细胞内泛素化调控是一个由泛素化和去泛素化协同调控的动态平衡可逆过程.去泛素酶(DUBs)是介导蛋白质去泛素化过程的蛋白质家族,它在许多复杂的细胞过程中发挥着关键作用,但其生物学特征尚未完全阐明.作为去泛素化酶的一种,USP 10在许多生物过程和癌症中都发挥重要的作用.为了进一步探索USP10在细胞中的功能,采用免疫沉淀与质谱联用(IP-MS)的方法鉴定USP10的相互作用蛋白质.通过Flag柱子的富集方式(Flag-USP10 IP-MS)共鉴定出165个与USP 10相互作用蛋白质.通过USP10内源抗体的富集方式(USP10 antibody IP-MS)鉴定出192个USP10相互作用蛋白质.基因本体(GO)分析表明,USP10的互作蛋白质中存在一组与无义介导的mRNA降解(NMD)相关蛋白质,包括无NMD的核心因子UPF1(Up-frameshift 1).进一步验证了USP10和UPF1在细胞质中共定位.此外,还确定了UPF1通过其HD结构域与全长的USP10相互作用.本研究提供了新的USP10相互作用蛋白质,为探索其在RNA调控和NMD通路中的重要性提供线索.“,”Regulation of the intracellular ubiquitination is a dynamic equilibrium reversible process,which is regulated by ubiquitination and deubiquitination.Deubiquitinases (DUBs) is a family of proteins that catalyze the deubiquitination of protein substrates.DUBs play a key role in many complex cellular processes,but the function and mechanism are not fully understood.USP10,a member of DUBs,is involved in multiple biological processes and tumor progression.To further explore the functions of USP10,we utilized immunoprecipitation coupled with mass spectrometry (IP-MS) to identify the interacting proteins of USP10.We identified 165 significant interacting proteins of USP10 by Flag-USP 10 IP-MS,and 192 significant interacting proteins using USP10 antibody IP-MS.The gene ontology (GO)term enrichment analysis revealed that there is a set of interactors related to nonsense-mediated mRNA decay (NMD),including UPF1 (Up-frameshift 1),a central factor of NMD.We further verified the subcellular colocalization of USP10 and UPF1 in cytoplasm.In addition,we also identified UPF1 interacts with full length USP10 through its HD domain.Our study identified new associated proteins of USP10 and provided important clues in understanding RNA regulation and NMD pathway.