NEMO subunit of IKK complex binds to activated IRAK1

NF-kappa-B essential modulator (NEMO, also known as IKKG abbreviated from Inhibitor of nuclear factor kappa-B kinase subunit gamma) is the regulatory subunit of the IKK complex which phosphorylates inhibitors of NF-kappa-B leading to dissociation of the inhibitor/NF-kappa-B complex. NEMO binds to K63-pUb chains (Ea et al. 2006; Wu et al. 2006), linking K63-pUb-hp-IRAK1 with the IKK complex. Models of IL-1R dependent activation of NF-kappaB suggest that the polyubiquitination of both TRAF6 and IRAK1 within a TRAF6:IRAK1 complex and their subsequent interactions with the TAK1 complex and IKK complex respectively brings these complexes into proximity, facilitating the TAK1-catalyzed activation of IKK (Moynagh, 2008).

NF-κB 信号通路关键调控因子（NEMO，亦称IKKG，源自于核因子κ-B激酶亚基γ的抑制剂）是IKK复合体的调节亚基，其功能在于磷酸化NF-κB的抑制剂，进而导致抑制剂/NF-κB复合物的解离。NEMO能够与K63-泛素化修饰的链（Ea等，2006；Wu等，2006）结合，将K63-泛素化修饰的hp-IRAK1与IKK复合体相连接。针对依赖IL-1R的NF-κB激活模型研究表明，在TRAF6:IRAK1复合体内，TRAF6和IRAK1的泛素化修饰及其随后与TAK1复合体和IKK复合体的相互作用，使得这些复合体彼此靠近，从而促进了TAK1催化的IKK激活（Moynagh，2008）。