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IKK-1 and IKK-2: cytokine-activated IkappaB kinases essential for NF-kappaB activation.

Science (New York, N.Y.) | Oct 31, 1997

http://www.ncbi.nlm.nih.gov/pubmed/9346484

Activation of the transcription factor nuclear factor kappa B (NF-kappaB) is controlled by sequential phosphorylation, ubiquitination, and degradation of its inhibitory subunit IkappaB. A large multiprotein complex, the IkappaB kinase (IKK) signalsome, was purified from HeLa cells and found to contain a cytokine-inducible IkappaB kinase activity that phosphorylates IkappaB-alpha and IkappaB-beta. Two components of the IKK signalsome, IKK-1 and IKK-2, were identified as closely related protein serine kinases containing leucine zipper and helix-loop-helix protein interaction motifs. Mutant versions of IKK-2 had pronounced effects on RelA nuclear translocation and NF-kappaB-dependent reporter activity, consistent with a critical role for the IKK kinases in the NF-kappaB signaling pathway.

Pubmed ID: 9346484 RIS Download

Mesh terms: Cell Cycle Proteins | Cloning, Molecular | Dual Specificity Phosphatase 1 | Enzyme Activation | HeLa Cells | Helix-Loop-Helix Motifs | Humans | I-kappa B Kinase | Immediate-Early Proteins | Leucine Zippers | Molecular Sequence Data | NF-kappa B | Phosphoprotein Phosphatases | Phosphorylation | Protein Phosphatase 1 | Protein Tyrosine Phosphatases | Protein-Serine-Threonine Kinases | Sequence Homology, Amino Acid | Substrate Specificity

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