Subcellular Localizations of RIG-I, TRIM25, and MAVS Complexes.
Identifieur interne : 000A63 ( Main/Exploration ); précédent : 000A62; suivant : 000A64Subcellular Localizations of RIG-I, TRIM25, and MAVS Complexes.
Auteurs : M T Sánchez-Aparicio [États-Unis] ; J. Ayll N [États-Unis] ; A. Leo-Macias [États-Unis] ; T. Wolff [Allemagne] ; A. García-Sastre [États-Unis]Source :
- Journal of virology [ 1098-5514 ] ; 2017.
Descripteurs français
- KwdFr :
- Complexes multiprotéiques (métabolisme), Espace intracellulaire, Facteurs de transcription (), Facteurs de transcription (métabolisme), Humains, Immunité innée, Interactions hôte-pathogène, Liaison aux protéines, Lignée cellulaire, Multimérisation de protéines, Protéine-58 à domaine DEAD (), Protéine-58 à domaine DEAD (métabolisme), Protéines adaptatrices de la transduction du signal (), Protéines adaptatrices de la transduction du signal (métabolisme), Protéines virales non structurales (métabolisme), Protéines à motif tripartite (), Protéines à motif tripartite (métabolisme), Transduction du signal, Transport de protéines, Ubiquitin-protein ligases (), Ubiquitin-protein ligases (métabolisme).
- MESH :
- métabolisme : Complexes multiprotéiques, Facteurs de transcription, Protéine-58 à domaine DEAD, Protéines adaptatrices de la transduction du signal, Protéines virales non structurales, Protéines à motif tripartite, Ubiquitin-protein ligases.
- Espace intracellulaire, Facteurs de transcription, Humains, Immunité innée, Interactions hôte-pathogène, Liaison aux protéines, Lignée cellulaire, Multimérisation de protéines, Protéine-58 à domaine DEAD, Protéines adaptatrices de la transduction du signal, Protéines à motif tripartite, Transduction du signal, Transport de protéines, Ubiquitin-protein ligases.
English descriptors
- KwdEn :
- Adaptor Proteins, Signal Transducing (chemistry), Adaptor Proteins, Signal Transducing (metabolism), Cell Line, DEAD Box Protein 58 (chemistry), DEAD Box Protein 58 (metabolism), Host-Pathogen Interactions, Humans, Immunity, Innate, Intracellular Space, Multiprotein Complexes (metabolism), Protein Binding, Protein Multimerization, Protein Transport, Signal Transduction, Transcription Factors (chemistry), Transcription Factors (metabolism), Tripartite Motif Proteins (chemistry), Tripartite Motif Proteins (metabolism), Ubiquitin-Protein Ligases (chemistry), Ubiquitin-Protein Ligases (metabolism), Viral Nonstructural Proteins (metabolism).
- MESH :
- chemical , chemistry : Adaptor Proteins, Signal Transducing, DEAD Box Protein 58, Transcription Factors, Tripartite Motif Proteins, Ubiquitin-Protein Ligases.
- chemical , metabolism : Adaptor Proteins, Signal Transducing, DEAD Box Protein 58, Multiprotein Complexes, Transcription Factors, Tripartite Motif Proteins, Ubiquitin-Protein Ligases, Viral Nonstructural Proteins.
- Cell Line, Host-Pathogen Interactions, Humans, Immunity, Innate, Intracellular Space, Protein Binding, Protein Multimerization, Protein Transport, Signal Transduction.
Abstract
The retinoic acid-inducible gene 1 (RIG-I) signaling pathway is essential for the recognition of viruses and the initiation of host interferon (IFN)-mediated antiviral responses. Once activated, RIG-I interacts with polyubiquitin chains generated by TRIM25 and binds mitochondrial antiviral signaling protein (MAVS), leading to the production of type I IFN. We now show specific interactions among these key partners in the RLR pathway through the use of bimolecular fluorescence complementation (BiFC) and super-resolution microscopy. Dimers of RIG-I, TRIM25, and MAVS localize into different compartments. Upon activation, we show that TRIM25 is redistributed into cytoplasmic dots associated with stress granules, while RIG-I associates with TRIM25/stress granules and with mitochondrial MAVS. In addition, MAVS competes with TRIM25 for RIG-I binding, and this suggests that upon TRIM25-mediated activation of RIG-I, RIG-I moves away from TRIM25 to interact with MAVS at the mitochondria. For the first time, the distribution of these three proteins was analyzed at the same time in virus-infected cells. We also investigated how specific viral proteins modify some of the protein complexes in the pathway. The protease NS3/4A from hepatitis C virus redistributes the complexes RIG-I/MAVS and MAVS/MAVS but not RIG-I/TRIM25. In contrast, the influenza A virus NS1 protein interacts with RIG-I and TRIM25 in specific areas in the cell cytoplasm and inhibits the formation of TRIM25 homocomplexes but not the formation of RIG-I/TRIM25 heterocomplexes, preventing the formation of RIG-I/MAVS complexes. Thus, we have localized spatially in the cell different complexes formed between RIG-I, TRIM25, and MAVS, in the presence or absence of two viral IFN antagonistic proteins.
DOI: 10.1128/JVI.01155-16
PubMed: 27807226
Affiliations:
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Le document en format XML
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<term>DEAD Box Protein 58 (chemistry)</term>
<term>DEAD Box Protein 58 (metabolism)</term>
<term>Host-Pathogen Interactions</term>
<term>Humans</term>
<term>Immunity, Innate</term>
<term>Intracellular Space</term>
<term>Multiprotein Complexes (metabolism)</term>
<term>Protein Binding</term>
<term>Protein Multimerization</term>
<term>Protein Transport</term>
<term>Signal Transduction</term>
<term>Transcription Factors (chemistry)</term>
<term>Transcription Factors (metabolism)</term>
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<term>Tripartite Motif Proteins (metabolism)</term>
<term>Ubiquitin-Protein Ligases (chemistry)</term>
<term>Ubiquitin-Protein Ligases (metabolism)</term>
<term>Viral Nonstructural Proteins (metabolism)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Complexes multiprotéiques (métabolisme)</term>
<term>Espace intracellulaire</term>
<term>Facteurs de transcription ()</term>
<term>Facteurs de transcription (métabolisme)</term>
<term>Humains</term>
<term>Immunité innée</term>
<term>Interactions hôte-pathogène</term>
<term>Liaison aux protéines</term>
<term>Lignée cellulaire</term>
<term>Multimérisation de protéines</term>
<term>Protéine-58 à domaine DEAD ()</term>
<term>Protéine-58 à domaine DEAD (métabolisme)</term>
<term>Protéines adaptatrices de la transduction du signal ()</term>
<term>Protéines adaptatrices de la transduction du signal (métabolisme)</term>
<term>Protéines virales non structurales (métabolisme)</term>
<term>Protéines à motif tripartite ()</term>
<term>Protéines à motif tripartite (métabolisme)</term>
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<term>Transport de protéines</term>
<term>Ubiquitin-protein ligases ()</term>
<term>Ubiquitin-protein ligases (métabolisme)</term>
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<term>Ubiquitin-Protein Ligases</term>
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<term>DEAD Box Protein 58</term>
<term>Multiprotein Complexes</term>
<term>Transcription Factors</term>
<term>Tripartite Motif Proteins</term>
<term>Ubiquitin-Protein Ligases</term>
<term>Viral Nonstructural Proteins</term>
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<term>Protéine-58 à domaine DEAD</term>
<term>Protéines adaptatrices de la transduction du signal</term>
<term>Protéines virales non structurales</term>
<term>Protéines à motif tripartite</term>
<term>Ubiquitin-protein ligases</term>
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<term>Host-Pathogen Interactions</term>
<term>Humans</term>
<term>Immunity, Innate</term>
<term>Intracellular Space</term>
<term>Protein Binding</term>
<term>Protein Multimerization</term>
<term>Protein Transport</term>
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<term>Facteurs de transcription</term>
<term>Humains</term>
<term>Immunité innée</term>
<term>Interactions hôte-pathogène</term>
<term>Liaison aux protéines</term>
<term>Lignée cellulaire</term>
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<term>Protéines adaptatrices de la transduction du signal</term>
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<front><div type="abstract" xml:lang="en">The retinoic acid-inducible gene 1 (RIG-I) signaling pathway is essential for the recognition of viruses and the initiation of host interferon (IFN)-mediated antiviral responses. Once activated, RIG-I interacts with polyubiquitin chains generated by TRIM25 and binds mitochondrial antiviral signaling protein (MAVS), leading to the production of type I IFN. We now show specific interactions among these key partners in the RLR pathway through the use of bimolecular fluorescence complementation (BiFC) and super-resolution microscopy. Dimers of RIG-I, TRIM25, and MAVS localize into different compartments. Upon activation, we show that TRIM25 is redistributed into cytoplasmic dots associated with stress granules, while RIG-I associates with TRIM25/stress granules and with mitochondrial MAVS. In addition, MAVS competes with TRIM25 for RIG-I binding, and this suggests that upon TRIM25-mediated activation of RIG-I, RIG-I moves away from TRIM25 to interact with MAVS at the mitochondria. For the first time, the distribution of these three proteins was analyzed at the same time in virus-infected cells. We also investigated how specific viral proteins modify some of the protein complexes in the pathway. The protease NS3/4A from hepatitis C virus redistributes the complexes RIG-I/MAVS and MAVS/MAVS but not RIG-I/TRIM25. In contrast, the influenza A virus NS1 protein interacts with RIG-I and TRIM25 in specific areas in the cell cytoplasm and inhibits the formation of TRIM25 homocomplexes but not the formation of RIG-I/TRIM25 heterocomplexes, preventing the formation of RIG-I/MAVS complexes. Thus, we have localized spatially in the cell different complexes formed between RIG-I, TRIM25, and MAVS, in the presence or absence of two viral IFN antagonistic proteins.</div>
</front>
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<name sortKey="Ayll N, J" sort="Ayll N, J" uniqKey="Ayll N J" first="J" last="Ayll N">J. Ayll N</name>
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<name sortKey="Leo Macias, A" sort="Leo Macias, A" uniqKey="Leo Macias A" first="A" last="Leo-Macias">A. Leo-Macias</name>
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