NEMO binds polyubiquitinated 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-kappa-B 的重要性调节因子（NEMO，亦称IKKG，由核因子κ-B激酶亚基γ抑制因子缩写而来）是IKK复合体的调控亚基，其通过磷酸化NF-kappa-B的抑制子导致抑制子/NF-kappa-B复合物的解离。NEMO与K63-pUb链（Ea等，2006；Wu等，2006）相结合，将K63-pUb-hp-IRAK1与IKK复合体相连接。关于IL-1R依赖性激活NF-kappaB的模型表明，在TRAF6:IRAK1复合物内，TRAF6和IRAK1的泛素化，以及它们随后分别与TAK1复合体和IKK复合体的相互作用，使得这些复合物彼此靠近，从而促进了TAK1催化的IKK激活（Moynagh，2008）。