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  6. Keywords
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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.
Website Age:
28 years and 1 months (reg. 1997-05-29).

Matching Content Categories {📚}

  • Education
  • Video & Online Content
  • Science

Content Management System {📝}

What CMS is link.springer.com built with?

Custom-built

No common CMS systems were detected on Link.springer.com, and no known web development framework was identified.

Traffic Estimate {📈}

What is the average monthly size of link.springer.com audience?

🌠 Phenomenal Traffic: 5M - 10M visitors per month


Based on our best estimate, this website will receive around 8,170,236 visitors per month in the current month.

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How Does Link.springer.com Make Money? {💸}

We find it hard to spot revenue streams.

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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

Schema {🗺️}

WebPage:
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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.
         datePublished:2015-09-12T00:00:00Z
         dateModified:2015-09-12T00:00:00Z
         pageStart:1085
         pageEnd:1101
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            IκBα
            TLR
            Ubiquitin
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            E3
            Cell Biology
            Biomedicine
            general
            Life Sciences
            Biochemistry
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                        type:PostalAddress
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               affiliation:
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                     address:
                        name:Department of Otolaryngology-Head and Neck Surgery, Hokkaido University Graduate School of Medicine, Sapporo, Japan
                        type:PostalAddress
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                     name:Hokkaido University Graduate School of Medicine
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                        type:PostalAddress
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                     address:
                        name:Department of Biochemistry, Hokkaido University Graduate School of Medicine, Sapporo, Japan
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                     name:Hokkaido University Graduate School of Medicine
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                        name:Department of Otolaryngology-Head and Neck Surgery, Hokkaido University Graduate School of Medicine, Sapporo, Japan
                        type:PostalAddress
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                     address:
                        name:Department of Biochemistry, Hokkaido University Graduate School of Medicine, Sapporo, Japan
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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.
      datePublished:2015-09-12T00:00:00Z
      dateModified:2015-09-12T00:00:00Z
      pageStart:1085
      pageEnd:1101
      sameAs:https://doi.org/10.1007/s00018-015-2040-x
      keywords:
         RelA/p65
         IκBα
         TLR
         Ubiquitin
         Ubiquitin ligase
         E3
         Cell Biology
         Biomedicine
         general
         Life Sciences
         Biochemistry
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                     type:PostalAddress
                  type:Organization
                  name:Hokkaido University Graduate School of Medicine
                  address:
                     name:Department of Otolaryngology-Head and Neck Surgery, Hokkaido University Graduate School of Medicine, Sapporo, Japan
                     type:PostalAddress
                  type:Organization
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            name:Masashi Watanabe
            affiliation:
                  name:Hokkaido University Graduate School of Medicine
                  address:
                     name:Department of Biochemistry, Hokkaido University Graduate School of Medicine, Sapporo, Japan
                     type:PostalAddress
                  type:Organization
            type:Person
            name:Yuji Nakamaru
            affiliation:
                  name:Hokkaido University Graduate School of Medicine
                  address:
                     name:Department of Otolaryngology-Head and Neck Surgery, Hokkaido University Graduate School of Medicine, Sapporo, Japan
                     type:PostalAddress
                  type:Organization
            type:Person
            name:Dai Takagi
            affiliation:
                  name:Hokkaido University Graduate School of Medicine
                  address:
                     name:Department of Otolaryngology-Head and Neck Surgery, Hokkaido University Graduate School of Medicine, Sapporo, Japan
                     type:PostalAddress
                  type:Organization
            type:Person
            name:Hidehisa Takahashi
            affiliation:
                  name:Hokkaido University Graduate School of Medicine
                  address:
                     name:Department of Biochemistry, Hokkaido University Graduate School of Medicine, Sapporo, Japan
                     type:PostalAddress
                  type:Organization
            type:Person
            name:Satoshi Fukuda
            affiliation:
                  name:Hokkaido University Graduate School of Medicine
                  address:
                     name:Department of Otolaryngology-Head and Neck Surgery, Hokkaido University Graduate School of Medicine, Sapporo, Japan
                     type:PostalAddress
                  type:Organization
            type:Person
            name:Shigetsugu Hatakeyama
            affiliation:
                  name:Hokkaido University Graduate School of Medicine
                  address:
                     name:Department of Biochemistry, Hokkaido University Graduate School of Medicine, Sapporo, Japan
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      address:
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         type:PostalAddress
      name:Hokkaido University Graduate School of Medicine
      address:
         name:Department of Biochemistry, Hokkaido University Graduate School of Medicine, Sapporo, Japan
         type:PostalAddress
      name:Hokkaido University Graduate School of Medicine
      address:
         name:Department of Otolaryngology-Head and Neck Surgery, Hokkaido University Graduate School of Medicine, Sapporo, Japan
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      name:Hokkaido University Graduate School of Medicine
      address:
         name:Department of Otolaryngology-Head and Neck Surgery, Hokkaido University Graduate School of Medicine, Sapporo, Japan
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      name:Hokkaido University Graduate School of Medicine
      address:
         name:Department of Biochemistry, Hokkaido University Graduate School of Medicine, Sapporo, Japan
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      name:Hokkaido University Graduate School of Medicine
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         name:Department of Otolaryngology-Head and Neck Surgery, Hokkaido University Graduate School of Medicine, Sapporo, Japan
         type:PostalAddress
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               type:PostalAddress
            type:Organization
      name:Masashi Watanabe
      affiliation:
            name:Hokkaido University Graduate School of Medicine
            address:
               name:Department of Biochemistry, Hokkaido University Graduate School of Medicine, Sapporo, Japan
               type:PostalAddress
            type:Organization
      name:Yuji Nakamaru
      affiliation:
            name:Hokkaido University Graduate School of Medicine
            address:
               name:Department of Otolaryngology-Head and Neck Surgery, Hokkaido University Graduate School of Medicine, Sapporo, Japan
               type:PostalAddress
            type:Organization
      name:Dai Takagi
      affiliation:
            name:Hokkaido University Graduate School of Medicine
            address:
               name:Department of Otolaryngology-Head and Neck Surgery, Hokkaido University Graduate School of Medicine, Sapporo, Japan
               type:PostalAddress
            type:Organization
      name:Hidehisa Takahashi
      affiliation:
            name:Hokkaido University Graduate School of Medicine
            address:
               name:Department of Biochemistry, Hokkaido University Graduate School of Medicine, Sapporo, Japan
               type:PostalAddress
            type:Organization
      name:Satoshi Fukuda
      affiliation:
            name:Hokkaido University Graduate School of Medicine
            address:
               name:Department of Otolaryngology-Head and Neck Surgery, Hokkaido University Graduate School of Medicine, Sapporo, Japan
               type:PostalAddress
            type:Organization
      name:Shigetsugu Hatakeyama
      affiliation:
            name:Hokkaido University Graduate School of Medicine
            address:
               name:Department of Biochemistry, Hokkaido University Graduate School of Medicine, Sapporo, Japan
               type:PostalAddress
            type:Organization
      email:[email protected]
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      name:Department of Biochemistry, Hokkaido University Graduate School of Medicine, Sapporo, Japan
      name:Department of Otolaryngology-Head and Neck Surgery, Hokkaido University Graduate School of Medicine, Sapporo, Japan
      name:Department of Biochemistry, Hokkaido University Graduate School of Medicine, Sapporo, Japan
      name:Department of Otolaryngology-Head and Neck Surgery, Hokkaido University Graduate School of Medicine, Sapporo, Japan
      name:Department of Otolaryngology-Head and Neck Surgery, Hokkaido University Graduate School of Medicine, Sapporo, Japan
      name:Department of Biochemistry, Hokkaido University Graduate School of Medicine, Sapporo, Japan
      name:Department of Otolaryngology-Head and Neck Surgery, Hokkaido University Graduate School of Medicine, Sapporo, Japan
      name:Department of Biochemistry, Hokkaido University Graduate School of Medicine, Sapporo, Japan
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