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• W1566535612 abstract "Post-translational modification and degradation of proteins by the ubiquitin-proteasome system are key regulatory mechanisms in cellular responses to various stimuli. The NF-kappaB signaling pathway is controlled by the ubiquitin-mediated proteolysis. RelA/p65, which is a main subunit of NF-kappaB, is ubiquitinated for degradation by SOCS-1, but the functional mechanism of its ubiquitination remains poorly understood. In this study we show that phosphorylation of RelA/p65 at Ser276 prevents its degradation by ubiquitin-mediated proteolysis. In contrast, impairment of Ser276 phosphorylation affects constitutive degradation of RelA/p65. Importantly, we identify Pim-1 as a further kinase responsible for the phosphorylation of RelA/p65 at Ser276. Depletion of Pim-1 hinders not only Ser276 phosphorylation but also transactivation of RelA/p65 target genes. We also show that Pim-1 contributes to recruitment of RelA/p65 to kappaB-elements to activate NF-kappaB signalling after TNF-alpha stimulation. In concert with these results, the knockdown of Pim-1 impairs IL-6 production and augments apoptosis by interfering RelA/p65 activation. These findings provide a model in which Pim-1 phosphorylation of RelA/p65 at Ser276 allows defense against ubiquitin-mediated degradation and whereby exerts activation of NF-kappaB signalling." @default.
• W1566535612 created "2016-06-24" @default.
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• W1566535612 date "2009-11-13" @default.
• W1566535612 modified "2023-10-16" @default.
• W1566535612 title "Pim-1 controls NF-κB signalling by stabilizing RelA/p65" @default.
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• W1566535612 doi "https://doi.org/10.1038/cdd.2009.174" @default.
• W1566535612 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/19911008" @default.
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