دورية أكاديمية
RelB/p50 dimers are differentially regulated by tumor necrosis factor-alpha and lymphotoxin-beta receptor activation: critical roles for p100.
| العنوان: | RelB/p50 dimers are differentially regulated by tumor necrosis factor-alpha and lymphotoxin-beta receptor activation: critical roles for p100. |
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| المؤلفون: | Derudder, Emmanuel, Dejardin, Emmanuel, Pritchard, Linda L., Green, Douglas R., Korner, Marie, Baud, Veronique |
| المصدر: | Journal of Biological Chemistry, 278 (26), 23278-84 (2003) |
| بيانات النشر: | American Society for Biochemistry and Molecular Biology |
| سنة النشر: | 2003 |
| المجموعة: | University of Liège: ORBi (Open Repository and Bibliography) |
| مصطلحات موضوعية: | Active Transport, Cell Nucleus, Animals, DNA/metabolism, Dimerization, Fibroblasts/metabolism, Gene Expression Regulation, I-kappa B Kinase, I-kappa B Proteins/metabolism, Lymphotoxin beta Receptor, Mice, NF-kappa B/metabolism, NF-kappa B p50 Subunit, Nuclear Proteins/metabolism/physiology, Protein Binding, Protein-Serine-Threonine Kinases/metabolism, Proto-Oncogene Proteins/antagonists & inhibitors/metabolism, Receptors, Tumor Necrosis Factor/metabolism/physiology, Transcription Factor RelB, Transcription Factors/antagonists & inhibitors/metabolism, Tumor Necrosis Factor-alpha/physiology, Life sciences, Biochemistry, biophysics & molecular biology, Sciences du vivant, Biochimie, biophysique & biologie moléculaire |
| الوصف: | peer reviewed ; 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. |
| نوع الوثيقة: | article in journal/newspaper |
| اللغة: | English |
| تدمد: | 0021-9258 1083-351X |
| العلاقة: | urn:issn:0021-9258; urn:issn:1083-351X; https://orbi.uliege.be/handle/2268/178937Test; info:hdl:2268/178937; scopus-id:2-s2.0-0037931474; info:pmid:12709443 |
| DOI: | 10.1074/jbc.M300106200 |
| الإتاحة: | https://doi.org/10.1074/jbc.M300106200Test https://orbi.uliege.be/handle/2268/178937Test |
| حقوق: | restricted access ; http://purl.org/coar/access_right/c_16ecTest ; info:eu-repo/semantics/restrictedAccess |
| رقم الانضمام: | edsbas.A6DD0C32 |
| قاعدة البيانات: | BASE |
Full Text Finder | تدمد: | 00219258 1083351X |
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| DOI: | 10.1074/jbc.M300106200 |