"NF-κB" activation is initiated by DAG, the second, membrane bound product of PLCγ hydrolysation of PIP2. DAG binds and recruits Protein kinase C θ (PKCθ) to the membrane where it can activated the membrane bound scaffold protein CARMA1. CARMA1 then undergoes a conformational change which allow it to oligomerise and bind the adapter proteins BCL10, CARD domain and MALT1. This multisubunit complex binds the Ubiquitin ligase TRAF6. Ubiquitination of TRAF6 serves as scaffold to recruit NEMO, IκB kinase (IKK) and TAK1. TAK 1 phosphorylates IKK, which in turn phosphorylates the NF-κB inhibitor I-κB, leading to the ubiquitination and subsequent degradation of I-κB.