RapamycinFungusV1, Main, Exploration, bibRecord, 000724

TRIM23 mediates virus-induced autophagy via activation of TBK1.

Identifieur interne : 000724 ( Main/Exploration ); précédent : 000723; suivant : 000725

TRIM23 mediates virus-induced autophagy via activation of TBK1.

Auteurs : Konstantin M J. Sparrer [États-Unis] ; Sebastian Gableske [États-Unis] ; Matthew A. Zurenski [États-Unis] ; Zachary M. Parker [États-Unis] ; Florian Full [États-Unis] ; Gavin J. Baumgart [États-Unis] ; Jiro Kato [États-Unis] ; Gustavo Pacheco-Rodriguez [États-Unis] ; Chengyu Liang [États-Unis] ; Owen Pornillos [États-Unis] ; Joel Moss [États-Unis] ; Martha Vaughan [États-Unis] ; Michaela U. Gack [États-Unis]

Source :

Nature microbiology [ 2058-5276 ] ; 2017.

RBID : pubmed:28871090

Descripteurs français

English descriptors

KwdEn :
- Autophagy (MeSH), Encephalomyocarditis virus (physiology), Enzyme Activation (MeSH), GTP-Binding Proteins (chemistry), GTP-Binding Proteins (genetics), GTP-Binding Proteins (metabolism), Guanosine Triphosphate (metabolism), Herpesvirus 1, Human (physiology), Host-Pathogen Interactions (MeSH), Humans (MeSH), Hydrolysis (MeSH), Immunity, Innate (MeSH), Influenza A virus (physiology), Phosphorylation (MeSH), Protein-Serine-Threonine Kinases (chemistry), Protein-Serine-Threonine Kinases (genetics), Protein-Serine-Threonine Kinases (metabolism), RNA Interference (MeSH), Signal Transduction (MeSH), Ubiquitin-Protein Ligases (genetics), Ubiquitin-Protein Ligases (metabolism), Ubiquitination (MeSH), Virus Physiological Phenomena (MeSH).
MESH :
- chemical , chemistry : GTP-Binding Proteins, Protein-Serine-Threonine Kinases.
- chemical , genetics : GTP-Binding Proteins, Protein-Serine-Threonine Kinases, Ubiquitin-Protein Ligases.
- chemical , metabolism : GTP-Binding Proteins, Guanosine Triphosphate, Protein-Serine-Threonine Kinases, Ubiquitin-Protein Ligases.
- physiology : Encephalomyocarditis virus, Herpesvirus 1, Human, Influenza A virus.
- Autophagy, Enzyme Activation, Host-Pathogen Interactions, Humans, Hydrolysis, Immunity, Innate, Phosphorylation, RNA Interference, Signal Transduction, Ubiquitination, Virus Physiological Phenomena.

Abstract

Autophagy and interferon (IFN)-mediated innate immunity are critical antiviral defence mechanisms, and recent evidence indicated that tripartite motif (TRIM) proteins are important regulators of both processes. Although the role of TRIM proteins in modulating antiviral cytokine responses has been well established, much less is known about their involvement in autophagy in response to different viral pathogens. Through a targeted RNAi screen examining the relevance of selected TRIM proteins in autophagy induced by herpes simplex virus 1 (HSV-1), encephalomyocarditis virus (EMCV) and influenza A virus (IAV), we identified several TRIM proteins that regulate autophagy in a virus-species-specific manner, as well as a few TRIM proteins that were essential for autophagy triggered by all three viruses and rapamycin, among them TRIM23. TRIM23 was critical for autophagy-mediated restriction of multiple viruses, and this activity was dependent on both its RING E3 ligase and ADP-ribosylation factor (ARF) GTPase activity. Mechanistic studies revealed that unconventional K27-linked auto-ubiquitination of the ARF domain is essential for the GTP hydrolysis activity of TRIM23 and activation of TANK-binding kinase 1 (TBK1) by facilitating its dimerization and ability to phosphorylate the selective autophagy receptor p62. Our work identifies the TRIM23-TBK1-p62 axis as a key component of selective autophagy and further reveals a role for K27-linked ubiquitination in GTPase-dependent TBK1 activation.

DOI: 10.1038/s41564-017-0017-2
PubMed: 28871090
PubMed Central: PMC5658249

Affiliations:

Links toward previous steps (curation, corpus...)

to stream Main, to step Corpus: 000740
to stream Main, to step Curation: 000740

Le document en format XML

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<author><name sortKey="Pacheco Rodriguez, Gustavo" sort="Pacheco Rodriguez, Gustavo" uniqKey="Pacheco Rodriguez G" first="Gustavo" last="Pacheco-Rodriguez">Gustavo Pacheco-Rodriguez</name>
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<author><name sortKey="Gack, Michaela U" sort="Gack, Michaela U" uniqKey="Gack M" first="Michaela U" last="Gack">Michaela U. Gack</name>
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<sourceDesc><biblStruct><analytic><title xml:lang="en">TRIM23 mediates virus-induced autophagy via activation of TBK1.</title>
<author><name sortKey="Sparrer, Konstantin M J" sort="Sparrer, Konstantin M J" uniqKey="Sparrer K" first="Konstantin M J" last="Sparrer">Konstantin M J. Sparrer</name>
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<orgName type="university">Université de Chicago</orgName>
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<author><name sortKey="Baumgart, Gavin J" sort="Baumgart, Gavin J" uniqKey="Baumgart G" first="Gavin J" last="Baumgart">Gavin J. Baumgart</name>
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<wicri:regionArea>Department of Microbiology, The University of Chicago, Chicago, IL, 60637</wicri:regionArea>
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<region type="state">Illinois</region>
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<author><name sortKey="Kato, Jiro" sort="Kato, Jiro" uniqKey="Kato J" first="Jiro" last="Kato">Jiro Kato</name>
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<country xml:lang="fr">États-Unis</country>
<wicri:regionArea>Cardiovascular and Pulmonary Branch, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, MD, 20892</wicri:regionArea>
<wicri:noRegion>20892</wicri:noRegion>
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<author><name sortKey="Pacheco Rodriguez, Gustavo" sort="Pacheco Rodriguez, Gustavo" uniqKey="Pacheco Rodriguez G" first="Gustavo" last="Pacheco-Rodriguez">Gustavo Pacheco-Rodriguez</name>
<affiliation wicri:level="1"><nlm:affiliation>Cardiovascular and Pulmonary Branch, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, MD, 20892, USA.</nlm:affiliation>
<country xml:lang="fr">États-Unis</country>
<wicri:regionArea>Cardiovascular and Pulmonary Branch, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, MD, 20892</wicri:regionArea>
<wicri:noRegion>20892</wicri:noRegion>
</affiliation>
</author>
<author><name sortKey="Liang, Chengyu" sort="Liang, Chengyu" uniqKey="Liang C" first="Chengyu" last="Liang">Chengyu Liang</name>
<affiliation wicri:level="4"><nlm:affiliation>Department of Molecular Microbiology and Immunology, Keck School of Medicine, University of Southern California, Los Angeles, CA, 90033, USA.</nlm:affiliation>
<country xml:lang="fr">États-Unis</country>
<wicri:regionArea>Department of Molecular Microbiology and Immunology, Keck School of Medicine, University of Southern California, Los Angeles, CA, 90033</wicri:regionArea>
<orgName type="university">Université de Californie du Sud</orgName>
<placeName><settlement type="city">Los Angeles</settlement>
<region type="state">Californie</region>
</placeName>
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</author>
<author><name sortKey="Pornillos, Owen" sort="Pornillos, Owen" uniqKey="Pornillos O" first="Owen" last="Pornillos">Owen Pornillos</name>
<affiliation wicri:level="1"><nlm:affiliation>Department of Molecular Physiology and Biological Physics, University of Virginia, Charlottesville, VA, 22908, USA.</nlm:affiliation>
<country xml:lang="fr">États-Unis</country>
<wicri:regionArea>Department of Molecular Physiology and Biological Physics, University of Virginia, Charlottesville, VA, 22908</wicri:regionArea>
<wicri:noRegion>22908</wicri:noRegion>
</affiliation>
</author>
<author><name sortKey="Moss, Joel" sort="Moss, Joel" uniqKey="Moss J" first="Joel" last="Moss">Joel Moss</name>
<affiliation wicri:level="1"><nlm:affiliation>Cardiovascular and Pulmonary Branch, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, MD, 20892, USA.</nlm:affiliation>
<country xml:lang="fr">États-Unis</country>
<wicri:regionArea>Cardiovascular and Pulmonary Branch, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, MD, 20892</wicri:regionArea>
<wicri:noRegion>20892</wicri:noRegion>
</affiliation>
</author>
<author><name sortKey="Vaughan, Martha" sort="Vaughan, Martha" uniqKey="Vaughan M" first="Martha" last="Vaughan">Martha Vaughan</name>
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<country xml:lang="fr">États-Unis</country>
<wicri:regionArea>Cardiovascular and Pulmonary Branch, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, MD, 20892</wicri:regionArea>
<wicri:noRegion>20892</wicri:noRegion>
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</author>
<author><name sortKey="Gack, Michaela U" sort="Gack, Michaela U" uniqKey="Gack M" first="Michaela U" last="Gack">Michaela U. Gack</name>
<affiliation wicri:level="4"><nlm:affiliation>Department of Microbiology, The University of Chicago, Chicago, IL, 60637, USA. mgack@uchicago.edu.</nlm:affiliation>
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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Autophagy (MeSH)</term>
<term>Encephalomyocarditis virus (physiology)</term>
<term>Enzyme Activation (MeSH)</term>
<term>GTP-Binding Proteins (chemistry)</term>
<term>GTP-Binding Proteins (genetics)</term>
<term>GTP-Binding Proteins (metabolism)</term>
<term>Guanosine Triphosphate (metabolism)</term>
<term>Herpesvirus 1, Human (physiology)</term>
<term>Host-Pathogen Interactions (MeSH)</term>
<term>Humans (MeSH)</term>
<term>Hydrolysis (MeSH)</term>
<term>Immunity, Innate (MeSH)</term>
<term>Influenza A virus (physiology)</term>
<term>Phosphorylation (MeSH)</term>
<term>Protein-Serine-Threonine Kinases (chemistry)</term>
<term>Protein-Serine-Threonine Kinases (genetics)</term>
<term>Protein-Serine-Threonine Kinases (metabolism)</term>
<term>RNA Interference (MeSH)</term>
<term>Signal Transduction (MeSH)</term>
<term>Ubiquitin-Protein Ligases (genetics)</term>
<term>Ubiquitin-Protein Ligases (metabolism)</term>
<term>Ubiquitination (MeSH)</term>
<term>Virus Physiological Phenomena (MeSH)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Activation enzymatique (MeSH)</term>
<term>Autophagie (MeSH)</term>
<term>Guanosine triphosphate (métabolisme)</term>
<term>Herpèsvirus humain de type 1 (physiologie)</term>
<term>Humains (MeSH)</term>
<term>Hydrolyse (MeSH)</term>
<term>Immunité innée (MeSH)</term>
<term>Interactions hôte-pathogène (MeSH)</term>
<term>Interférence par ARN (MeSH)</term>
<term>Phosphorylation (MeSH)</term>
<term>Phénomènes physiologiques viraux (MeSH)</term>
<term>Protein-Serine-Threonine Kinases (composition chimique)</term>
<term>Protein-Serine-Threonine Kinases (génétique)</term>
<term>Protein-Serine-Threonine Kinases (métabolisme)</term>
<term>Protéines G (composition chimique)</term>
<term>Protéines G (génétique)</term>
<term>Protéines G (métabolisme)</term>
<term>Transduction du signal (MeSH)</term>
<term>Ubiquitin-protein ligases (génétique)</term>
<term>Ubiquitin-protein ligases (métabolisme)</term>
<term>Ubiquitination (MeSH)</term>
<term>Virus de l'encéphalomyocardite (physiologie)</term>
<term>Virus de la grippe A (physiologie)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>GTP-Binding Proteins</term>
<term>Protein-Serine-Threonine Kinases</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>GTP-Binding Proteins</term>
<term>Protein-Serine-Threonine Kinases</term>
<term>Ubiquitin-Protein Ligases</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>GTP-Binding Proteins</term>
<term>Guanosine Triphosphate</term>
<term>Protein-Serine-Threonine Kinases</term>
<term>Ubiquitin-Protein Ligases</term>
</keywords>
<keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Protein-Serine-Threonine Kinases</term>
<term>Protéines G</term>
</keywords>
<keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Protein-Serine-Threonine Kinases</term>
<term>Protéines G</term>
<term>Ubiquitin-protein ligases</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Guanosine triphosphate</term>
<term>Protein-Serine-Threonine Kinases</term>
<term>Protéines G</term>
<term>Ubiquitin-protein ligases</term>
</keywords>
<keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Herpèsvirus humain de type 1</term>
<term>Virus de l'encéphalomyocardite</term>
<term>Virus de la grippe A</term>
</keywords>
<keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Encephalomyocarditis virus</term>
<term>Herpesvirus 1, Human</term>
<term>Influenza A virus</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Autophagy</term>
<term>Enzyme Activation</term>
<term>Host-Pathogen Interactions</term>
<term>Humans</term>
<term>Hydrolysis</term>
<term>Immunity, Innate</term>
<term>Phosphorylation</term>
<term>RNA Interference</term>
<term>Signal Transduction</term>
<term>Ubiquitination</term>
<term>Virus Physiological Phenomena</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr"><term>Activation enzymatique</term>
<term>Autophagie</term>
<term>Humains</term>
<term>Hydrolyse</term>
<term>Immunité innée</term>
<term>Interactions hôte-pathogène</term>
<term>Interférence par ARN</term>
<term>Phosphorylation</term>
<term>Phénomènes physiologiques viraux</term>
<term>Transduction du signal</term>
<term>Ubiquitination</term>
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<front><div type="abstract" xml:lang="en">Autophagy and interferon (IFN)-mediated innate immunity are critical antiviral defence mechanisms, and recent evidence indicated that tripartite motif (TRIM) proteins are important regulators of both processes. Although the role of TRIM proteins in modulating antiviral cytokine responses has been well established, much less is known about their involvement in autophagy in response to different viral pathogens. Through a targeted RNAi screen examining the relevance of selected TRIM proteins in autophagy induced by herpes simplex virus 1 (HSV-1), encephalomyocarditis virus (EMCV) and influenza A virus (IAV), we identified several TRIM proteins that regulate autophagy in a virus-species-specific manner, as well as a few TRIM proteins that were essential for autophagy triggered by all three viruses and rapamycin, among them TRIM23. TRIM23 was critical for autophagy-mediated restriction of multiple viruses, and this activity was dependent on both its RING E3 ligase and ADP-ribosylation factor (ARF) GTPase activity. Mechanistic studies revealed that unconventional K27-linked auto-ubiquitination of the ARF domain is essential for the GTP hydrolysis activity of TRIM23 and activation of TANK-binding kinase 1 (TBK1) by facilitating its dimerization and ability to phosphorylate the selective autophagy receptor p62. Our work identifies the TRIM23-TBK1-p62 axis as a key component of selective autophagy and further reveals a role for K27-linked ubiquitination in GTPase-dependent TBK1 activation.</div>
</front>
</TEI>
<pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">28871090</PMID>
<DateCompleted><Year>2018</Year>
<Month>06</Month>
<Day>11</Day>
</DateCompleted>
<DateRevised><Year>2018</Year>
<Month>11</Month>
<Day>13</Day>
</DateRevised>
<Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">2058-5276</ISSN>
<JournalIssue CitedMedium="Internet"><Volume>2</Volume>
<Issue>11</Issue>
<PubDate><Year>2017</Year>
<Month>Nov</Month>
</PubDate>
</JournalIssue>
<Title>Nature microbiology</Title>
<ISOAbbreviation>Nat Microbiol</ISOAbbreviation>
</Journal>
<ArticleTitle>TRIM23 mediates virus-induced autophagy via activation of TBK1.</ArticleTitle>
<Pagination><MedlinePgn>1543-1557</MedlinePgn>
</Pagination>
<ELocationID EIdType="doi" ValidYN="Y">10.1038/s41564-017-0017-2</ELocationID>
<Abstract><AbstractText>Autophagy and interferon (IFN)-mediated innate immunity are critical antiviral defence mechanisms, and recent evidence indicated that tripartite motif (TRIM) proteins are important regulators of both processes. Although the role of TRIM proteins in modulating antiviral cytokine responses has been well established, much less is known about their involvement in autophagy in response to different viral pathogens. Through a targeted RNAi screen examining the relevance of selected TRIM proteins in autophagy induced by herpes simplex virus 1 (HSV-1), encephalomyocarditis virus (EMCV) and influenza A virus (IAV), we identified several TRIM proteins that regulate autophagy in a virus-species-specific manner, as well as a few TRIM proteins that were essential for autophagy triggered by all three viruses and rapamycin, among them TRIM23. TRIM23 was critical for autophagy-mediated restriction of multiple viruses, and this activity was dependent on both its RING E3 ligase and ADP-ribosylation factor (ARF) GTPase activity. Mechanistic studies revealed that unconventional K27-linked auto-ubiquitination of the ARF domain is essential for the GTP hydrolysis activity of TRIM23 and activation of TANK-binding kinase 1 (TBK1) by facilitating its dimerization and ability to phosphorylate the selective autophagy receptor p62. Our work identifies the TRIM23-TBK1-p62 axis as a key component of selective autophagy and further reveals a role for K27-linked ubiquitination in GTPase-dependent TBK1 activation.</AbstractText>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Sparrer</LastName>
<ForeName>Konstantin M J</ForeName>
<Initials>KMJ</Initials>
<AffiliationInfo><Affiliation>Department of Microbiology, The University of Chicago, Chicago, IL, 60637, USA.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Gableske</LastName>
<ForeName>Sebastian</ForeName>
<Initials>S</Initials>
<AffiliationInfo><Affiliation>Department of Microbiology, The University of Chicago, Chicago, IL, 60637, USA.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Zurenski</LastName>
<ForeName>Matthew A</ForeName>
<Initials>MA</Initials>
<AffiliationInfo><Affiliation>Department of Microbiology, The University of Chicago, Chicago, IL, 60637, USA.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Parker</LastName>
<ForeName>Zachary M</ForeName>
<Initials>ZM</Initials>
<AffiliationInfo><Affiliation>Department of Microbiology, The University of Chicago, Chicago, IL, 60637, USA.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Full</LastName>
<ForeName>Florian</ForeName>
<Initials>F</Initials>
<AffiliationInfo><Affiliation>Department of Microbiology, The University of Chicago, Chicago, IL, 60637, USA.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Baumgart</LastName>
<ForeName>Gavin J</ForeName>
<Initials>GJ</Initials>
<AffiliationInfo><Affiliation>Department of Microbiology, The University of Chicago, Chicago, IL, 60637, USA.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Kato</LastName>
<ForeName>Jiro</ForeName>
<Initials>J</Initials>
<AffiliationInfo><Affiliation>Cardiovascular and Pulmonary Branch, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, MD, 20892, USA.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Pacheco-Rodriguez</LastName>
<ForeName>Gustavo</ForeName>
<Initials>G</Initials>
<AffiliationInfo><Affiliation>Cardiovascular and Pulmonary Branch, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, MD, 20892, USA.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Liang</LastName>
<ForeName>Chengyu</ForeName>
<Initials>C</Initials>
<AffiliationInfo><Affiliation>Department of Molecular Microbiology and Immunology, Keck School of Medicine, University of Southern California, Los Angeles, CA, 90033, USA.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Pornillos</LastName>
<ForeName>Owen</ForeName>
<Initials>O</Initials>
<Identifier Source="ORCID">http://orcid.org/0000-0001-9056-5002</Identifier>
<AffiliationInfo><Affiliation>Department of Molecular Physiology and Biological Physics, University of Virginia, Charlottesville, VA, 22908, USA.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Moss</LastName>
<ForeName>Joel</ForeName>
<Initials>J</Initials>
<AffiliationInfo><Affiliation>Cardiovascular and Pulmonary Branch, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, MD, 20892, USA.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Vaughan</LastName>
<ForeName>Martha</ForeName>
<Initials>M</Initials>
<AffiliationInfo><Affiliation>Cardiovascular and Pulmonary Branch, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, MD, 20892, USA.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Gack</LastName>
<ForeName>Michaela U</ForeName>
<Initials>MU</Initials>
<Identifier Source="ORCID">http://orcid.org/0000-0002-2163-2598</Identifier>
<AffiliationInfo><Affiliation>Department of Microbiology, The University of Chicago, Chicago, IL, 60637, USA. mgack@uchicago.edu.</Affiliation>
</AffiliationInfo>
</Author>
</AuthorList>
<Language>eng</Language>
<GrantList CompleteYN="Y"><Grant><GrantID>R01 AI087846</GrantID>
<Acronym>AI</Acronym>
<Agency>NIAID NIH HHS</Agency>
<Country>United States</Country>
</Grant>
<Grant><GrantID>R01 CA140964</GrantID>
<Acronym>CA</Acronym>
<Agency>NCI NIH HHS</Agency>
<Country>United States</Country>
</Grant>
<Grant><GrantID>R01 GM112508</GrantID>
<Acronym>GM</Acronym>
<Agency>NIGMS NIH HHS</Agency>
<Country>United States</Country>
</Grant>
<Grant><GrantID>R21 AI118509</GrantID>
<Acronym>AI</Acronym>
<Agency>NIAID NIH HHS</Agency>
<Country>United States</Country>
</Grant>
</GrantList>
<PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType>
</PublicationTypeList>
<ArticleDate DateType="Electronic"><Year>2017</Year>
<Month>09</Month>
<Day>04</Day>
</ArticleDate>
</Article>
<MedlineJournalInfo><Country>England</Country>
<MedlineTA>Nat Microbiol</MedlineTA>
<NlmUniqueID>101674869</NlmUniqueID>
<ISSNLinking>2058-5276</ISSNLinking>
</MedlineJournalInfo>
<ChemicalList><Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="C080681">TRIM23 protein, human</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>86-01-1</RegistryNumber>
<NameOfSubstance UI="D006160">Guanosine Triphosphate</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>EC 2.3.2.27</RegistryNumber>
<NameOfSubstance UI="D044767">Ubiquitin-Protein Ligases</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>EC 2.7.11.1</RegistryNumber>
<NameOfSubstance UI="D017346">Protein-Serine-Threonine Kinases</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>EC 2.7.11.1</RegistryNumber>
<NameOfSubstance UI="C403191">TBK1 protein, human</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>EC 3.6.1.-</RegistryNumber>
<NameOfSubstance UI="D019204">GTP-Binding Proteins</NameOfSubstance>
</Chemical>
</ChemicalList>
<CitationSubset>IM</CitationSubset>
<MeshHeadingList><MeshHeading><DescriptorName UI="D001343" MajorTopicYN="Y">Autophagy</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D004686" MajorTopicYN="N">Encephalomyocarditis virus</DescriptorName>
<QualifierName UI="Q000502" MajorTopicYN="N">physiology</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D004789" MajorTopicYN="N">Enzyme Activation</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D019204" MajorTopicYN="N">GTP-Binding Proteins</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
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<MeshHeading><DescriptorName UI="D018259" MajorTopicYN="N">Herpesvirus 1, Human</DescriptorName>
<QualifierName UI="Q000502" MajorTopicYN="N">physiology</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D054884" MajorTopicYN="Y">Host-Pathogen Interactions</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D006868" MajorTopicYN="N">Hydrolysis</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D007113" MajorTopicYN="N">Immunity, Innate</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D009980" MajorTopicYN="N">Influenza A virus</DescriptorName>
<QualifierName UI="Q000502" MajorTopicYN="N">physiology</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D010766" MajorTopicYN="N">Phosphorylation</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D017346" MajorTopicYN="N">Protein-Serine-Threonine Kinases</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D034622" MajorTopicYN="N">RNA Interference</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D015398" MajorTopicYN="N">Signal Transduction</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D044767" MajorTopicYN="N">Ubiquitin-Protein Ligases</DescriptorName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D054875" MajorTopicYN="N">Ubiquitination</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D018406" MajorTopicYN="Y">Virus Physiological Phenomena</DescriptorName>
</MeshHeading>
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<PubmedData><History><PubMedPubDate PubStatus="received"><Year>2017</Year>
<Month>03</Month>
<Day>03</Day>
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TRIM23 mediates virus-induced autophagy via activation of TBK1.

TRIM23 mediates virus-induced autophagy via activation of TBK1.

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