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Chakraborty S Senyuk V Sitailo S Chi Y Nucifora G 《The Journal of biological chemistry》2001,276(48):44936-44943
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Yihui Fan Yang Yu Yi Shi Wenjing Sun Min Xie Ningling Ge Renfang Mao Alex Chang Gufeng Xu Michael D. Schneider Hong Zhang Songbin Fu Jun Qin Jianhua Yang 《The Journal of biological chemistry》2010,285(8):5347-5360
Transforming growth factor-β-activated kinase 1 (TAK1) plays an essential role in the tumor necrosis factor α (TNFα)- and interleukin-1β (IL-1β)-induced IκB kinase (IKK)/nuclear factor-κB (NF-κB) and c-Jun N-terminal kinase (JNK)/activator protein 1 (AP-1) activation. Here we report that TNFα and IL-1β induce Lys63-linked TAK1 polyubiquitination at the Lys158 residue within the kinase domain. Tumor necrosis factor receptor-associated factors 2 and 6 (TRAF2 and -6) act as the ubiquitin E3 ligases to mediate Lys63-linked TAK1 polyubiquitination at the Lys158 residue in vivo and in vitro. Lys63-linked TAK1 polyubiquitination at the Lys158 residue is required for TAK1-mediated IKK complex recruitment. Reconstitution of TAK1-deficient mouse embryo fibroblast cells with TAK1 wild type or a TAK1 mutant containing a K158R mutation revealed the importance of this site in TNFα and IL-1β-mediated IKK/NF-κB and JNK/AP-1 activation as well as IL-6 gene expression. Our findings demonstrate that Lys63-linked polyubiquitination of TAK1 at Lys158 is essential for its own kinase activation and its ability to mediate its downstream signal transduction pathways in response to TNFα and IL-1β stimulation. 相似文献
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