IKAP is a scaffold protein of the IκB kinase complex

Lucie Cohen, William J. Henzel and Patrick A. Baeuerle ()
Additional contact information
Lucie Cohen: Tularik Inc.
William J. Henzel: Genentech Inc.
Patrick A. Baeuerle: Tularik Inc.

Nature, 1998, vol. 395, issue 6699, 292-296

Abstract: Abstract The transcription factor NF-κB coordinates the activation of numerous genes in response to pathogens and pro-inflammatory cytokines, and is, therefore, vital in the development of acute and chronic inflammatory diseases1,2,3,4,5,6. NF-κB is activated by phsophorylation of its inhibitory subunit, IκB-α (ref. 7), on serine residues 32 and 36 by cytokine-activated IκB kinases (IKKs); this phosphorylation precedes rapid degradation of IκB8,9,10,11. IKK-α and IKK-β isozymes are found in large complexes of relative molecular mass 700,000–900,000 (Mr 70K–90K), but little is known about other components that organize and regulate these complexes12,13,14,15,16,17. IKK-α was independently discovered as a NF-κB-inducing kinase18 (NIK)-associated protein in a yeast two-hybrid screen19, and IKK-β was also identified by homology screening20. It is, however, unknown whether NIK is part of the IKK complex. Here we isolate large, interleukin-1-inducible IKK complexes that contain NIK, IKK-α, IKK-β, IκB-α, NF-κB/RelA and a protein of Mr 150K. This latter component is a new protein, termed IKK-complex-associated protein (IKAP), which can bind NIK and IKKs and assemble them into an active kinase complex. We show that IKAP is a scaffold protein and a regulator for threedifferent kinases involved in pro-inflammatory cytokine signalling.

Date: 1998
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DOI: 10.1038/26254

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