The nuclear factor NF-?B controls the expression of many genes and has been shown to play a role in inflammation, coagulation and apoptosis. Under normal conditions NF-?B is bound to its inhibitor I?B, and the complex remains in the cytoplasm. Degradation of the I?B leaves NF-?B free to cross the nuclear membrane and bind to the promoter regions of genes and activate transcription. Tumour necrosis factor (TNF) is known to initiate one pathway for NF-?B activation. Association of TNF with TNFR1 causes the formation of a complex involving TRAF2 and NIK, which results in NF-?B activation through degradation of its inhibitor. Binding of TNF to TNF receptor type 1 (TNRF1) also activates phosphatidylinositol-3-OH kinase (PI3K), which in turn activates the serine/threonine kinase Akt. As activated Akt is formed through a branch of the TNF pathway, the authors sought to identify whether this also plays a role in activation of NF-?B.