TRIM30α Is a Negative-Feedback Regulator of the Intracellular DNA and DNA Virus-Triggered Response by Targeting STING

Uncontrolled immune responses to intracellular DNA have been shown to induce autoimmune diseases. Homeostasis regulation of immune responses to cytosolic DNA is critical for limiting the risk of autoimmunity and survival of the host. Here, we report that the E3 ubiquitin ligase tripartite motif prot...

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Published in	PLoS pathogens Vol. 11; no. 6; p. e1005012
Main Authors	Wang, Yanming, Lian, Qiaoshi, Yang, Bo, Yan, Shanshan, Zhou, Haiyan, He, Lan, Lin, Guomei, Lian, Zhexiong, Jiang, Zhengfan, Sun, Bing
Format	Journal Article
Language	English
Published	United States Public Library of Science 01.06.2015 Public Library of Science (PLoS)
Subjects	Animals Cell Line DNA - metabolism DNA Viruses - genetics DNA Viruses - metabolism DNA-Binding Proteins - metabolism Immunity, Innate Membrane Proteins - metabolism Mice, Inbred C57BL Signal Transduction - immunology Transcription Factors - metabolism Ubiquitin-Protein Ligases - metabolism Ubiquitination
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Abstract	Uncontrolled immune responses to intracellular DNA have been shown to induce autoimmune diseases. Homeostasis regulation of immune responses to cytosolic DNA is critical for limiting the risk of autoimmunity and survival of the host. Here, we report that the E3 ubiquitin ligase tripartite motif protein 30α (TRIM30α) was induced by herpes simplex virus type 1 (HSV-1) infection in dendritic cells (DCs). Knockdown or genetic ablation of TRIM30α augmented the type I IFNs and interleukin-6 response to intracellular DNA and DNA viruses. Trim30α-deficient mice were more resistant to infection by DNA viruses. Biochemical analyses showed that TRIM30α interacted with the stimulator of interferon genes (STING), which is a critical regulator of the DNA-sensing response. Overexpression of TRIM30α promoted the degradation of STING via K48-linked ubiquitination at Lys275 through a proteasome-dependent pathway. These findings indicate that E3 ligase TRIM30α is an important negative-feedback regulator of innate immune responses to DNA viruses by targeting STING.
AbstractList	Uncontrolled immune responses to intracellular DNA have been shown to induce autoimmune diseases. Homeostasis regulation of immune responses to cytosolic DNA is critical for limiting the risk of autoimmunity and survival of the host. Here, we report that the E3 ubiquitin ligase tripartite motif protein 30α (TRIM30α) was induced by herpes simplex virus type 1 (HSV-1) infection in dendritic cells (DCs). Knockdown or genetic ablation of TRIM30α augmented the type I IFNs and interleukin-6 response to intracellular DNA and DNA viruses. Trim30α-deficient mice were more resistant to infection by DNA viruses. Biochemical analyses showed that TRIM30α interacted with the stimulator of interferon genes (STING), which is a critical regulator of the DNA-sensing response. Overexpression of TRIM30α promoted the degradation of STING via K48-linked ubiquitination at Lys275 through a proteasome-dependent pathway. These findings indicate that E3 ligase TRIM30α is an important negative-feedback regulator of innate immune responses to DNA viruses by targeting STING. Uncontrolled immune responses to intracellular DNA have been shown to induce autoimmune diseases. Homeostasis regulation of immune responses to cytosolic DNA is critical for limiting the risk of autoimmunity and survival of the host. Here, we report that the E3 ubiquitin ligase tripartite motif protein 30α (TRIM30α) was induced by herpes simplex virus type 1 (HSV-1) infection in dendritic cells (DCs). Knockdown or genetic ablation of TRIM30α augmented the type I IFNs and interleukin-6 response to intracellular DNA and DNA viruses. Trim30α-deficient mice were more resistant to infection by DNA viruses. Biochemical analyses showed that TRIM30α interacted with the stimulator of interferon genes (STING), which is a critical regulator of the DNA-sensing response. Overexpression of TRIM30α promoted the degradation of STING via K48-linked ubiquitination at Lys275 through a proteasome-dependent pathway. These findings indicate that E3 ligase TRIM30α is an important negative-feedback regulator of innate immune responses to DNA viruses by targeting STING.Uncontrolled immune responses to intracellular DNA have been shown to induce autoimmune diseases. Homeostasis regulation of immune responses to cytosolic DNA is critical for limiting the risk of autoimmunity and survival of the host. Here, we report that the E3 ubiquitin ligase tripartite motif protein 30α (TRIM30α) was induced by herpes simplex virus type 1 (HSV-1) infection in dendritic cells (DCs). Knockdown or genetic ablation of TRIM30α augmented the type I IFNs and interleukin-6 response to intracellular DNA and DNA viruses. Trim30α-deficient mice were more resistant to infection by DNA viruses. Biochemical analyses showed that TRIM30α interacted with the stimulator of interferon genes (STING), which is a critical regulator of the DNA-sensing response. Overexpression of TRIM30α promoted the degradation of STING via K48-linked ubiquitination at Lys275 through a proteasome-dependent pathway. These findings indicate that E3 ligase TRIM30α is an important negative-feedback regulator of innate immune responses to DNA viruses by targeting STING. Uncontrolled immune responses to intracellular DNA have been shown to induce autoimmune diseases. Homeostasis regulation of immune responses to cytosolic DNA is critical for limiting the risk of autoimmunity and survival of the host. Here, we report that the E3 ubiquitin ligase tripartite motif protein 30α (TRIM30α) was induced by herpes simplex virus type 1 (HSV-1) infection in dendritic cells (DCs). Knockdown or genetic ablation of TRIM30α augmented the type I IFNs and interleukin-6 response to intracellular DNA and DNA viruses. Trim30α -deficient mice were more resistant to infection by DNA viruses. Biochemical analyses showed that TRIM30α interacted with the stimulator of interferon genes (STING), which is a critical regulator of the DNA-sensing response. Overexpression of TRIM30α promoted the degradation of STING via K48-linked ubiquitination at Lys275 through a proteasome-dependent pathway. These findings indicate that E3 ligase TRIM30α is an important negative-feedback regulator of innate immune responses to DNA viruses by targeting STING. Negative-feedback regulation is a broad and pivotal biological event to maintain the homeostasis of the host. Viral DNA species derived from DNA viruses or retroviruses can activate STING signaling to produce pro-inflammatory cytokines and type I interferon, which further recruit immune cells or induce interferon stimulated genes (ISGs) to clear viral infection respectively. However, excessive STING-signaling activation has been shown to induce autoimmune disorders. Thus, it is important to finely turn off STING signaling. Here we demonstrate that TRIM30α is rapidly induced followed by STING activation. Trim30α -deficient mice show more resistance to infection by DNA viruses. Meanwhile, knockdown or genetic ablation of TRIM30α augments the type I IFNs and IL-6 responses to intracellular DNA and DNA viruses. Biochemical analyses show that TRIM30α interacts with STING and promotes the degradation of STING via K48-linked ubiquitination at Lys275. These findings demonstrate that induced TRIM30α is a negative-feedback regulator of STING pathway activation triggered by DNA and DNA viruses, which helps the host to avoid excessive response and maintain homeostasis.
Author	Lin, Guomei Lian, Zhexiong Lian, Qiaoshi Zhou, Haiyan Wang, Yanming Yang, Bo Jiang, Zhengfan Yan, Shanshan He, Lan Sun, Bing
AuthorAffiliation	University of California Berkeley, UNITED STATES 1 Institute of Biochemistry and Cell Biology, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, Shanghai, China 2 School of Life Sciences, University of Science and Technology of China, Hefei, China 4 Key Laboratory of Molecular Virology & Immunology, Institute Pasteur of Shanghai, Chinese Academy of Sciences, Shanghai, China 3 State Key Laboratory of Protein and Plant Gene Research, Key Laboratory of Cell Proliferation and Differentiation of the Ministry of Education, School of Life Sciences, Peking University, Beijing, China; Peking University-Tsinghua University Joint Center for Life Sciences, Beijing, China
AuthorAffiliation_xml	– name: 2 School of Life Sciences, University of Science and Technology of China, Hefei, China – name: 4 Key Laboratory of Molecular Virology & Immunology, Institute Pasteur of Shanghai, Chinese Academy of Sciences, Shanghai, China – name: 3 State Key Laboratory of Protein and Plant Gene Research, Key Laboratory of Cell Proliferation and Differentiation of the Ministry of Education, School of Life Sciences, Peking University, Beijing, China; Peking University-Tsinghua University Joint Center for Life Sciences, Beijing, China – name: University of California Berkeley, UNITED STATES – name: 1 Institute of Biochemistry and Cell Biology, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, Shanghai, China
Author_xml	– sequence: 1 givenname: Yanming surname: Wang fullname: Wang, Yanming – sequence: 2 givenname: Qiaoshi surname: Lian fullname: Lian, Qiaoshi – sequence: 3 givenname: Bo surname: Yang fullname: Yang, Bo – sequence: 4 givenname: Shanshan surname: Yan fullname: Yan, Shanshan – sequence: 5 givenname: Haiyan surname: Zhou fullname: Zhou, Haiyan – sequence: 6 givenname: Lan surname: He fullname: He, Lan – sequence: 7 givenname: Guomei surname: Lin fullname: Lin, Guomei – sequence: 8 givenname: Zhexiong surname: Lian fullname: Lian, Zhexiong – sequence: 9 givenname: Zhengfan surname: Jiang fullname: Jiang, Zhengfan – sequence: 10 givenname: Bing surname: Sun fullname: Sun, Bing
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Cites_doi	10.1016/j.immuni.2009.01.008 10.1038/nature06013 10.1126/science.1232458 10.4049/jimmunol.175.5.2851 10.1038/nri2413 10.1038/nature08476 10.1038/ni1577 10.4049/jimmunol.1202507 10.1038/35099560 10.1038/ni.2492 10.1126/science.1093620 10.1016/j.cell.2008.06.032 10.1038/ni.2491 10.1016/j.immuni.2013.05.004 10.1016/j.it.2013.10.010 10.1038/ni.1932 10.1038/ni1087 10.4049/jimmunol.1001099 10.1038/ni.1702 10.1126/science.1229963 10.1073/pnas.0900850106 10.1038/ni.2091 10.4049/jimmunol.170.4.1728 10.1038/nature07725 10.1016/j.cell.2009.06.015 10.1038/ni.1864 10.1038/ni.1779 10.1038/nature07317 10.1038/35047123 10.1016/j.cell.2010.01.022 10.1016/j.cell.2013.09.049
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Notes	ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 Conceived and designed the experiments: BS YW QL BY ZL ZJ. Performed the experiments: YW QL BY SY HZ LH GL. Analyzed the data: YW QL BY. Contributed reagents/materials/analysis tools: ZJ. Wrote the paper: YW QL. The authors have declared that no competing interests exist.
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References	O Takeuchi (ref1) 2010; 140 H Ishikawa (ref25) 2009; 461 V Hornung (ref9) 2009; 458 Y-H Chiu (ref12) 2009; 138 M Yoneyama (ref5) 2005; 175 VAK Rathinam (ref10) 2010; 11 M Shi (ref22) 2008; 9 M Yoneyama (ref4) 2004; 5 A Ablasser (ref11) 2009; 10 L Zhang (ref21) 2014 J Wu (ref30) 2013; 339 Y Hu (ref23) 2010; 185 DB Stetson (ref17) 2008; 134 DL Burdette (ref27) 2012; 14 K Ozato (ref28) 2008; 8 Z Zhang (ref18) 2013; 14 W Sun (ref26) 2009; 106 L Sun (ref15) 2013; 339 L Unterholzner (ref16) 2010; 11 L Alexopoulou (ref2) 2001; 413 H Hemmi (ref7) 2000; 408 B Zhong (ref19) 2009; 30 Z Zhang (ref14) 2011; 12 R Paludan Søren (ref6) 2013; 38 T Burckstummer (ref8) 2009; 10 H Konno (ref20) 2013; 155 H Ishikawa (ref24) 2008; 455 F Heil (ref3) 2004; 303 A Takaoka (ref13) 2007; 448 B Yang (ref31) 2013; 190 W Hou (ref32) 2003; 170 GN Barber (ref29) 2014; 35
References_xml	– volume: 30 start-page: 397 year: 2009 ident: ref19 article-title: The Ubiquitin Ligase RNF5 Regulates Antiviral Responses by Mediating Degradation of the Adaptor Protein MITA publication-title: Immunity doi: 10.1016/j.immuni.2009.01.008 – volume: 448 start-page: 501 year: 2007 ident: ref13 article-title: DAI (DLM-1/ZBP1) is a cytosolic DNA sensor and an activator of innate immune response publication-title: Nature doi: 10.1038/nature06013 – volume: 339 start-page: 786 year: 2013 ident: ref15 article-title: Cyclic GMP-AMP synthase is a cytosolic DNA sensor that activates the type I interferon pathway publication-title: Science doi: 10.1126/science.1232458 – volume: 175 start-page: 2851 year: 2005 ident: ref5 article-title: Shared and unique functions of the DExD/H-box helicases RIG-I, MDA5, and LGP2 in antiviral innate immunity publication-title: Journal of Immunology doi: 10.4049/jimmunol.175.5.2851 – volume: 8 start-page: 849 year: 2008 ident: ref28 article-title: TRIM family proteins and their emerging roles in innate immunity publication-title: Nature Reviews Immunology doi: 10.1038/nri2413 – volume: 461 start-page: 788 year: 2009 ident: ref25 article-title: STING regulates intracellular DNA-mediated, type I interferon-dependent innate immunity publication-title: Nature doi: 10.1038/nature08476 – volume: 9 start-page: 369 year: 2008 ident: ref22 article-title: TRIM30 alpha negatively regulates TLR-mediated NF-kappa B activation by targeting TAB2 and TAB3 for degradation publication-title: Nat Immunol doi: 10.1038/ni1577 – volume: 190 start-page: 3613 year: 2013 ident: ref31 article-title: Novel Function of Trim44 Promotes an Antiviral Response by Stabilizing VISA publication-title: The Journal of Immunology doi: 10.4049/jimmunol.1202507 – volume: 413 start-page: 732 year: 2001 ident: ref2 article-title: Recognition of double-stranded RNA and activation of NF-kappa B by Toll-like receptor 3 publication-title: Nature doi: 10.1038/35099560 – volume: 14 start-page: 172 year: 2013 ident: ref18 article-title: The E3 ubiquitin ligase TRIM21 negatively regulates the innate immune response to intracellular double-stranded DNA publication-title: Nat Immunol doi: 10.1038/ni.2492 – volume: 303 start-page: 1526 year: 2004 ident: ref3 article-title: Species-specific recognition of single-stranded RNA via toll-like receptor 7 and 8 publication-title: Science doi: 10.1126/science.1093620 – volume: 134 start-page: 587 year: 2008 ident: ref17 article-title: Trex1 Prevents Cell-Intrinsic Initiation of Autoimmunity publication-title: Cell doi: 10.1016/j.cell.2008.06.032 – volume: 14 start-page: 19 year: 2012 ident: ref27 article-title: STING and the innate immune response to nucleic acids in the cytosol publication-title: Nature Immunology doi: 10.1038/ni.2491 – volume: 38 start-page: 870 year: 2013 ident: ref6 article-title: Immune Sensing of DNA publication-title: Immunity doi: 10.1016/j.immuni.2013.05.004 – volume: 35 start-page: 88 year: 2014 ident: ref29 article-title: STING-dependent cytosolic DNA sensing pathways publication-title: Trends Immunol doi: 10.1016/j.it.2013.10.010 – volume: 11 start-page: 997 year: 2010 ident: ref16 article-title: IFI16 is an innate immune sensor for intracellular DNA publication-title: Nature Immunology doi: 10.1038/ni.1932 – volume: 5 start-page: 730 year: 2004 ident: ref4 article-title: The RNA helicase RIG-I has an essential function in double-stranded RNA-induced innate antiviral responses publication-title: Nature Immunology doi: 10.1038/ni1087 – volume: 185 start-page: 7699 year: 2010 ident: ref23 article-title: Tripartite-motif protein 30 negatively regulates NLRP3 inflammasome activation by modulating reactive oxygen species production publication-title: J Immunol doi: 10.4049/jimmunol.1001099 – volume: 10 start-page: 266 year: 2009 ident: ref8 article-title: An orthogonal proteomic-genomic screen identifies AIM2 as a cytoplasmic DNA sensor for the inflammasome publication-title: Nature Immunology doi: 10.1038/ni.1702 – volume: 339 start-page: 826 year: 2013 ident: ref30 article-title: Cyclic GMP-AMP is an endogenous second messenger in innate immune signaling by cytosolic DNA publication-title: Science doi: 10.1126/science.1229963 – year: 2014 ident: ref21 article-title: NLRC3, a Member of the NLR Family of Proteins, Is a Negative Regulator of Innate Immune Signaling Induced by the DNA Sensor STING publication-title: Immunity – volume: 106 start-page: 8653 year: 2009 ident: ref26 article-title: ERIS, an endoplasmic reticulum IFN stimulator, activates innate immune signaling through dimerization publication-title: Proc Natl Acad Sci U S A doi: 10.1073/pnas.0900850106 – volume: 12 start-page: 959 year: 2011 ident: ref14 article-title: The helicase DDX41 senses intracellular DNA mediated by the adaptor STING in dendritic cells publication-title: Nat Immunol doi: 10.1038/ni.2091 – volume: 170 start-page: 1728 year: 2003 ident: ref32 article-title: Pertussis toxin enhances Th1 responses by stimulation of dendritic cells publication-title: J Immunol doi: 10.4049/jimmunol.170.4.1728 – volume: 458 start-page: 514 year: 2009 ident: ref9 article-title: AIM2 recognizes cytosolic dsDNA and forms a caspase-1-activating inflammasome with ASC publication-title: Nature doi: 10.1038/nature07725 – volume: 138 start-page: 576 year: 2009 ident: ref12 article-title: RNA Polymerase III Detects Cytosolic DNA and Induces Type I Interferons through the RIG-I Pathway publication-title: Cell doi: 10.1016/j.cell.2009.06.015 – volume: 11 start-page: 395 year: 2010 ident: ref10 article-title: The AIM2 inflammasome is essential for host defense against cytosolic bacteria and DNA viruses publication-title: Nature Immunology doi: 10.1038/ni.1864 – volume: 10 start-page: 1065 year: 2009 ident: ref11 article-title: RIG-I-dependent sensing of poly(dA:dT) through the induction of an RNA polymerase III—transcribed RNA intermediate publication-title: Nature Immunology doi: 10.1038/ni.1779 – volume: 455 start-page: 674 year: 2008 ident: ref24 article-title: STING is an endoplasmic reticulum adaptor that facilitates innate immune signalling publication-title: Nature doi: 10.1038/nature07317 – volume: 408 start-page: 740 year: 2000 ident: ref7 article-title: A Toll-like receptor recognizes bacterial DNA publication-title: Nature doi: 10.1038/35047123 – volume: 140 start-page: 805 year: 2010 ident: ref1 article-title: Pattern Recognition Receptors and Inflammation publication-title: Cell doi: 10.1016/j.cell.2010.01.022 – volume: 155 start-page: 688 year: 2013 ident: ref20 article-title: Cyclic dinucleotides trigger ULK1 (ATG1) phosphorylation of STING to prevent sustained innate immune signaling publication-title: Cell doi: 10.1016/j.cell.2013.09.049
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Snippet	Uncontrolled immune responses to intracellular DNA have been shown to induce autoimmune diseases. Homeostasis regulation of immune responses to cytosolic DNA...
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SubjectTerms	Animals Cell Line DNA - metabolism DNA Viruses - genetics DNA Viruses - metabolism DNA-Binding Proteins - metabolism Immunity, Innate Membrane Proteins - metabolism Mice, Inbred C57BL Signal Transduction - immunology Transcription Factors - metabolism Ubiquitin-Protein Ligases - metabolism Ubiquitination
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Title	TRIM30α Is a Negative-Feedback Regulator of the Intracellular DNA and DNA Virus-Triggered Response by Targeting STING
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