SINTBAD, a novel component of innate antiviral immunity, shares a TBK1-binding domain with NAP1 and TANK
The expression of antiviral genes during infection is controlled by inducible transcription factors such as IRF3 (interferon regulatory factor). Activation of IRF3 requires its phosphorylation by TBK1 (TANK‐binding kinase) or IKKi (inhibitor of nuclear factor κB kinase, inducible). We have identifie...
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| Veröffentlicht in: | The EMBO journal 2007-07, Vol.26 (13), p.3180-3190 |
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| description | The expression of antiviral genes during infection is controlled by inducible transcription factors such as IRF3 (interferon regulatory factor). Activation of IRF3 requires its phosphorylation by TBK1 (TANK‐binding kinase) or IKKi (inhibitor of nuclear factor κB kinase, inducible). We have identified a new and essential component of this pathway, the adaptor protein SINTBAD (similar to NAP1 TBK1 adaptor). SINTBAD constitutively binds TBK1 and IKKi but not related kinases. Upon infection with Sendai virus, SINTBAD is essential for the efficient induction of IRF‐dependent transcription, as are two further TBK1 adaptors, TANK and NAP1. We identified a conserved TBK1/IKKi‐binding domain (TBD) in the three adaptors, predicted to form an α‐helix with residues essential for kinase binding clustering on one side. Isolated TBDs compete with adaptor binding to TBK1 and prevent poly(I:C)‐induced IRF‐dependent transcription. Our results suggest that efficient signal transduction upon viral infection requires SINTBAD, TANK and NAP1 because they link TBK1 and IKKi to virus‐activated signalling cascades. |
| doi_str_mv | 10.1038/sj.emboj.7601743 |
| format | Article |
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Activation of IRF3 requires its phosphorylation by TBK1 (TANK‐binding kinase) or IKKi (inhibitor of nuclear factor κB kinase, inducible). We have identified a new and essential component of this pathway, the adaptor protein SINTBAD (similar to NAP1 TBK1 adaptor). SINTBAD constitutively binds TBK1 and IKKi but not related kinases. Upon infection with Sendai virus, SINTBAD is essential for the efficient induction of IRF‐dependent transcription, as are two further TBK1 adaptors, TANK and NAP1. We identified a conserved TBK1/IKKi‐binding domain (TBD) in the three adaptors, predicted to form an α‐helix with residues essential for kinase binding clustering on one side. Isolated TBDs compete with adaptor binding to TBK1 and prevent poly(I:C)‐induced IRF‐dependent transcription. 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Activation of IRF3 requires its phosphorylation by TBK1 (TANK‐binding kinase) or IKKi (inhibitor of nuclear factor κB kinase, inducible). We have identified a new and essential component of this pathway, the adaptor protein SINTBAD (similar to NAP1 TBK1 adaptor). SINTBAD constitutively binds TBK1 and IKKi but not related kinases. Upon infection with Sendai virus, SINTBAD is essential for the efficient induction of IRF‐dependent transcription, as are two further TBK1 adaptors, TANK and NAP1. We identified a conserved TBK1/IKKi‐binding domain (TBD) in the three adaptors, predicted to form an α‐helix with residues essential for kinase binding clustering on one side. Isolated TBDs compete with adaptor binding to TBK1 and prevent poly(I:C)‐induced IRF‐dependent transcription. Our results suggest that efficient signal transduction upon viral infection requires SINTBAD, TANK and NAP1 because they link TBK1 and IKKi to virus‐activated signalling cascades.</description><subject>Adaptor Proteins, Signal Transducing - chemistry</subject><subject>Adaptor Proteins, Signal Transducing - genetics</subject><subject>Adaptor Proteins, Signal Transducing - metabolism</subject><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>antiviral response</subject><subject>Binding Sites</subject><subject>Cell Line</subject><subject>Conserved Sequence</subject><subject>EMBO19</subject><subject>EMBO37</subject><subject>Enzyme Activation</subject><subject>Gene expression</subject><subject>Humans</subject><subject>I-kappa B Kinase - metabolism</subject><subject>Immunity, Innate - drug effects</subject><subject>Immunity, Innate - immunology</subject><subject>Infections</subject><subject>innate immunity</subject><subject>Interferon Regulatory Factors - metabolism</subject><subject>Kinases</subject><subject>Membrane Proteins - chemistry</subject><subject>Membrane Proteins - metabolism</subject><subject>Mice</subject><subject>Molecular biology</subject><subject>Molecular Sequence Data</subject><subject>Poly I-C - pharmacology</subject><subject>Protein Binding</subject><subject>Protein Serine-Threonine Kinases - metabolism</subject><subject>Proteins - chemistry</subject><subject>Proteins - metabolism</subject><subject>RNA Interference</subject><subject>Sendai virus</subject><subject>Sendai virus - immunology</subject><subject>Sequence Alignment</subject><subject>Signal transduction</subject><subject>tRNA Methyltransferases</subject><subject>Viruses</subject><issn>0261-4189</issn><issn>1460-2075</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2007</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>8G5</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><sourceid>GUQSH</sourceid><sourceid>M2O</sourceid><recordid>eNqFUs9v0zAUjhCIlcGdC8jiwGkpdvwruSC12xhjo1BRiaPlJK-tS2IXO-nof09KqnYgoZ18-H68773PUfSS4CHBNH0XVkOoc7caSoGJZPRRNCBM4DjBkj-OBjgRJGYkzU6iZyGsMMY8leRpdEIkF6mU6SBafruezMajizOkkXUbqFDh6rWzYBvk5shYqxtA2jZmY7yukKnr1ppme4bCUnsInWw2viFxbmxp7AKVrtbGojvTLNFk9JV00hLNRpOb59GTua4CvNi_p9Hsw-Xs_GN8--Xq-nx0GxcCMxozNscMJKdCF7kAQXPJoKSMcShBEKETnICkCU0ILxjBgkPBMjFPcsJSCvQ0et_brtu8hrLo9uhiq7U3tfZb5bRRfyPWLNXCbRTJCMMZ6Qze7g28-9lCaFRtQgFVpS24NiiJJcFZxh8kJhhLQciO-OYf4sq13nZH6IbyhMuU7Ui4JxXeheBhfohMsNp1rcJK_ela7bvuJK_vr3oU7MvtCFlPuDMVbB80VJefx5-O5qTXhk5mF-Dvhf5_oFe9pvszrYfDwCMe97gJDfw6wNr_UEJSydX3yZW6mE5lmgqhpvQ3uArfyw</recordid><startdate>20070711</startdate><enddate>20070711</enddate><creator>Ryzhakov, Grigory</creator><creator>Randow, Felix</creator><general>John Wiley & Sons, Ltd</general><general>Nature Publishing Group UK</general><general>Blackwell Publishing Ltd</general><general>Nature Publishing Group</general><scope>BSCLL</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7QG</scope><scope>7QL</scope><scope>7QP</scope><scope>7T5</scope><scope>7TK</scope><scope>7TM</scope><scope>7TO</scope><scope>7U9</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>8AO</scope><scope>8C1</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>8G5</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>BKSAR</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>GUQSH</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2O</scope><scope>M7N</scope><scope>M7P</scope><scope>MBDVC</scope><scope>P64</scope><scope>PCBAR</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>Q9U</scope><scope>RC3</scope><scope>7QO</scope><scope>7T7</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20070711</creationdate><title>SINTBAD, a novel component of innate antiviral immunity, shares a TBK1-binding domain with NAP1 and TANK</title><author>Ryzhakov, Grigory ; Randow, Felix</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c6043-44f04e7536acb6e63b74ed3445ede616a202e7323215c41065ec496f2b1483e3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2007</creationdate><topic>Adaptor Proteins, Signal Transducing - chemistry</topic><topic>Adaptor Proteins, Signal Transducing - genetics</topic><topic>Adaptor Proteins, Signal Transducing - metabolism</topic><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>antiviral response</topic><topic>Binding Sites</topic><topic>Cell Line</topic><topic>Conserved Sequence</topic><topic>EMBO19</topic><topic>EMBO37</topic><topic>Enzyme Activation</topic><topic>Gene expression</topic><topic>Humans</topic><topic>I-kappa B Kinase - metabolism</topic><topic>Immunity, Innate - drug effects</topic><topic>Immunity, Innate - immunology</topic><topic>Infections</topic><topic>innate immunity</topic><topic>Interferon Regulatory Factors - metabolism</topic><topic>Kinases</topic><topic>Membrane Proteins - chemistry</topic><topic>Membrane Proteins - metabolism</topic><topic>Mice</topic><topic>Molecular biology</topic><topic>Molecular Sequence Data</topic><topic>Poly I-C - pharmacology</topic><topic>Protein Binding</topic><topic>Protein Serine-Threonine Kinases - metabolism</topic><topic>Proteins - chemistry</topic><topic>Proteins - metabolism</topic><topic>RNA Interference</topic><topic>Sendai virus</topic><topic>Sendai virus - immunology</topic><topic>Sequence Alignment</topic><topic>Signal transduction</topic><topic>tRNA Methyltransferases</topic><topic>Viruses</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Ryzhakov, Grigory</creatorcontrib><creatorcontrib>Randow, Felix</creatorcontrib><collection>Istex</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Animal Behavior Abstracts</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Immunology Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Oncogenes and Growth Factors Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>Public Health Database</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>Research Library (Alumni Edition)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>Earth, Atmospheric & Aquatic Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>Research Library Prep</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Research Library</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biological Science Database</collection><collection>Research Library (Corporate)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Earth, Atmospheric & Aquatic Science Database</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central Basic</collection><collection>Genetics Abstracts</collection><collection>Biotechnology Research Abstracts</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>The EMBO journal</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext_linktorsrc</fulltext></delivery><addata><au>Ryzhakov, Grigory</au><au>Randow, Felix</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>SINTBAD, a novel component of innate antiviral immunity, shares a TBK1-binding domain with NAP1 and TANK</atitle><jtitle>The EMBO journal</jtitle><stitle>EMBO J</stitle><addtitle>EMBO J</addtitle><date>2007-07-11</date><risdate>2007</risdate><volume>26</volume><issue>13</issue><spage>3180</spage><epage>3190</epage><pages>3180-3190</pages><issn>0261-4189</issn><eissn>1460-2075</eissn><coden>EMJODG</coden><abstract>The expression of antiviral genes during infection is controlled by inducible transcription factors such as IRF3 (interferon regulatory factor). Activation of IRF3 requires its phosphorylation by TBK1 (TANK‐binding kinase) or IKKi (inhibitor of nuclear factor κB kinase, inducible). We have identified a new and essential component of this pathway, the adaptor protein SINTBAD (similar to NAP1 TBK1 adaptor). SINTBAD constitutively binds TBK1 and IKKi but not related kinases. Upon infection with Sendai virus, SINTBAD is essential for the efficient induction of IRF‐dependent transcription, as are two further TBK1 adaptors, TANK and NAP1. We identified a conserved TBK1/IKKi‐binding domain (TBD) in the three adaptors, predicted to form an α‐helix with residues essential for kinase binding clustering on one side. Isolated TBDs compete with adaptor binding to TBK1 and prevent poly(I:C)‐induced IRF‐dependent transcription. Our results suggest that efficient signal transduction upon viral infection requires SINTBAD, TANK and NAP1 because they link TBK1 and IKKi to virus‐activated signalling cascades.</abstract><cop>Chichester, UK</cop><pub>John Wiley & Sons, Ltd</pub><pmid>17568778</pmid><doi>10.1038/sj.emboj.7601743</doi><tpages>11</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Adaptor Proteins, Signal Transducing - chemistry Adaptor Proteins, Signal Transducing - genetics Adaptor Proteins, Signal Transducing - metabolism Amino Acid Sequence Animals antiviral response Binding Sites Cell Line Conserved Sequence EMBO19 EMBO37 Enzyme Activation Gene expression Humans I-kappa B Kinase - metabolism Immunity, Innate - drug effects Immunity, Innate - immunology Infections innate immunity Interferon Regulatory Factors - metabolism Kinases Membrane Proteins - chemistry Membrane Proteins - metabolism Mice Molecular biology Molecular Sequence Data Poly I-C - pharmacology Protein Binding Protein Serine-Threonine Kinases - metabolism Proteins - chemistry Proteins - metabolism RNA Interference Sendai virus Sendai virus - immunology Sequence Alignment Signal transduction tRNA Methyltransferases Viruses |
| title | SINTBAD, a novel component of innate antiviral immunity, shares a TBK1-binding domain with NAP1 and TANK |
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