号途径中重要接头蛋白——髓样分化因子88(MyD88)的相互作用,结果表明USP7和MyD88可在细胞质中共定位并可发生相互作用.该研究对阐释TLR信号通路的机制奠定了重要的基础.