We are analyzing https://link.springer.com/article/10.1007/s00018-015-2040-x.

Title:
TRIM39 negatively regulates the NFκB-mediated signaling pathway through stabilization of Cactin | Cellular and Molecular Life Sciences
Description:
NFκB is one of the central regulators of cell survival, immunity, inflammation, carcinogenesis and organogenesis. The activation of NFκB is strictly regulated by several posttranslational modifications including phosphorylation, neddylation and ubiquitination. Several types of ubiquitination play important roles in multi-step regulations of the NFκB pathway. Some of the tripartite motif-containing (TRIM) proteins functioning as E3 ubiquitin ligases are known to regulate various biological processes such as inflammatory signaling pathways. One of the TRIM family proteins, TRIM39, for which the gene has single nucleotide polymorphisms, has been identified as one of the genetic factors in Behcet’s disease. However, the role of TRIM39 in inflammatory signaling had not been fully elucidated. In this study, to elucidate the function of TRIM39 in inflammatory signaling, we performed yeast two-hybrid screening using TRIM39 as a bait and identified Cactin, which has been reported to inhibit NFκB- and TLR-mediated transcriptions. We show that TRIM39 stabilizes Cactin protein and that Cactin is upregulated after TNFα stimulation. TRIM39 knockdown also causes activation of the NFκB signal. These findings suggest that TRIM39 negatively regulates the NFκB signal in collaboration with Cactin induced by inflammatory stimulants such as TNFα.
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Keywords {🔍}

pubmed, article, google, scholar, cas, trim, central, protein, hatakeyama, signaling, cell, ubiquitin, nfkappab, cactin, proteins, supplementary, material, pdf, regulates, nfκb, suzuki, family, gene, biol, res, polymorphism, privacy, cookies, function, content, negatively, pathway, watanabe, inflammatory, role, access, ligase, sci, usa, biochem, immunol, mol, publish, search, september, takahashi, activation, ubiquitination, ligases, pathways,

Topics {✒️}

e6-ap ubiquitin-protein ligase month download article/chapter ubiquitin-modifying enzyme a20 slimb f-box protein e3-ligase trim family ubiquitin-protein ligase system e3 ubiquitin ligases negatively regulates nf-kappab central regulators dai takagi & satoshi fukuda ubiquitin-protein ligases il-6 gene transcription nf-κb pathway—determinant genetic factors ubiquitin ligase domains irf-3/7-mediated signal pathways moap-1-binding protein inhibits nf-kappab ret finger protein tlr-mediated transcriptions nf-kappab pathway nf-kappab signaling nf-kappab activity cacn-1/cactin interacts genetically nfκb-mediated signaling pathway full article pdf privacy choices/manage cookies single nucleotide polymorphisms linear ubiquitin chains trim39 negatively regulates nf-kappab activation protein ubiquitination involving ubiquitin-dependent degradation il-6-induced regulation inflammatory signaling pathways article cellular ikbl promoter polymorphism tripartite motif trim family proteins retinoblastoma protein function nf-kappab european economic area multi-step regulations innate antiviral response related subjects m1 leukemia cells lopes-virella mf u937 mononuclear cells early zebrafish development mig-2 gtpase signaling

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         description:NFκB is one of the central regulators of cell survival, immunity, inflammation, carcinogenesis and organogenesis. The activation of NFκB is strictly regulated by several posttranslational modifications including phosphorylation, neddylation and ubiquitination. Several types of ubiquitination play important roles in multi-step regulations of the NFκB pathway. Some of the tripartite motif-containing (TRIM) proteins functioning as E3 ubiquitin ligases are known to regulate various biological processes such as inflammatory signaling pathways. One of the TRIM family proteins, TRIM39, for which the gene has single nucleotide polymorphisms, has been identified as one of the genetic factors in Behcet’s disease. However, the role of TRIM39 in inflammatory signaling had not been fully elucidated. In this study, to elucidate the function of TRIM39 in inflammatory signaling, we performed yeast two-hybrid screening using TRIM39 as a bait and identified Cactin, which has been reported to inhibit NFκB- and TLR-mediated transcriptions. We show that TRIM39 stabilizes Cactin protein and that Cactin is upregulated after TNFα stimulation. TRIM39 knockdown also causes activation of the NFκB signal. These findings suggest that TRIM39 negatively regulates the NFκB signal in collaboration with Cactin induced by inflammatory stimulants such as TNFα.
         datePublished:2015-09-12T00:00:00Z
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            Biochemistry
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      headline:TRIM39 negatively regulates the NFκB-mediated signaling pathway through stabilization of Cactin
      description:NFκB is one of the central regulators of cell survival, immunity, inflammation, carcinogenesis and organogenesis. The activation of NFκB is strictly regulated by several posttranslational modifications including phosphorylation, neddylation and ubiquitination. Several types of ubiquitination play important roles in multi-step regulations of the NFκB pathway. Some of the tripartite motif-containing (TRIM) proteins functioning as E3 ubiquitin ligases are known to regulate various biological processes such as inflammatory signaling pathways. One of the TRIM family proteins, TRIM39, for which the gene has single nucleotide polymorphisms, has been identified as one of the genetic factors in Behcet’s disease. However, the role of TRIM39 in inflammatory signaling had not been fully elucidated. In this study, to elucidate the function of TRIM39 in inflammatory signaling, we performed yeast two-hybrid screening using TRIM39 as a bait and identified Cactin, which has been reported to inhibit NFκB- and TLR-mediated transcriptions. We show that TRIM39 stabilizes Cactin protein and that Cactin is upregulated after TNFα stimulation. TRIM39 knockdown also causes activation of the NFκB signal. These findings suggest that TRIM39 negatively regulates the NFκB signal in collaboration with Cactin induced by inflammatory stimulants such as TNFα.
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         TLR
         Ubiquitin
         Ubiquitin ligase
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         general
         Life Sciences
         Biochemistry
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