Solt Laura A, Madge Lisa A, May Michael J
Department of Animal Biology, University of Pennsylvania School of Veterinary Medicine, Philadelphia, Pennsylvania 19104, USA.
J Biol Chem. 2009 Oct 2;284(40):27596-608. doi: 10.1074/jbc.M109.047563. Epub 2009 Aug 7.
Proinflammatory NF-kappaB activation requires the IkappaB (inhibitor of NF-kappaB) kinase (IKK) complex that contains two catalytic subunits named IKKalpha and IKKbeta and a regulatory subunit named NF-kappaB essential modulator (NEMO). NEMO and IKKbeta are essential for tumor necrosis factor (TNF)-induced NF-kappaB activation, and we recently demonstrated that NEMO and IKKalpha are sufficient for interleukin (IL)-1-induced signaling. IKKalpha and IKKbeta both contain a functional NEMO-binding domain (NBD); however, the role of NEMO association with each kinase in NF-kappaB signaling and IKK complex formation remains unclear. To address this question, we stably reconstituted IKKalpha(-/-) and IKKbeta(-/-) murine embryonic fibroblasts (MEFs) with wild-type (WT) or NBD-deficient (DeltaNBD) versions of IKKalpha and IKKbeta, respectively. TNF-induced classical NF-kappaB activation in IKKbeta(-/-) MEFs was rescued by IKKbeta(WT) but not IKKbeta(DeltaNBD), whereas neither IKKbeta(WT) nor IKKbeta(DeltaNBD) affected IL-1-induced NF-kappaB signaling. As previously described, classical NF-kappaB transcriptional activity was absent in IKKalpha(-/-) cells. Reconstitution with either IKKalpha(WT) or IKKalpha(DeltaNBD) rescued both IL-1 and TNF-induced transcription, demonstrating that NEMO association is not required for IKKalpha-dependent regulation of NF-kappaB-dependent transcription. Stably expressed IKKalpha(WT) or IKKbeta(WT) associated with endogenous IKKs and NEMO in IKKalpha(-/-) or IKKbeta(-/-) MEFs, respectively, resulting in formation of the heterotrimeric IKKalpha-IKKbeta-NEMO complex. In contrast, although the IKKalpha(DeltaNBD) and IKKbeta(DeltaNBD) mutants associated with endogenous IKKs containing an NBD, these dimeric endogenous IKK-IKK(DeltaNBD) complexes did not associate with NEMO. These findings therefore demonstrate that formation of the heterotrimeric IKKalpha-IKKbeta-NEMO holocomplex absolutely requires two intact NEMO-binding domains.
促炎的核因子-κB(NF-κB)激活需要IκB(NF-κB抑制剂)激酶(IKK)复合物,该复合物包含两个名为IKKα和IKKβ的催化亚基以及一个名为NF-κB必需调节因子(NEMO)的调节亚基。NEMO和IKKβ对于肿瘤坏死因子(TNF)诱导的NF-κB激活至关重要,并且我们最近证明NEMO和IKKα足以介导白细胞介素(IL)-1诱导的信号传导。IKKα和IKKβ均含有功能性的NEMO结合结构域(NBD);然而,NEMO与每种激酶在NF-κB信号传导和IKK复合物形成中的作用仍不清楚。为了解决这个问题,我们分别用野生型(WT)或NBD缺陷型(ΔNBD)的IKKα和IKKβ稳定地重建了IKKα(-/-)和IKKβ(-/-)小鼠胚胎成纤维细胞(MEF)。IKKβ(WT)可挽救IKKβ(-/-)MEF中TNF诱导的经典NF-κB激活,但IKKβ(ΔNBD)不能,而IKKβ(WT)和IKKβ(ΔNBD)均不影响IL-1诱导的NF-κB信号传导。如前所述,IKKα(-/-)细胞中不存在经典的NF-κB转录活性。用IKKα(WT)或IKKα(ΔNBD)重建可挽救IL-1和TNF诱导的转录,表明IKKα依赖性调节NF-κB依赖性转录不需要NEMO结合。稳定表达的IKKα(WT)或IKKβ(WT)分别与IKKα(-/-)或IKKβ(-/-)MEF中的内源性IKK和NEMO结合,导致形成三聚体IKKα-IKKβ-NEMO复合物。相反,尽管IKKα(ΔNBD)和IKKβ(ΔNBD)突变体与含有NBD的内源性IKK结合,但这些二聚体内源性IKK-IKK(ΔNBD)复合物不与NEMO结合。因此,这些发现表明三聚体IKKα-IKKβ-NEMO全复合物的形成绝对需要两个完整的NEMO结合结构域。