Regulation of NF-κB by deubiquitinases.
Regulation of NF-κB by deubiquitinases.
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DOI：
10.1111/j.1600-065x.2012.01100.x
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发表时间：
2012-03
影响因子：
8.7
通讯作者：
Dixit VM
中科院分区：
文献类型：
--
作者：
Harhaj EW;Dixit VM
核因子-κB （NF-κB）通路是先天免疫和适应性免疫的重要调节因子。非典型k63连接的多泛素化在NF-κB信号通路中发挥关键调节作用，通过作为支架募集含有泛素结合域的激酶复合物。泛素化是通过去泛素酶来平衡的，去泛素酶可以切割多泛素链，并反对E3泛素连接酶的功能。因此，去泛素酶在NF-κB信号的终止和炎症的消退中起着重要作用。本文就去泛素酶对NF-κB的调控进行综述，重点关注A20和CYLD。去泛素酶和调节NF-κB的泛素/蛋白酶体成分可能成为炎症性疾病和癌症的新治疗靶点。
The nuclear factor-κB (NF-κB) pathway is a critical regulator of innate and adaptive immunity. Noncanonical K63-linked polyubiquitination plays a key regulatory role in NF-κB signaling pathways by functioning as a scaffold to recruit kinase complexes containing ubiquitin-binding domains. Ubiquitination is balanced by deubiquitinases that cleave polyubiquitin chains and oppose the function of E3 ubiquitin ligases. Deubiquitinases therefore play an important role in the termination of NF-κB signaling and the resolution of inflammation. In this review, we focus on NF-κB regulation by deubiquitinases with an emphasis on A20 and CYLD. Deubiquitinases and the ubiquitin/proteasome components that regulate NF-κB may serve as novel therapeutic targets for inflammatory diseases and cancer.