Academic Journal
Tumor Necrosis Factor α-induced Phosphorylation of RelA/p65 on Ser 529 Is Controlled by Casein Kinase II
| العنوان: | Tumor Necrosis Factor α-induced Phosphorylation of RelA/p65 on Ser 529 Is Controlled by Casein Kinase II |
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| المؤلفون: | Wang, D., Westerheide, S. D., Hanson, J. L., Baldwin A.S., Jr |
| المصدر: | The Journal of Biological Chemistry, 275(42) |
| سنة النشر: | 2000 |
| المجموعة: | Carolina Digital Repository (UNC - University of North Carolina) |
| مصطلحات موضوعية: | Humans, Transfection, Protein-Serine-Threonine Kinases, Transcription Factor RelA, Transcription, Genetic, Casein Kinase II, DNA-Binding Proteins, HeLa Cells, NF-kappa B, Substrate Specificity, Tumor Necrosis Factor-alpha, Serine, Recombinant Proteins, Phosphorylation |
| الوصف: | Nuclear factor kappaB (NF-kappaB)/Rel transcription factors are key regulators of a variety of genes involved in immune and inflammatory responses, growth, differentiation, apoptosis, and development. In unstimulated cells, NF-kappaB/Rel proteins are sequestered in the cytoplasm by IkappaB inhibitor proteins. Many extracellular stimuli, such as tumor necrosis factor alpha (TNFalpha), cause rapid phosphorylation of IkappaB at N-terminal serine residues leading to ubiquitination and degradation of the inhibitor. Subsequently, NF-kappaB proteins translocate to the nucleus and activate gene expression through kappaB response elements. TNFalpha, as well as certain other stimuli, also induces the phosphorylation of the NF-kappaB proteins. Previously, we have shown that TNFalpha induces RelA/p65 phosphorylation at serine 529 and that this inducible phosphorylation increases NF-kappaB transcriptional activity on an exogenously supplied reporter (). In this report, we demonstrate that casein kinase II (CKII) interacts with p65 in vivo and can phosphorylate p65 at serine 529 in vitro. A CKII inhibitor (PD144795) inhibited TNFalpha-induced p65 phosphorylation in vivo. Furthermore, our results indicate that the association between IkappaBalpha and p65 inhibits p65 phosphorylation by CKII and that degradation of IkappaBalpha allows CKII to phosphorylate p65 to increase NF-kappaB transactivation potential. These data may explain the ability of CKII to modulate cell growth and demonstrate a mechanism whereby CKII can function in an inducible manner. |
| نوع الوثيقة: | article in journal/newspaper |
| اللغة: | English |
| Relation: | https://cdr.lib.unc.edu/downloads/bz60d538x?file=thumbnail; https://cdr.lib.unc.edu/downloads/bz60d538x |
| DOI: | 10.17615/gacc-jv13 |
| الاتاحة: | https://doi.org/10.17615/gacc-jv13 https://cdr.lib.unc.edu/downloads/bz60d538x?file=thumbnail https://cdr.lib.unc.edu/downloads/bz60d538x |
| Rights: | http://rightsstatements.org/vocab/InC/1.0/ |
| رقم الانضمام: | edsbas.241E8B87 |
| قاعدة البيانات: | BASE |
| DOI: | 10.17615/gacc-jv13 |
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