Inhibitor of kappaB kinase beta Adenovirus (Ad-IKKb)

The IkB kinases, IKK (alpha) (previously designated CHUK) and IKK (beta), are members of the helix-loop-helix, leucine zipper family of interacting proteins. IKK (alpha) specifically phosphorylates IkB (alpha) on the sites, serines 32 and 36, to trigger its degradation. The IKK complex appears to be critical for NFkB activation in response to proinflammatory cytokines. Phosphorylation of IkB by IKK (alpha) is stimulated by the NFkB inducing kinase (NIK), which itself is a central regulator for NFkB activation. The functional IKK complex contains three subunits, IKK (alpha), IKK (beta) and IKK (gamma) (also designated NEMO, for NFkB essential modulator), and each appear to make essential contributions to IkB phosphorylation. TANK binding kinase (TBK1), also designated T2K, is an IKK-related kinase that complexes with TRAF2 and TANK in the NF?B activation pathway. IKK-i is an IKK-related serine/threonine kinase that is expressed in immune cells and is inducible by LPS, TNF (alpha), IL-1 and IL-6. Overexpression of IKK-i results in IkB (alpha) phosphorylation and NFkB activation.