Key function for the Ubc13 E2 ubiquitin-conjugating enzyme in immune receptor signaling
Key function for the Ubc13 E2 ubiquitin-conjugating enzyme in immune receptor signaling
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DOI：
10.1038/ni1367
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发表时间：
2006-09-01
影响因子：
30.5
通讯作者：
Akira, Shizuo
中科院分区：
文献类型：
--
作者：
Yamamoto, Masahiro;Okamoto, Toru;Akira, Shizuo
UBC13E2泛素结合酶在用赖氨酸63连接的多泛素链‘标记’目标蛋白的过程中是关键的，这对于免疫受体信号的传递是必不可少的，最终导致转录因子NF-kappa B的激活。除肿瘤坏死因子外，UBC13基因缺失的细胞对所有刺激的反应显示出几乎正常的核因子-kappaB激活，但丝裂原激活蛋白激酶的激活明显减弱。UBC13诱导的丝裂原活化蛋白激酶的激活至少部分需要适配器蛋白IKKc的泛素化。这些结果表明，UBC13在哺乳动物的免疫反应中起着关键作用。
The Ubc13 E2 ubiquitin-conjugating enzyme is key in the process of 'tagging' target proteins with lysine 63-linked polyubiquitin chains, which are essential for the transmission of immune receptor signals culminating in activation of the transcription factor NF-kappa B. Here we demonstrate that conditional ablation of Ubc13 resulted in defective B cell development and in impaired B cell and macrophage activation. In response to all tested stimuli except tumor necrosis factor, Ubc13-deficient cells showed almost normal NF-kappa B activation but considerably impaired activation of mitogen- activated protein kinase. Ubc13-induced activation of mitogen- activated protein kinase required, at least in part, ubiquitination of the adaptor protein IKKc. These results show that Ubc13 is key in the mammalian immune response.