A20 inhibits NF-kappaB activation by dual ubiquitin-editing functions.
A20 inhibits NF-kappaB activation by dual ubiquitin-editing functions.
复制标题
DOI：
--
复制
发表时间：
2005
影响因子：
13.8
通讯作者：
K. Heyninck;R. Beyaert
中科院分区：
文献类型：
--
作者：
K. Heyninck;R. Beyaert
转录因子NF-κ B的失调可以介导除癌症之外的几种炎性疾病。因此，包括锌指蛋白A20在内的几种蛋白质严格控制其激活。最近，人们描述了A20响应促炎细胞因子肿瘤坏死因子（TNF）而下调NF-kappaB激活的潜在机制。A20显示出两种相反的活性：TNF受体相互作用蛋白（RIP）的顺序去泛素化和泛素化，从而将RIP靶向蛋白酶体降解。
Deregulation of the transcription factor NF-kappaB can mediate several inflammatory diseases in addition to cancer. Therefore, several proteins, including the zinc finger protein A20, tightly control its activation. Recently, the underlying mechanism by which A20 downregulates NF-kappaB activation in response to the pro-inflammatory cytokine tumor necrosis factor (TNF) has been described. A20 was shown to exert two opposing activities: sequential de-ubiquitination and ubiquitination of the TNF receptor-interacting protein (RIP), thereby targeting RIP to proteasomal degradation.