Elucidation of TRIM25 ubiquitination targets involved in diverse cellular and antiviral processes
The tripartite motif (TRIM) family of E3 ubiquitin ligases is well known for its roles in antiviral restriction and innate immunity regulation, in addition to many other cellular pathways. In particular, TRIM25-mediated ubiquitination affects both carcinogenesis and antiviral response. While individ...
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| Veröffentlicht in: | PLOS PATHOGENS 2022-09, Vol.18 (9), p.e1010743 |
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| creator | Yang, Emily Huang, Serina Jami-Alahmadi, Yasaman McInerney, Gerald M Wohlschlegel, James A Li, Melody M H |
| description | The tripartite motif (TRIM) family of E3 ubiquitin ligases is well known for its roles in antiviral restriction and innate immunity regulation, in addition to many other cellular pathways. In particular, TRIM25-mediated ubiquitination affects both carcinogenesis and antiviral response. While individual substrates have been identified for TRIM25, it remains unclear how it regulates diverse processes. Here we characterized a mutation, R54P, critical for TRIM25 catalytic activity, which we successfully utilized to "trap" substrates. We demonstrated that TRIM25 targets proteins implicated in stress granule formation (G3BP1/2), nonsense-mediated mRNA decay (UPF1), nucleoside synthesis (NME1), and mRNA translation and stability (PABPC4). The R54P mutation abolishes TRIM25 inhibition of alphaviruses independently of the host interferon response, suggesting that this antiviral effect is a direct consequence of ubiquitination. Consistent with that, we observed diminished antiviral activity upon knockdown of several TRIM25-R54P specific interactors including NME1 and PABPC4. Our findings highlight that multiple substrates mediate the cellular and antiviral activities of TRIM25, illustrating the multi-faceted role of this ubiquitination network in modulating diverse biological processes. |
| doi_str_mv | 10.1371/journal.ppat.1010743 |
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In particular, TRIM25-mediated ubiquitination affects both carcinogenesis and antiviral response. While individual substrates have been identified for TRIM25, it remains unclear how it regulates diverse processes. Here we characterized a mutation, R54P, critical for TRIM25 catalytic activity, which we successfully utilized to "trap" substrates. We demonstrated that TRIM25 targets proteins implicated in stress granule formation (G3BP1/2), nonsense-mediated mRNA decay (UPF1), nucleoside synthesis (NME1), and mRNA translation and stability (PABPC4). The R54P mutation abolishes TRIM25 inhibition of alphaviruses independently of the host interferon response, suggesting that this antiviral effect is a direct consequence of ubiquitination. Consistent with that, we observed diminished antiviral activity upon knockdown of several TRIM25-R54P specific interactors including NME1 and PABPC4. Our findings highlight that multiple substrates mediate the cellular and antiviral activities of TRIM25, illustrating the multi-faceted role of this ubiquitination network in modulating diverse biological processes.</description><identifier>ISSN: 1553-7374</identifier><identifier>ISSN: 1553-7366</identifier><identifier>EISSN: 1553-7374</identifier><identifier>DOI: 10.1371/journal.ppat.1010743</identifier><identifier>PMID: 36067236</identifier><language>eng</language><publisher>United States: Public Library of Science</publisher><subject>Antiviral activity ; Antiviral Agents - metabolism ; Antiviral drugs ; Biological activity ; Biology and Life Sciences ; Carcinogenesis ; Carcinogens ; Catalytic activity ; Cellular proteins ; DNA Helicases - metabolism ; Enzymes ; Experiments ; Health aspects ; Infections ; Innate immunity ; Interferon ; Interferons - metabolism ; Kinases ; Ligases ; mRNA stability ; mRNA turnover ; Mutation ; Nonsense-mediated mRNA decay ; Nucleosides - metabolism ; Poly-ADP-Ribose Binding Proteins - metabolism ; Proteins ; Research and Analysis Methods ; RNA Helicases - metabolism ; RNA Recognition Motif Proteins - metabolism ; Substrates ; Transcription ; Tripartite Motif Proteins - genetics ; Tripartite Motif Proteins - metabolism ; Ubiquitin ; Ubiquitin-proteasome system ; Ubiquitin-protein ligase ; Ubiquitin-Protein Ligases - metabolism ; Ubiquitination ; Ubiquitins - metabolism ; Viral infections</subject><ispartof>PLOS PATHOGENS, 2022-09, Vol.18 (9), p.e1010743</ispartof><rights>COPYRIGHT 2022 Public Library of Science</rights><rights>2022 Yang et al. This is an open access article distributed under the terms of the Creative Commons Attribution License: http://creativecommons.org/licenses/by/4.0/ (the “License”), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><rights>2022 Yang et al 2022 Yang et al</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c699t-50aed561fe339c190a44c869d6b2ccc422cd2c78434b174303a07372d6fe21733</citedby><cites>FETCH-LOGICAL-c699t-50aed561fe339c190a44c869d6b2ccc422cd2c78434b174303a07372d6fe21733</cites><orcidid>0000-0002-6905-7940</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC9481182/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC9481182/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,550,723,776,780,860,881,2096,2915,23845,27901,27902,53766,53768,79342,79343</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/36067236$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttp://kipublications.ki.se/Default.aspx?queryparsed=id:151419336$$DView record from Swedish Publication Index$$Hfree_for_read</backlink></links><search><creatorcontrib>Yang, Emily</creatorcontrib><creatorcontrib>Huang, Serina</creatorcontrib><creatorcontrib>Jami-Alahmadi, Yasaman</creatorcontrib><creatorcontrib>McInerney, Gerald M</creatorcontrib><creatorcontrib>Wohlschlegel, James A</creatorcontrib><creatorcontrib>Li, Melody M H</creatorcontrib><title>Elucidation of TRIM25 ubiquitination targets involved in diverse cellular and antiviral processes</title><title>PLOS PATHOGENS</title><addtitle>PLoS Pathog</addtitle><description>The tripartite motif (TRIM) family of E3 ubiquitin ligases is well known for its roles in antiviral restriction and innate immunity regulation, in addition to many other cellular pathways. In particular, TRIM25-mediated ubiquitination affects both carcinogenesis and antiviral response. While individual substrates have been identified for TRIM25, it remains unclear how it regulates diverse processes. Here we characterized a mutation, R54P, critical for TRIM25 catalytic activity, which we successfully utilized to "trap" substrates. We demonstrated that TRIM25 targets proteins implicated in stress granule formation (G3BP1/2), nonsense-mediated mRNA decay (UPF1), nucleoside synthesis (NME1), and mRNA translation and stability (PABPC4). The R54P mutation abolishes TRIM25 inhibition of alphaviruses independently of the host interferon response, suggesting that this antiviral effect is a direct consequence of ubiquitination. Consistent with that, we observed diminished antiviral activity upon knockdown of several TRIM25-R54P specific interactors including NME1 and PABPC4. Our findings highlight that multiple substrates mediate the cellular and antiviral activities of TRIM25, illustrating the multi-faceted role of this ubiquitination network in modulating diverse biological processes.</description><subject>Antiviral activity</subject><subject>Antiviral Agents - metabolism</subject><subject>Antiviral drugs</subject><subject>Biological activity</subject><subject>Biology and Life Sciences</subject><subject>Carcinogenesis</subject><subject>Carcinogens</subject><subject>Catalytic activity</subject><subject>Cellular proteins</subject><subject>DNA Helicases - metabolism</subject><subject>Enzymes</subject><subject>Experiments</subject><subject>Health aspects</subject><subject>Infections</subject><subject>Innate immunity</subject><subject>Interferon</subject><subject>Interferons - metabolism</subject><subject>Kinases</subject><subject>Ligases</subject><subject>mRNA stability</subject><subject>mRNA turnover</subject><subject>Mutation</subject><subject>Nonsense-mediated mRNA decay</subject><subject>Nucleosides - metabolism</subject><subject>Poly-ADP-Ribose Binding Proteins - metabolism</subject><subject>Proteins</subject><subject>Research and Analysis Methods</subject><subject>RNA Helicases - metabolism</subject><subject>RNA Recognition Motif Proteins - metabolism</subject><subject>Substrates</subject><subject>Transcription</subject><subject>Tripartite Motif Proteins - genetics</subject><subject>Tripartite Motif Proteins - metabolism</subject><subject>Ubiquitin</subject><subject>Ubiquitin-proteasome system</subject><subject>Ubiquitin-protein ligase</subject><subject>Ubiquitin-Protein Ligases - metabolism</subject><subject>Ubiquitination</subject><subject>Ubiquitins - metabolism</subject><subject>Viral infections</subject><issn>1553-7374</issn><issn>1553-7366</issn><issn>1553-7374</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2022</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>BENPR</sourceid><sourceid>D8T</sourceid><sourceid>DOA</sourceid><recordid>eNqVUk1v1DAUjBCItgv_AEGknjjs4q_YyQWpqgqsVEAq5Ww59sviJRuntrPQf4-3SatGggOyLD89z4w9o5dlrzBaYSrwu60bfKfaVd-ruMIII8Hok-wYFwVdCirY00f1UXYSwhYhhinmz7MjyhEXhPLjTF20g7ZGReu63DX59dX6MynyobY3g422Gy-i8huIIbfd3rV7MKnIjd2DD5BraNuhVT5XnUk72r31qs177zSEAOFF9qxRbYCX07nIvn-4uD7_tLz8-nF9fna51Lyq4rJACkzBcQOUVhpXSDGmS14ZXhOtNSNEG6JFySircbKKqELJGjG8AYIFpYvszajbty7IKZ0giSAFOWRwQKxHhHFqK3tvd8rfSqesvGs4v5HKR6tbkArjmiGjKS6BaUxrBphDybkSChDopLUctcIv6Id6pja1fqYKJCswunv7_fS7od6B0dDFlNKMNr_p7A-5cXtZsRLjkiSB00nAu5sBQvyHxQm1UcmF7RqXxPTOBi3PBEGFKGhKbZGt_oJKy8DOatdBY1N_Rng7IyRMhN9xo4YQ5Prb1X9gv8yxbMRq70Lw0DwEgpE8TPm9SXmYcjlNeaK9fhzmA-l-rOkfrt75Ig</recordid><startdate>20220901</startdate><enddate>20220901</enddate><creator>Yang, Emily</creator><creator>Huang, Serina</creator><creator>Jami-Alahmadi, Yasaman</creator><creator>McInerney, Gerald M</creator><creator>Wohlschlegel, James A</creator><creator>Li, Melody M H</creator><general>Public Library of Science</general><general>Public Library of Science (PLoS)</general><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>ISN</scope><scope>ISR</scope><scope>3V.</scope><scope>7QL</scope><scope>7U9</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>COVID</scope><scope>DWQXO</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M7P</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>5PM</scope><scope>ADTPV</scope><scope>AOWAS</scope><scope>D8T</scope><scope>ZZAVC</scope><scope>DOA</scope><orcidid>https://orcid.org/0000-0002-6905-7940</orcidid></search><sort><creationdate>20220901</creationdate><title>Elucidation of TRIM25 ubiquitination targets involved in diverse cellular and antiviral processes</title><author>Yang, Emily ; Huang, Serina ; Jami-Alahmadi, Yasaman ; McInerney, Gerald M ; Wohlschlegel, James A ; Li, Melody M H</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c699t-50aed561fe339c190a44c869d6b2ccc422cd2c78434b174303a07372d6fe21733</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2022</creationdate><topic>Antiviral activity</topic><topic>Antiviral Agents - metabolism</topic><topic>Antiviral drugs</topic><topic>Biological activity</topic><topic>Biology and Life Sciences</topic><topic>Carcinogenesis</topic><topic>Carcinogens</topic><topic>Catalytic activity</topic><topic>Cellular proteins</topic><topic>DNA Helicases - metabolism</topic><topic>Enzymes</topic><topic>Experiments</topic><topic>Health aspects</topic><topic>Infections</topic><topic>Innate immunity</topic><topic>Interferon</topic><topic>Interferons - metabolism</topic><topic>Kinases</topic><topic>Ligases</topic><topic>mRNA stability</topic><topic>mRNA turnover</topic><topic>Mutation</topic><topic>Nonsense-mediated mRNA decay</topic><topic>Nucleosides - metabolism</topic><topic>Poly-ADP-Ribose Binding Proteins - metabolism</topic><topic>Proteins</topic><topic>Research and Analysis Methods</topic><topic>RNA Helicases - metabolism</topic><topic>RNA Recognition Motif Proteins - metabolism</topic><topic>Substrates</topic><topic>Transcription</topic><topic>Tripartite Motif Proteins - genetics</topic><topic>Tripartite Motif Proteins - metabolism</topic><topic>Ubiquitin</topic><topic>Ubiquitin-proteasome system</topic><topic>Ubiquitin-protein ligase</topic><topic>Ubiquitin-Protein Ligases - metabolism</topic><topic>Ubiquitination</topic><topic>Ubiquitins - metabolism</topic><topic>Viral infections</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Yang, Emily</creatorcontrib><creatorcontrib>Huang, Serina</creatorcontrib><creatorcontrib>Jami-Alahmadi, Yasaman</creatorcontrib><creatorcontrib>McInerney, Gerald M</creatorcontrib><creatorcontrib>Wohlschlegel, James A</creatorcontrib><creatorcontrib>Li, Melody M H</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Gale In Context: Canada</collection><collection>Gale In Context: Science</collection><collection>ProQuest Central (Corporate)</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Virology and AIDS Abstracts</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Medical Database (Alumni Edition)</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>ProQuest Central (Alumni Edition)</collection><collection>ProQuest One Sustainability</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>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>Coronavirus Research Database</collection><collection>ProQuest Central Korea</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</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>Biological Science Database</collection><collection>Publicly Available Content 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 China</collection><collection>PubMed Central (Full Participant titles)</collection><collection>SwePub</collection><collection>SwePub Articles</collection><collection>SWEPUB Freely available online</collection><collection>SwePub Articles full text</collection><collection>DOAJ Directory of Open Access Journals</collection><jtitle>PLOS PATHOGENS</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Yang, Emily</au><au>Huang, Serina</au><au>Jami-Alahmadi, Yasaman</au><au>McInerney, Gerald M</au><au>Wohlschlegel, James A</au><au>Li, Melody M H</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Elucidation of TRIM25 ubiquitination targets involved in diverse cellular and antiviral processes</atitle><jtitle>PLOS PATHOGENS</jtitle><addtitle>PLoS Pathog</addtitle><date>2022-09-01</date><risdate>2022</risdate><volume>18</volume><issue>9</issue><spage>e1010743</spage><pages>e1010743-</pages><issn>1553-7374</issn><issn>1553-7366</issn><eissn>1553-7374</eissn><abstract>The tripartite motif (TRIM) family of E3 ubiquitin ligases is well known for its roles in antiviral restriction and innate immunity regulation, in addition to many other cellular pathways. In particular, TRIM25-mediated ubiquitination affects both carcinogenesis and antiviral response. While individual substrates have been identified for TRIM25, it remains unclear how it regulates diverse processes. Here we characterized a mutation, R54P, critical for TRIM25 catalytic activity, which we successfully utilized to "trap" substrates. We demonstrated that TRIM25 targets proteins implicated in stress granule formation (G3BP1/2), nonsense-mediated mRNA decay (UPF1), nucleoside synthesis (NME1), and mRNA translation and stability (PABPC4). The R54P mutation abolishes TRIM25 inhibition of alphaviruses independently of the host interferon response, suggesting that this antiviral effect is a direct consequence of ubiquitination. Consistent with that, we observed diminished antiviral activity upon knockdown of several TRIM25-R54P specific interactors including NME1 and PABPC4. Our findings highlight that multiple substrates mediate the cellular and antiviral activities of TRIM25, illustrating the multi-faceted role of this ubiquitination network in modulating diverse biological processes.</abstract><cop>United States</cop><pub>Public Library of Science</pub><pmid>36067236</pmid><doi>10.1371/journal.ppat.1010743</doi><tpages>e1010743</tpages><orcidid>https://orcid.org/0000-0002-6905-7940</orcidid><oa>free_for_read</oa></addata></record> |
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| subjects | Antiviral activity Antiviral Agents - metabolism Antiviral drugs Biological activity Biology and Life Sciences Carcinogenesis Carcinogens Catalytic activity Cellular proteins DNA Helicases - metabolism Enzymes Experiments Health aspects Infections Innate immunity Interferon Interferons - metabolism Kinases Ligases mRNA stability mRNA turnover Mutation Nonsense-mediated mRNA decay Nucleosides - metabolism Poly-ADP-Ribose Binding Proteins - metabolism Proteins Research and Analysis Methods RNA Helicases - metabolism RNA Recognition Motif Proteins - metabolism Substrates Transcription Tripartite Motif Proteins - genetics Tripartite Motif Proteins - metabolism Ubiquitin Ubiquitin-proteasome system Ubiquitin-protein ligase Ubiquitin-Protein Ligases - metabolism Ubiquitination Ubiquitins - metabolism Viral infections |
| title | Elucidation of TRIM25 ubiquitination targets involved in diverse cellular and antiviral processes |
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