For Publishers
DiscoveryMetadataPeer reviewHostingPublishing
For Researchers
JoinPublishReviewCollect
Register
Blog
About
Search
Advanced search
My ScienceOpen
Search
For Publishers
For Researchers
Blog
About
41
views
78
references
 Top references
cited by
70
    
0 reviews
 Review
0
comments
 Comment
0
recommends
+1 Recommend
0 collections
    0
    shares
      830
      similar
       All similar
      • Record: found
      • Abstract: found
      • Article: found
      Is Open Access

      TRIM25 in the Regulation of the Antiviral Innate Immunity

      review-article

      Read this article at

      ScienceOpenPublisherPMC
          There is no author summary for this article yet. Authors can add summaries to their articles on ScienceOpen to make them more accessible to a non-specialist audience.

          Abstract

          TRIM25 is an E3 ubiquitin ligase enzyme that is involved in various cellular processes, including regulation of the innate immune response against viruses. TRIM25-mediated ubiquitination of the cytosolic pattern recognition receptor RIG-I is an essential step for initiation of the intracellular antiviral response and has been thoroughly documented. In recent years, however, additional roles of TRIM25 in early innate immunity are emerging, including negative regulation of RIG-I, activation of the melanoma differentiation-associated protein 5–mitochondrial antiviral signaling protein–TRAF6 antiviral axis and modulation of p53 levels and activity. In addition, the ability of TRIM25 to bind RNA may uncover new mechanisms by which this molecule regulates intracellular signaling and/or RNA virus replication.

          Related collections

          Most cited references78

          • Record: found
          • Abstract: found
          • Article: not found

          Triggering the interferon antiviral response through an IKK-related pathway.

          Sonia Sharma, Benjamin tenOever, Nathalie Grandvaux … (2003)
          Rapid induction of type I interferon expression, a central event in establishing the innate antiviral response, requires cooperative activation of numerous transcription factors. Although signaling pathways that activate the transcription factors nuclear factor kappaB and ATF-2/c-Jun have been well characterized, activation of the interferon regulatory factors IRF-3 and IRF-7 has remained a critical missing link in understanding interferon signaling. We report here that the IkappaB kinase (IKK)-related kinases IKKepsilon and TANK-binding kinase 1 are components of the virus-activated kinase that phosphorylate IRF-3 and IRF-7. These studies illustrate an essential role for an IKK-related kinase pathway in triggering the host antiviral response to viral infection.
          Article 0 comments Cited 404 times – based on 0 reviews     Review now
            Bookmark
            • Record: found
            • Abstract: found
            • Article: not found

            Influenza A virus NS1 targets the ubiquitin ligase TRIM25 to evade recognition by the host viral RNA sensor RIG-I.

            Michaela Ulrike Gack, Randy Allen Albrecht, Tomohiko Urano … (2009)
            The ubiquitin ligase TRIM25 mediates Lysine 63-linked ubiquitination of the N-terminal CARD domains of the viral RNA sensor RIG-I to facilitate type I interferon (IFN) production and antiviral immunity. Here, we report that the influenza A virus nonstructural protein 1 (NS1) specifically inhibits TRIM25-mediated RIG-I CARD ubiquitination, thereby suppressing RIG-I signal transduction. A novel domain in NS1 comprising E96/E97 residues mediates its interaction with the coiled-coil domain of TRIM25, thus blocking TRIM25 multimerization and RIG-I CARD domain ubiquitination. Furthermore, a recombinant influenza A virus expressing an E96A/E97A NS1 mutant is defective in blocking TRIM25-mediated antiviral IFN response and loses virulence in mice. Our findings reveal a mechanism by which influenza virus inhibits host IFN response and also emphasize the vital role of TRIM25 in modulating antiviral defenses.
            Article 0 comments Cited 353 times – based on 0 reviews     Review now
              Bookmark
              • Record: found
              • Abstract: found
              • Article: not found

              New insights into ubiquitin E3 ligase mechanism.

              Christopher Berndsen, Cynthia Wolberger (2014)
              E3 ligases carry out the final step in the ubiquitination cascade, catalyzing transfer of ubiquitin from an E2 enzyme to form a covalent bond with a substrate lysine. Three distinct classes of E3 ligases have been identified that stimulate transfer of ubiquitin and ubiquitin-like proteins through either a direct or an indirect mechanism. Only recently have the catalytic mechanisms of E3 ligases begun to be elucidated.
              Article 0 comments Cited 283 times – based on 0 reviews     Review now
                Bookmark
                All references

                Author and article information

                Contributors
                María Martín-Vicente: URI : http://frontiersin.org/people/u/467584
                Luz M. Medrano: URI : http://frontiersin.org/people/u/466658
                Salvador Resino: URI : http://frontiersin.org/people/u/407901
                Adolfo García-Sastre: URI : http://frontiersin.org/people/u/476313
                Isidoro Martínez: URI : http://frontiersin.org/people/u/371343
                Journal
                Journal ID (nlm-ta): Front Immunol
                Journal ID (iso-abbrev): Front Immunol
                Journal ID (publisher-id): Front. Immunol.
                Title: Frontiers in Immunology
                Publisher: Frontiers Media S.A.
                ISSN (Electronic): 1664-3224
                Publication date (Electronic): 22 September 2017
                Publication date Collection: 2017
                Volume: 8
                Electronic Location Identifier: 1187
                Affiliations
                [1] 1Unidad de Infección Viral e Inmunidad, Centro Nacional de Microbiología, Instituto de Salud Carlos III , Madrid, Spain
                [2] 2Department of Microbiology, Icahn School of Medicine at Mount Sinai , New York, NY, United States
                [3] 3Global Health and Emerging Pathogens Institute, Icahn School of Medicine at Mount Sinai , New York, NY, United States
                [4] 4Department of Medicine, Division of Infectious Diseases, Icahn School of Medicine at Mount Sinai , New York, NY, United States
                Author notes

                Edited by: Thomas A. Kufer, University of Hohenheim, Germany

                Reviewed by: Ashley Mansell, Hudson Institute of Medical Research, Australia; Isabelle Vergne, Centre National de la Recherche Scientifique (CNRS), France

                *Correspondence: Isidoro Martínez, imago@ 123456isciii.es

                Specialty section: This article was submitted to Molecular Innate Immunity, a section of the journal Frontiers in Immunology

                Article
                DOI: 10.3389/fimmu.2017.01187
                PMC ID: 5614919
                SO-VID: c2a2c2ae-a269-428a-9ffc-703e13d18602
                Copyright © Copyright © 2017 Martín-Vicente, Medrano, Resino, García-Sastre and Martínez.
                License:

                This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

                History
                Date received : 06 July 2017
                Date accepted : 07 September 2017
                Page count
                Figures: 3, Tables: 0, Equations: 0, References: 115, Pages: 9, Words: 6899
                Funding
                Funded by: Instituto de Salud Carlos III 10.13039/501100004587
                Award ID: PI15CIII/00024, PI14CIII/00011, CD14/00002
                Funded by: National Institutes of Health 10.13039/100000002
                Award ID: R33AI119304, R21AI129486, U19AI106754, P01AI097092, R01DA033773, R01AI088770, U19AI117873, U19AI118610, R01AI125524, U01AI124297, and R01AI127658
                Funded by: Institute of Allergy and Infectious Diseases 10.13039/100000060
                Award ID: HHSN272201400008C
                Categories
                Subject: Immunology
                Subject: Review

                ScienceOpen disciplines: Immunology
                Keywords: trim25,innate immunity,ubiquitination,virus,e3 ubiquitin ligase
                Data availability:
                ScienceOpen disciplines: Immunology
                Keywords: trim25, innate immunity, ubiquitination, virus, e3 ubiquitin ligase

                Comments

                Comment on this article

                scite_

                Similar content830

                See all similar

                Cited by69

                See all cited by

                Most referenced authors1,254

                See all reference authors