| pubmed-article:10648602 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10648602 | lifeskim:mentions | umls-concept:C0205112 | lld:lifeskim |
| pubmed-article:10648602 | lifeskim:mentions | umls-concept:C0754623 | lld:lifeskim |
| pubmed-article:10648602 | lifeskim:mentions | umls-concept:C0439855 | lld:lifeskim |
| pubmed-article:10648602 | lifeskim:mentions | umls-concept:C1948023 | lld:lifeskim |
| pubmed-article:10648602 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
| pubmed-article:10648602 | lifeskim:mentions | umls-concept:C1879547 | lld:lifeskim |
| pubmed-article:10648602 | lifeskim:mentions | umls-concept:C0348080 | lld:lifeskim |
| pubmed-article:10648602 | pubmed:issue | 4 | lld:pubmed |
| pubmed-article:10648602 | pubmed:dateCreated | 2000-2-15 | lld:pubmed |
| pubmed-article:10648602 | pubmed:abstractText | Signal-induced nuclear expression of the eukaryotic NF-kappaB transcription factor involves the stimulatory action of select mitogen-activated protein kinase kinase kinases on the IkappaB kinases (IKKalpha and IKKbeta) which reside in a macromolecular signaling complex termed the signalsome. While genetic studies indicate that IKKbeta is the principal kinase involved in proinflammatory cytokine-induced IkappaB phosphorylation, the function of the equivalently expressed IKKalpha is less clear. Here we demonstrate that assembly of IKKalpha with IKKbeta in the heterodimeric signalsome serves two important functions: (i) in unstimulated cells, IKKalpha inhibits the constitutive IkappaB kinase activity of IKKbeta; (ii) in activated cells, IKKalpha kinase activity is required for the induction of IKKbeta. The introduction of kinase-inactive IKKalpha, activation loop mutants of IKKalpha, or IKKalpha antisense RNA into 293 or HeLa cells blocks NIK (NF-kappaB-inducing kinase)-induced phosphorylation of the IKKbeta activation loop occurring in functional signalsomes. In contrast, catalytically inactive mutants of IKKbeta do not block NIK-mediated phosphorylation of IKKalpha in these macromolecular signaling complexes. This requirement for kinase-proficient IKKalpha to activate IKKbeta in heterodimeric IKK signalsomes is also observed with other NF-kappaB inducers, including tumor necrosis factor alpha, human T-cell leukemia virus type 1 Tax, Cot, and MEKK1. Conversely, the theta isoform of protein kinase C, which also induces NF-kappaB/Rel, directly targets IKKbeta for phosphorylation and activation, possibly acting through homodimeric IKKbeta complexes. Together, our findings indicate that activation of the heterodimeric IKK complex by a variety of different inducers proceeds in a directional manner and is dependent on the kinase activity of IKKalpha to activate IKKbeta. | lld:pubmed |
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| pubmed-article:10648602 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10648602 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10648602 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:10648602 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:10648602 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:10648602 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10648602 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:10648602 | pubmed:issn | 0270-7306 | lld:pubmed |
| pubmed-article:10648602 | pubmed:author | pubmed-author:GreeneW CWC | lld:pubmed |
| pubmed-article:10648602 | pubmed:author | pubmed-author:LieAA | lld:pubmed |
| pubmed-article:10648602 | pubmed:author | pubmed-author:GeleziunasRR | lld:pubmed |
| pubmed-article:10648602 | pubmed:author | pubmed-author:O'MahonyAA | lld:pubmed |
| pubmed-article:10648602 | pubmed:issnType | Print | lld:pubmed |
