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rdf:type |
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lifeskim:mentions |
umls-concept:C0035820,
umls-concept:C0429403,
umls-concept:C0596448,
umls-concept:C0851285,
umls-concept:C1412939,
umls-concept:C1416931,
umls-concept:C1417708,
umls-concept:C1423613,
umls-concept:C1456820,
umls-concept:C1511545,
umls-concept:C1514758,
umls-concept:C1539081,
umls-concept:C1705525,
umls-concept:C1822796
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pubmed:issue |
26
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pubmed:dateCreated |
2003-6-23
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pubmed:abstractText |
Tumor necrosis factor-alpha (TNF-alpha) and lymphotoxin-beta receptor (LTbetaR) signaling both play important roles in inflammatory and immune responses through activation of NF-kappaB. Using various deficient mouse embryonic fibroblast cells, we have compared the signaling pathways leading to NF-kappaB induction in response to TNF-alpha and LTbetaR activation. We demonstrate that LTbetaR ligation induces not only RelA/p50 dimers but also RelB/p50 dimers, whereas TNF-alpha induces only RelA/p50 dimers. LTbetaR-induced binding of RelB/p50 requires processing of p100 that is mediated by IKKalpha but is independent of IKKbeta, NEMO/IKKgamma, and RelA. Moreover, we show that RelB, p50, and p100 can associate in the same complex and that TNF-alpha but not LTbeta signaling increases the association of p100 with RelB/p50 dimers in the nucleus, leading to the specific inhibition of RelB DNA binding. These results suggest that the alternative NF-kappaB pathway based on p100 processing may account not only for the activation of RelB/p52 dimers but also for that of RelB/p50 dimers and that p100 regulates the binding activity of RelB/p50 dimers via at least two distinct mechanisms depending on the signaling pathway involved.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Chuk protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/DNA,
http://linkedlifedata.com/resource/pubmed/chemical/I-kappa B Kinase,
http://linkedlifedata.com/resource/pubmed/chemical/I-kappa B Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Ikbkb protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Ikbke protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Ltbr protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Lymphotoxin beta Receptor,
http://linkedlifedata.com/resource/pubmed/chemical/NF-kappa B,
http://linkedlifedata.com/resource/pubmed/chemical/NF-kappa B p50 Subunit,
http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Protein-Serine-Threonine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Tumor Necrosis Factor,
http://linkedlifedata.com/resource/pubmed/chemical/Relb protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Snd1 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factor RelB,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors,
http://linkedlifedata.com/resource/pubmed/chemical/Tumor Necrosis Factor-alpha
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
27
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pubmed:volume |
278
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
23278-84
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:12709443-Active Transport, Cell Nucleus,
pubmed-meshheading:12709443-Animals,
pubmed-meshheading:12709443-DNA,
pubmed-meshheading:12709443-Dimerization,
pubmed-meshheading:12709443-Fibroblasts,
pubmed-meshheading:12709443-Gene Expression Regulation,
pubmed-meshheading:12709443-I-kappa B Kinase,
pubmed-meshheading:12709443-I-kappa B Proteins,
pubmed-meshheading:12709443-Lymphotoxin beta Receptor,
pubmed-meshheading:12709443-Mice,
pubmed-meshheading:12709443-NF-kappa B,
pubmed-meshheading:12709443-NF-kappa B p50 Subunit,
pubmed-meshheading:12709443-Nuclear Proteins,
pubmed-meshheading:12709443-Protein Binding,
pubmed-meshheading:12709443-Protein-Serine-Threonine Kinases,
pubmed-meshheading:12709443-Proto-Oncogene Proteins,
pubmed-meshheading:12709443-Receptors, Tumor Necrosis Factor,
pubmed-meshheading:12709443-Transcription Factor RelB,
pubmed-meshheading:12709443-Transcription Factors,
pubmed-meshheading:12709443-Tumor Necrosis Factor-alpha
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pubmed:year |
2003
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pubmed:articleTitle |
RelB/p50 dimers are differentially regulated by tumor necrosis factor-alpha and lymphotoxin-beta receptor activation: critical roles for p100.
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pubmed:affiliation |
Laboratoire Oncogenèse, Différenciation et Transduction du Signal, CNRS UPR 9079, Institut André Lwoff, 7 rue Guy Moquet, 94801 Villejuif, France.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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