International Immunology · 1999 · 372 citations · 19 references
Life SciencesImmunologyMolecular BiologyInflammationInnate ImmunitySignal TransductionCytokine BiologyCytokine RegulationInflammatory SignalingInnate Immune Signaling PathwaysMacrophage BiologyProtein Kinase CascadesBasic Leucine Zipper DomainsHelix-loop-helix MotifImmune Stress ResponseLeucine Zipper ProteinsMacrophage Signaling PathwaysNf-κb SignalingPhosphorylation Cascades In Immune CellsProinflammatory Mediators
Using the suppression subtractive hybridization technique, we isolated a novel kinase, IKK-i, whose message is drastically induced by lipopolysaccharide (LPS) in the mouse macrophage cell line RAW264. 7. The predicted protein contains the kinase domain in its N-terminus, which shares 30% identity to that of IKK-alpha or IKK-beta. The C-terminal portion contains a leucine zipper and a potential helix-loop-helix domain, as in the case of IKK-alpha and IKK-beta. IKK-i is expressed mainly in immune cells, and is induced in response to proinflammatory cytokines such as tumor necrosis factor-alpha, IL-1 and IL-6, in addition to LPS. Overexpression of wild-type IKK-i phosphorylated serine residues Ser32 and Ser36 of IkappaB-alpha (preferentially Ser36), and significantly stimulated NF-kappaB activation. These results suggest that IKK-i is an inducible IkappaB kinase which may play a special role in the immune response.
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Luda Diatchenko, Yun‐Fai Chris Lau, A. Patricia Campbell et al. · Proceedings of the National Academy of Sciences · 1996 · 3K citations
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A cytokine-responsive IκB kinase that activates the transcription factor NF-κB
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