The Mitochondrial Targeting Chaperone 14-3-3ε Regulates a RIG-I Translocon that Mediates Membrane Association and Innate Antiviral Immunity
RIG-I is a cytosolic pathogen recognition receptor that initiates immune responses against RNA viruses. Upon viral RNA recognition, antiviral signaling requires RIG-I redistribution from the cytosol to membranes where it binds the adaptor protein, MAVS. Here we identify the mitochondrial targeting c...
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| Veröffentlicht in: | Cell host & microbe 2012-05, Vol.11 (5), p.528-537 |
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| container_title | Cell host & microbe |
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| creator | Liu, Helene Minyi Loo, Yueh-Ming Horner, Stacy M. Zornetzer, Gregory A. Katze, Michael G. Gale, Michael |
| description | RIG-I is a cytosolic pathogen recognition receptor that initiates immune responses against RNA viruses. Upon viral RNA recognition, antiviral signaling requires RIG-I redistribution from the cytosol to membranes where it binds the adaptor protein, MAVS. Here we identify the mitochondrial targeting chaperone protein, 14-3-3ε, as a RIG-I-binding partner and essential component of a translocation complex or “translocon” containing RIG-I, 14-3-3ε, and the TRIM25 ubiquitin ligase. The RIG-I translocon directs RIG-I redistribution from the cytosol to membranes where it mediates MAVS-dependent innate immune signaling during acute RNA virus infection. 14-3-3ε is essential for the stable interaction of RIG-I with TRIM25, which facilitates RIG-I ubiquitination and initiation of innate immunity against hepatitis C virus and other pathogenic RNA viruses. Our results define 14-3-3ε as a key component of a RIG-I translocon required for innate antiviral immunity.
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► RIG-I undergoes cytosol-to-membrane translocation during acute virus infection ► RNA ligand binding and CARD domains of RIG-I are required for RIG-I translocation ► 14-3-3ε is an essential chaperone protein component of the RIG-I translocon ► RIG-I/14-3-3ε/TRIM25 translocon is essential for antiviral innate immunity |
| doi_str_mv | 10.1016/j.chom.2012.04.006 |
| format | Article |
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► RIG-I undergoes cytosol-to-membrane translocation during acute virus infection ► RNA ligand binding and CARD domains of RIG-I are required for RIG-I translocation ► 14-3-3ε is an essential chaperone protein component of the RIG-I translocon ► RIG-I/14-3-3ε/TRIM25 translocon is essential for antiviral innate immunity</description><identifier>ISSN: 1931-3128</identifier><identifier>ISSN: 1934-6069</identifier><identifier>EISSN: 1934-6069</identifier><identifier>DOI: 10.1016/j.chom.2012.04.006</identifier><identifier>PMID: 22607805</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>14-3-3 Proteins - metabolism ; Cell Line ; DEAD Box Protein 58 ; DEAD-box RNA Helicases - metabolism ; Hepacivirus - immunology ; Humans ; Membrane Proteins - metabolism ; Models, Biological ; Molecular Chaperones - metabolism ; Protein Binding ; Protein Interaction Mapping ; Receptors, Immunologic ; Transcription Factors - metabolism ; Tripartite Motif Proteins ; Ubiquitin-Protein Ligases - metabolism</subject><ispartof>Cell host & microbe, 2012-05, Vol.11 (5), p.528-537</ispartof><rights>2012 Elsevier Inc.</rights><rights>Copyright © 2012 Elsevier Inc. All rights reserved.</rights><rights>2012 Elsevier Inc. All rights reserved. 2012</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c455t-828520257aa5602212c0d138f84fbb897cd602ede5afeebdd1d5a5d4fda1c1c3</citedby><cites>FETCH-LOGICAL-c455t-828520257aa5602212c0d138f84fbb897cd602ede5afeebdd1d5a5d4fda1c1c3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S1931312812001035$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>230,314,776,780,881,3537,27901,27902,65306</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/22607805$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Liu, Helene Minyi</creatorcontrib><creatorcontrib>Loo, Yueh-Ming</creatorcontrib><creatorcontrib>Horner, Stacy M.</creatorcontrib><creatorcontrib>Zornetzer, Gregory A.</creatorcontrib><creatorcontrib>Katze, Michael G.</creatorcontrib><creatorcontrib>Gale, Michael</creatorcontrib><title>The Mitochondrial Targeting Chaperone 14-3-3ε Regulates a RIG-I Translocon that Mediates Membrane Association and Innate Antiviral Immunity</title><title>Cell host & microbe</title><addtitle>Cell Host Microbe</addtitle><description>RIG-I is a cytosolic pathogen recognition receptor that initiates immune responses against RNA viruses. Upon viral RNA recognition, antiviral signaling requires RIG-I redistribution from the cytosol to membranes where it binds the adaptor protein, MAVS. Here we identify the mitochondrial targeting chaperone protein, 14-3-3ε, as a RIG-I-binding partner and essential component of a translocation complex or “translocon” containing RIG-I, 14-3-3ε, and the TRIM25 ubiquitin ligase. The RIG-I translocon directs RIG-I redistribution from the cytosol to membranes where it mediates MAVS-dependent innate immune signaling during acute RNA virus infection. 14-3-3ε is essential for the stable interaction of RIG-I with TRIM25, which facilitates RIG-I ubiquitination and initiation of innate immunity against hepatitis C virus and other pathogenic RNA viruses. Our results define 14-3-3ε as a key component of a RIG-I translocon required for innate antiviral immunity.
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► RIG-I undergoes cytosol-to-membrane translocation during acute virus infection ► RNA ligand binding and CARD domains of RIG-I are required for RIG-I translocation ► 14-3-3ε is an essential chaperone protein component of the RIG-I translocon ► RIG-I/14-3-3ε/TRIM25 translocon is essential for antiviral innate immunity</description><subject>14-3-3 Proteins - metabolism</subject><subject>Cell Line</subject><subject>DEAD Box Protein 58</subject><subject>DEAD-box RNA Helicases - metabolism</subject><subject>Hepacivirus - immunology</subject><subject>Humans</subject><subject>Membrane Proteins - metabolism</subject><subject>Models, Biological</subject><subject>Molecular Chaperones - metabolism</subject><subject>Protein Binding</subject><subject>Protein Interaction Mapping</subject><subject>Receptors, Immunologic</subject><subject>Transcription Factors - metabolism</subject><subject>Tripartite Motif Proteins</subject><subject>Ubiquitin-Protein Ligases - metabolism</subject><issn>1931-3128</issn><issn>1934-6069</issn><issn>1934-6069</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2012</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kc9u1DAQxiMEoqXwAhyQj1wSbMdOshJCWq1oidQVUpW75diTjVeJvdjOSn0HXofX4Jnq7ZYKLpxszfzmmz9flr0nuCCYVJ_2hRrdXFBMaIFZgXH1Irskq5LlFa5WLx__JC8JbS6yNyHsMeYc1-R1dkFphesG88vsZzcC2prokpTV3sgJddLvIBq7Q5tRHsA7C4iwvMzL37_QHeyWSUYISKK79iZvUeelDZNTzqI4yoi2oM0jsIW5TzlA6xCcSjGTEGk1aq1NAFrbaI7Gp47tPC_WxPu32atBTgHePb1XWXf9tdt8y2-_37Sb9W2uGOcxb2jDKaa8lpJXmFJCFdakbIaGDX3frGqlUxg0cDkA9FoTzSXXbNCSKKLKq-zLWfaw9DNoBTamKcTBm1n6e-GkEf9mrBnFzh1FWfKmxjwJfHwS8O7HAiGK2QQF05S2dUsQyR1OWcUZTig9o8q7EDwMz20IPnGV2IuTi-LkosBMJBdT0Ye_B3wu-WNbAj6fAUhXOhrwIigDVqXTe1BRaGf-p_8A47GxfA</recordid><startdate>20120517</startdate><enddate>20120517</enddate><creator>Liu, Helene Minyi</creator><creator>Loo, Yueh-Ming</creator><creator>Horner, Stacy M.</creator><creator>Zornetzer, Gregory A.</creator><creator>Katze, Michael G.</creator><creator>Gale, Michael</creator><general>Elsevier Inc</general><scope>6I.</scope><scope>AAFTH</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>7X8</scope><scope>5PM</scope></search><sort><creationdate>20120517</creationdate><title>The Mitochondrial Targeting Chaperone 14-3-3ε Regulates a RIG-I Translocon that Mediates Membrane Association and Innate Antiviral Immunity</title><author>Liu, Helene Minyi ; Loo, Yueh-Ming ; Horner, Stacy M. ; Zornetzer, Gregory A. ; Katze, Michael G. ; Gale, Michael</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c455t-828520257aa5602212c0d138f84fbb897cd602ede5afeebdd1d5a5d4fda1c1c3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2012</creationdate><topic>14-3-3 Proteins - metabolism</topic><topic>Cell Line</topic><topic>DEAD Box Protein 58</topic><topic>DEAD-box RNA Helicases - metabolism</topic><topic>Hepacivirus - immunology</topic><topic>Humans</topic><topic>Membrane Proteins - metabolism</topic><topic>Models, Biological</topic><topic>Molecular Chaperones - metabolism</topic><topic>Protein Binding</topic><topic>Protein Interaction Mapping</topic><topic>Receptors, Immunologic</topic><topic>Transcription Factors - metabolism</topic><topic>Tripartite Motif Proteins</topic><topic>Ubiquitin-Protein Ligases - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Liu, Helene Minyi</creatorcontrib><creatorcontrib>Loo, Yueh-Ming</creatorcontrib><creatorcontrib>Horner, Stacy M.</creatorcontrib><creatorcontrib>Zornetzer, Gregory A.</creatorcontrib><creatorcontrib>Katze, Michael G.</creatorcontrib><creatorcontrib>Gale, Michael</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Cell host & microbe</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Liu, Helene Minyi</au><au>Loo, Yueh-Ming</au><au>Horner, Stacy M.</au><au>Zornetzer, Gregory A.</au><au>Katze, Michael G.</au><au>Gale, Michael</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The Mitochondrial Targeting Chaperone 14-3-3ε Regulates a RIG-I Translocon that Mediates Membrane Association and Innate Antiviral Immunity</atitle><jtitle>Cell host & microbe</jtitle><addtitle>Cell Host Microbe</addtitle><date>2012-05-17</date><risdate>2012</risdate><volume>11</volume><issue>5</issue><spage>528</spage><epage>537</epage><pages>528-537</pages><issn>1931-3128</issn><issn>1934-6069</issn><eissn>1934-6069</eissn><abstract>RIG-I is a cytosolic pathogen recognition receptor that initiates immune responses against RNA viruses. Upon viral RNA recognition, antiviral signaling requires RIG-I redistribution from the cytosol to membranes where it binds the adaptor protein, MAVS. Here we identify the mitochondrial targeting chaperone protein, 14-3-3ε, as a RIG-I-binding partner and essential component of a translocation complex or “translocon” containing RIG-I, 14-3-3ε, and the TRIM25 ubiquitin ligase. The RIG-I translocon directs RIG-I redistribution from the cytosol to membranes where it mediates MAVS-dependent innate immune signaling during acute RNA virus infection. 14-3-3ε is essential for the stable interaction of RIG-I with TRIM25, which facilitates RIG-I ubiquitination and initiation of innate immunity against hepatitis C virus and other pathogenic RNA viruses. Our results define 14-3-3ε as a key component of a RIG-I translocon required for innate antiviral immunity.
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► RIG-I undergoes cytosol-to-membrane translocation during acute virus infection ► RNA ligand binding and CARD domains of RIG-I are required for RIG-I translocation ► 14-3-3ε is an essential chaperone protein component of the RIG-I translocon ► RIG-I/14-3-3ε/TRIM25 translocon is essential for antiviral innate immunity</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>22607805</pmid><doi>10.1016/j.chom.2012.04.006</doi><tpages>10</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | Cell host & microbe, 2012-05, Vol.11 (5), p.528-537 |
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| language | eng |
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| source | MEDLINE; Elsevier ScienceDirect Journals Complete; Open Access: Cell Press Free Archives; EZB Electronic Journals Library |
| subjects | 14-3-3 Proteins - metabolism Cell Line DEAD Box Protein 58 DEAD-box RNA Helicases - metabolism Hepacivirus - immunology Humans Membrane Proteins - metabolism Models, Biological Molecular Chaperones - metabolism Protein Binding Protein Interaction Mapping Receptors, Immunologic Transcription Factors - metabolism Tripartite Motif Proteins Ubiquitin-Protein Ligases - metabolism |
| title | The Mitochondrial Targeting Chaperone 14-3-3ε Regulates a RIG-I Translocon that Mediates Membrane Association and Innate Antiviral Immunity |
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