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Overview
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IKKβ is a serine/threonine protein kinase that phosphorylates the I-kappa-B protein which is an inhibitor of the transcription factor NF-kappa-B complex. Phosphorylation of I-kappa-B protein triggers the degradation of the inhibitor via the ubiquitination pathway, thereby activating NF-kappa-B complex. The activity of IKKβ is stimulated by TNF and IL1 and IKKβ forms a heterodimer that interacts with NIK. Overexpression of catalytically inactive IKKβ blocks cytokine-induced NF-kappa-B activation. Aspirin and sodium salicylate can specifically inhibit IKKβ activity in vitro and in vivo by binding to IKKβ to reduce ATP binding.
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Overview