β-Transducin Repeat-containing Protein 1 (β-TrCP1)-mediated Silencing Mediator of Retinoic Acid and Thyroid Hormone Receptor (SMRT) Protein Degradation Promotes Tumor Necrosis Factor α (TNFα)-induced Inflammatory Gene Expression

Hsu, Kuo Sheng; Kao, Hung Ying

doi:10.1074/jbc.m113.473124

Cited by 7 publications

(7 citation statements)

References 49 publications

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“…The relative mRNA expression was calculated by the 2 Ϫ(⌬⌬Ct) method. The PCR primers used in this study and their sequences were previously described (24).…”

Section: Generation Of Stable Knockdownmentioning

confidence: 99%

“…Immunoprecipitation was performed using anti-ACTN4 and anti-p65 antibodies. The PCR primers used in this study and their sequences were previously described (24).…”

Section: Generation Of Stable Knockdownmentioning

confidence: 99%

“…ChIP Assay-ChIP assays were carried out as described with modifications (24). Chromatin was sheared by sonication, and the extracts were precleared by protein-A-coupled beads (Repligen).…”

Section: Generation Of Stable Knockdownmentioning

confidence: 99%

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α-Actinin 4 Potentiates Nuclear Factor κ-Light-chain-enhancer of Activated B-cell (NF-κB) Activity in Podocytes Independent of Its Cytoplasmic Actin Binding Function

Zhao¹,

Hsu²,

Lim³

et al. 2015

Journal of Biological Chemistry

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Background: ACTN4 is an actin-binding protein and is associated with kidney diseases. Results: Nuclear ACTN4 interacts with NF-B and is recruited to NF-B-targeted promoters to potentiate its transcription activity. Conclusion: ACTN4 coactivates NF-B activity independently of its cytoplasmic activity in cultured human podocytes. Significance: Nuclear ACTN4 may play an important role in glomerular function.

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“…The relative mRNA expression was calculated by the 2 Ϫ(⌬⌬Ct) method. The PCR primers used in this study and their sequences were previously described (24).…”

Section: Generation Of Stable Knockdownmentioning

confidence: 99%

“…Immunoprecipitation was performed using anti-ACTN4 and anti-p65 antibodies. The PCR primers used in this study and their sequences were previously described (24).…”

Section: Generation Of Stable Knockdownmentioning

confidence: 99%

See 1 more Smart Citation

α-Actinin 4 Potentiates Nuclear Factor κ-Light-chain-enhancer of Activated B-cell (NF-κB) Activity in Podocytes Independent of Its Cytoplasmic Actin Binding Function

Zhao¹,

Hsu²,

Lim³

et al. 2015

Journal of Biological Chemistry

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“…Similarly, in IL-17-mediated inflammation, β-TrCP degrades Act1, an adaptor protein associated with IL-17 receptor desensitization [ 40 ]. During TNF-α induced inflammation, β-TrCP1 promotes such activity via degrading an anti-inflammatory protein, silencing mediator of retinoic acid and thyroid hormone receptor (SMRT) [ 41 ]. Recently, β-TrCP was also implicated in inflammatory cytokine production via polyubiquitination and degradation of AUF1 [ 42 ], another ARE-binding cytokine mRNA decay factor, similar to TTP.…”

Section: Discussionmentioning

confidence: 99%

Involvement of p38-βTrCP-Tristetraprolin-TNFα axis in radiation pneumonitis

et al. 2017

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Early release of tumor necrosis factor-alpha (TNF-α) during radiotherapy of thoracic cancers plays an important role in radiation pneumonitis, whose inhibition may provide lung radioprotection. We previously reported radiation inactivates Tristetraprolin (TTP), a negative regulator of TNF-α synthesis, which correlated with increased TNF-α release. However, the molecular events involved in radiation-induced TTP inactivation remain unclear. To determine if eliminating Ttp in mice resulted in a phenotypic response to radiation, Ttp-null mice lungs were exposed to a single dose of 15 Gy, and TNF-α release and lung inflammation were analyzed at different time points post-irradiation. Ttp−/− mice with elevated (9.5±0.6 fold) basal TNF-α showed further increase (12.2±0.9 fold, p<0.02) in TNF-α release and acute lung inflammation within a week post-irradiation. Further studies using mouse lung macrophage (MH-S), human lung fibroblast (MRC-5), and exogenous human TTP overexpressing U2OS and HEK293 cells upon irradiation (a single dose of 4 Gy) promoted p38-mediated TTP phosphorylation at the serine 186 position, which primed it to be recognized by an ubiquitin ligase (E3), beta transducing repeat containing protein (β-TrCP), to promote polyubiquitination-mediated proteasomal degradation. Consequently, a serine 186 to alanine (SA) mutant of TTP was resistant to radiation-induced degradation. Similarly, either a p38 kinase inhibitor (SB203580), or siRNA-mediated β-TrCP knockdown, or overexpression of dominant negative Cullin1 mutants protected TTP from radiation-induced degradation. Consequently, SB203580 pretreatment blocked radiation-induced TNF-α release and radioprotected macrophages. Together, these data establish the involvement of the p38-βTrCP-TTP-TNFα signaling axis in radiation-induced lung inflammation and identified p38 inhibition as a possible lung radioprotection strategy.

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“…ChIP assays were modified from our published protocol. 79 Briefly, HUVECs were treated with 1% formaldehyde for 10 min at room temperature and the crosslinking reaction was stopped by adding glycine to a final concentration of 0.125 M and incubated for 5 min. Cells were harvested and chromatin was sheared by sonication to an average length of 300–700 bp.…”

Section: Methodsmentioning

confidence: 99%

Translational control of PML contributes to TNFα-induced apoptosis of MCF7 breast cancer cells and decreased angiogenesis in HUVECs

et al. 2015

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The tumor suppressor protein promyelocytic leukemia (PML) is a key regulator of inflammatory responses and tumorigenesis and functions through the assembly of subnuclear structures known as PML nuclear bodies (NBs). The inflammation-related cytokine tumor necrosis factor-α (TNFα) is known to induce PML protein accumulation and PML NB formation that mediate TNFα-induced cell death in cancer cells and inhibition of migration and capillary tube formation in endothelial cells (ECs). In this study, we uncover a novel mechanism of PML gene regulation in which the p38 MAPK and its downstream kinase MAP kinase-activated protein kinase 1 (MNK1) mediate TNFα-induced PML protein accumulation and PML NB formation. The mechanism includes the presence of an internal ribosome entry site (IRES) found within the well-conserved 100 nucleotides upstream of the PML initiation codon. The activity of the PML IRES is induced by TNFα in a manner that involves MNK1 activation. It is proposed that the p38–MNK1–PML network regulates TNFα-induced apoptosis in breast cancer cells and TNFα-mediated inhibition of migration and capillary tube formation in ECs.

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β-Transducin Repeat-containing Protein 1 (β-TrCP1)-mediated Silencing Mediator of Retinoic Acid and Thyroid Hormone Receptor (SMRT) Protein Degradation Promotes Tumor Necrosis Factor α (TNFα)-induced Inflammatory Gene Expression

Cited by 7 publications

References 49 publications

α-Actinin 4 Potentiates Nuclear Factor κ-Light-chain-enhancer of Activated B-cell (NF-κB) Activity in Podocytes Independent of Its Cytoplasmic Actin Binding Function

α-Actinin 4 Potentiates Nuclear Factor κ-Light-chain-enhancer of Activated B-cell (NF-κB) Activity in Podocytes Independent of Its Cytoplasmic Actin Binding Function

Involvement of p38-βTrCP-Tristetraprolin-TNFα axis in radiation pneumonitis

Translational control of PML contributes to TNFα-induced apoptosis of MCF7 breast cancer cells and decreased angiogenesis in HUVECs

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