Tumor Necrosis Factor Alpha Induction of NF-κB Requires the Novel Coactivator SIMPL

Kwon, Hyung‐Joo; Breese, Erin H.; Vig-Varga, E.; Luo, Yong; Lee, Younghee; Goebl, Mark G.; Harrington, Maureen A.

doi:10.1128/mcb.24.21.9317-9326.2004

Cited by 31 publications

(53 citation statements)

References 31 publications

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“…The cells were used for transfection with FuGene 6 Transfection Reagent (Roche) in accordance with the manufacturer's instructions. We confirmed the equivalent transfection efficiency by cotransfecting the promoterless Renilla luciferase vector pRL-null (Promega) [39]. After placing the transfected cells in a complete medium for 24 h, we added IFN-c (200 U/ mL), CpG-DNA (3 lM) or LPS (100 ng/mL) for the indicated periods.…”

Section: Transfection and Luciferase Assaymentioning

confidence: 90%

Direct role of NF‐κB activation in Toll‐like receptor‐triggered HLA‐DRA expression

Lee

Kim

et al. 2006

Eur J Immunol

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Microbial components, such as DNA containing immunostimulatory CpG motifs (CpG-DNA) and lipopolysaccharides (LPS), elicit the cell surface expression of MHC class II (MHC-II) through Toll-like receptor (TLR)/IL-1R. Here, we show that CpG-DNA and LPS induce expression of the HLA-DRA in the human B cell line, RPMI 8226. Ectopic expression of the dominant negative mutant of CIITA and RNA interference targeting the CIITA gene indicate that CIITA activation is not enough for the maximal MHC-II expression induced by CpG-DNA and LPS. Additionally, nuclear factor (NF)-jB activation is required for the CpG-DNA-activated and LPS-activated HLA-DRA expression, whereas IFN-c-induced MHC-II expression depends on CIITA rather than on NF-jB. Comprehensive mutant analyses, electrophoretic mobility shift assays and chromatin immunoprecipitation assays, reveal that the functional interaction of NF-jB with the promoter element is necessary for the TLR-mediated HLA-DRA induction by CpG-DNA and LPS. This novel mechanism provides the regulation of MHC-II gene expression with complexity and functional diversity.

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Section: Transfection and Luciferase Assaymentioning

confidence: 90%

Direct role of NF‐κB activation in Toll‐like receptor‐triggered HLA‐DRA expression

Lee

Kim

et al. 2006

Eur J Immunol

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“…The signaling molecule that interacts with pelle-like kinase (SIMPL) binds IRAK1 and is required for TNF␣-mediated NF-B activation in 293 cells (53). In response to TNF␣, SIMPL localizes into the nucleus, binds to p65, and induces p65-mediated transcription (53).…”

Section: Discussionmentioning

confidence: 99%

IL-1 receptor-associated kinase 1 is critical for latent membrane protein 1-induced p65/RelA serine 536 phosphorylation and NF-κB activation

Song

Jen

Soni

et al. 2006

Proc. Natl. Acad. Sci. U.S.A.

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Epstein–Barr virus latent infection integral membrane protein 1 (LMP1) mimics a constitutively active TNF receptor (TNFR). LMP1 has two C-terminal cytosolic domains, transformation effector sites (TES)1 and -2, that engage TNFR-associated factors (TRAFs) and the TNFR-associated death domain protein, respectively, and activate NF-κB. NF-κB activation is critical for Epstein–Barr virus-infected lymphoblast survival. TES1- and TES2-mediated NF-κB activations are IL-1 receptor-associated kinase 1 (IRAK1)-dependent. Because IRAK1 is upstream of TRAF6 in IL-1 activation of NF-κB, the potential role of IRAK1 in LMP1-mediated NF-κB activation through TRAF6 and inhibitor of κB (IκB) kinase (IKK) was initially investigated. Surprisingly, LMP1 expression activated TRAF6 ubiquitination, IKKβ induction of IκBα phosphorylation, and p65 nuclear translocation in both WT and IRAK1-deficient I1A 293 cells. LMP1 also induced IKKα-mediated p100 processing and p52 nuclear localization in WT and IRAK1-deficient I1A 293 cells. Further, LMP1 TES1 and TES2 induced p65, p50, and p52 NF-κB DNA binding in WT and IRAK1-deficient I1A 293 cells. However, LMP1 induced p65/RelA S536 phosphorylation only in WT 293 cells or in IRAK1 kinase point mutant reconstituted I1A 293 cells but not in IRAK1-deficient I1A 293 cells. IRAK1 was also required for LMP1 activation of p38, one of the kinases that can mediate p65/RelA S536 phosphorylation and activate NF-κB-dependent transcription. Thus, the critical IRAK1 role in LMP1-induced NF-κB activation is in mediating p65/RelA S536 phosphorylation through an effect on p38 or other p65 S536 kinases.

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“…In addition, it is becoming clear that not all activated NF-kB is the same. Thus, IL-1b and TNF-a can both activate NF-kB, but the resultant co-activator complex is distinct since TNF-a-stimulated NF-kB can recruit the novel co-activator SIMPL to the NF-kB-coactivator complex, whereas this does not occur with IL-1b [127].…”

Section: S-glutathiolation Modulation Of Transcription Factorsmentioning

confidence: 99%

Oxidative stress and redox regulation of lung inflammation in COPD

Rahman

Adcock²

2006

Eur Respir J

783

599

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Reactive oxygen species, either directly or via the formation of lipid peroxidation products, may play a role in enhancing inflammation through the activation of stress kinases (cJun activated kinase, extracellular signal-regulated kinase, p38) and redox-sensitive transcription factors, such as nuclear factor (NF)-kB and activator protein-1. This results in increased expression of a battery of distinct pro-inflammatory mediators. Oxidative stress activates NF-kBmediated transcription of pro-inflammatory mediators either through activation of its activating inhibitor of kB-a kinase or the enhanced recruitment and activation of transcriptional coactivators. Enhanced NF-kB-co-activator complex formation results in targeted increases in histone modifications, such as acetylation leading to inflammatory gene expression.Emerging evidence suggests the glutathione redox couple may entail dynamic regulation of protein function by reversible disulphide bond formation on kinases, phosphatases and transcription factors. Oxidative stress also inhibits histone deacetylase activity and in doing so further enhances inflammatory gene expression and may attenuate glucocorticoid sensitivity.The antioxidant/anti-inflammatory effects of thiol molecules (glutathione, N-acetyl-L-cysteine and N-acystelyn, erdosteine), dietary polyphenols (curcumin-diferuloylmethane, cathechins/ quercetin and reserveratol), specific spin traps, such as a-phenyl-N-tert-butyl nitrone, a catalytic antioxidant (extracellular superoxide dismutase (SOD) mimetic, SOD mimetic M40419 and SOD, and catalase manganic salen compound, eukarion-8), porphyrins (AEOL 10150 and AEOL 10113) and theophylline have all been shown to play a role in either controlling NF-kB activation or affecting histone modifications with subsequent effects on inflammatory gene expression in lung epithelial cells.Thus, oxidative stress regulates both key signal transduction pathways and histone modifications involved in lung inflammation. Various approaches to enhance lung antioxidant capacity and clinical trials of antioxidant compounds in chronic obstructive pulmonary disease are also discussed.

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Tumor Necrosis Factor Alpha Induction of NF-κB Requires the Novel Coactivator SIMPL

Cited by 31 publications

References 31 publications

Direct role of NF‐κB activation in Toll‐like receptor‐triggered HLA‐DRA expression

Direct role of NF‐κB activation in Toll‐like receptor‐triggered HLA‐DRA expression

IL-1 receptor-associated kinase 1 is critical for latent membrane protein 1-induced p65/RelA serine 536 phosphorylation and NF-κB activation

Oxidative stress and redox regulation of lung inflammation in COPD

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