IKKα is a member of the serine/threonine protein kinase family. The protein, a component of a cytokine-activated protein complex that is an inhibitor of the essential transcription factor NF-kappa-B complex, phosphorylates sites that trigger the degradation of the inhibitor via the ubiquination pathway, thereby activating the transcription factor. The classical active IKK complex, composed of IKK alpha, IKK beta, and two forms of processed IKK gamma, phosphorylates and inactivates IkB, resulting in the release and nuclear translocation of active NFkB. IKK-a specifically phosphorylates IkB-alpha. Phosphorylation of IkB by IKKå is stimulated by the NFkB inducing kinase (NIK), which itself is a central regulator for NFkB activation in response to TNF and IL-1.
