Identification of Tyrosine-9 of MAVS as Critical Target for Inducible Phosphorylation That Determines Activation
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{"title"=>"Identification of tyrosine-9 of MAVS as critical target for inducible phosphorylation that determines activation", "type"=>"journal", "authors"=>[{"first_name"=>"Chaoyang", "last_name"=>"Wen", "scopus_author_id"=>"7201367127"}, {"first_name"=>"Zhifeng", "last_name"=>"Yan", "scopus_author_id"=>"35996022000"}, {"first_name"=>"Xiaoli", "last_name"=>"Yang", "scopus_author_id"=>"56651227500"}, {"first_name"=>"Kai", "last_name"=>"Guan", "scopus_author_id"=>"35174688900"}, {"first_name"=>"Changzhi", "last_name"=>"Xu", "scopus_author_id"=>"55332330900"}, {"first_name"=>"Ting", "last_name"=>"Song", "scopus_author_id"=>"35764832500"}, {"first_name"=>"Zirui", "last_name"=>"Zheng", "scopus_author_id"=>"35175433900"}, {"first_name"=>"Wenjun", "last_name"=>"Wang", "scopus_author_id"=>"57192619544"}, {"first_name"=>"Ying", "last_name"=>"Wang", "scopus_author_id"=>"56757773500"}, {"first_name"=>"Man", "last_name"=>"Zhao", "scopus_author_id"=>"57198160724"}, {"first_name"=>"Yanhong", "last_name"=>"Zhang", "scopus_author_id"=>"56289319700"}, {"first_name"=>"Tao", "last_name"=>"Xu", "scopus_author_id"=>"57199173741"}, {"first_name"=>"Jianping", "last_name"=>"Dou", "scopus_author_id"=>"57197267457"}, {"first_name"=>"Jingmei", "last_name"=>"Liu", "scopus_author_id"=>"55332471200"}, {"first_name"=>"Quanbin", "last_name"=>"Xu", "scopus_author_id"=>"26654561600"}, {"first_name"=>"Xiang", "last_name"=>"He", "scopus_author_id"=>"23097465500"}, {"first_name"=>"Congwen", "last_name"=>"Wei", "scopus_author_id"=>"25959768700"}, {"first_name"=>"Hui", "last_name"=>"Zhong", "scopus_author_id"=>"35244129000"}], "year"=>2012, "source"=>"PLoS ONE", "identifiers"=>{"sgr"=>"84864829089", "pmid"=>"22844514", "doi"=>"10.1371/journal.pone.0041687", "pui"=>"365407224", "isbn"=>"1932-6203 (Electronic)\\n1932-6203 (Linking)", "issn"=>"19326203", "scopus"=>"2-s2.0-84864829089"}, "id"=>"d9e608db-cd46-347b-b57c-1040a79a54d4", "abstract"=>"BACKGROUND: Innate immunity to viruses involves receptors such as RIG-I, which senses viral RNA and triggers an IFN-beta signaling pathway involving the outer mitochondrial membrane protein MAVS. However, the functional status of MAVS phosphorylation remains elusive. METHODOLOGY/PRINCIPAL FINDINGS: Here we demonstrate for the first time that MAVS undergoes extensive tyrosine phosphorylation upon viral infection, indicating that MAVS phosphorylation might play an important role in MAVS function. A tyrosine-scanning mutational analysis revealed that MAVS tyrosine-9 (Y9) is a phosphorylation site that is required for IFN-beta signaling. Indeed, MAVS Y9F mutation severely impaired TRAF3/TRAF6 recruitment and displayed decreased tyrosine phosphorylation in response to VSV infection compared to wild type MAVS. Functionally, MAVS Y9 phosphorylation contributed to MAVS antiviral function without interfering with its apoptosis property. CONCLUSIONS/SIGNIFICANCE: These experiments identify a novel residue of MAVS that is crucially involved in the recruitment of TRAF3/TRAF6 and in downstream propagation of MAVS signaling.", "link"=>"http://www.mendeley.com/research/identification-tyrosine9-mavs-critical-target-inducible-phosphorylation-determines-activation", "reader_count"=>23, "reader_count_by_academic_status"=>{"Unspecified"=>1, "Researcher"=>6, "Student > Ph. D. Student"=>8, "Student > Master"=>3, "Student > Bachelor"=>3, "Lecturer"=>1, "Professor"=>1}, "reader_count_by_user_role"=>{"Unspecified"=>1, "Researcher"=>6, "Student > Ph. D. Student"=>8, "Student > Master"=>3, "Student > Bachelor"=>3, "Lecturer"=>1, "Professor"=>1}, "reader_count_by_subject_area"=>{"Unspecified"=>1, "Biochemistry, Genetics and Molecular Biology"=>3, "Agricultural and Biological Sciences"=>15, "Medicine and Dentistry"=>1, "Neuroscience"=>1, "Chemistry"=>1, "Immunology and Microbiology"=>1}, "reader_count_by_subdiscipline"=>{"Medicine and Dentistry"=>{"Medicine and Dentistry"=>1}, "Neuroscience"=>{"Neuroscience"=>1}, "Chemistry"=>{"Chemistry"=>1}, "Immunology and Microbiology"=>{"Immunology and Microbiology"=>1}, "Agricultural and Biological Sciences"=>{"Agricultural and Biological Sciences"=>15}, "Biochemistry, Genetics and Molecular Biology"=>{"Biochemistry, Genetics and Molecular Biology"=>3}, "Unspecified"=>{"Unspecified"=>1}}, "reader_count_by_country"=>{"United States"=>1}, "group_count"=>1}

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Figshare

  • {"files"=>["https://ndownloader.figshare.com/files/602860"], "description"=>"<p>(A–B) HEK293T cells were infected with VSV at a multiplicity of infection (MOI) of 0.002 for the indicated times (A) or at a different MOI for 30 min (B). Anti-MAVS immunoprecipitates were analyzed by immunoblotting with anti-P-Tyr or anti-MAVS antibody. (C–D) MCF-7 (C) or HepG2 (D) cells were infected with VSV at a MOI of 0.002 for the indicated times. Anti-MAVS immunoprecipitates were analyzed by immunoblotting with anti-P-Tyr or anti-MAVS antibody.</p>", "links"=>[], "tags"=>["undergoes", "tyrosine", "phosphorylation"], "article_id"=>273319, "categories"=>["Biological Sciences", "Biochemistry", "Immunology"], "users"=>["Chaoyang Wen", "Zhifeng Yan", "Xiaoli Yang", "Kai Guan", "Changzhi Xu", "Ting Song", "Zirui Zheng", "Wenjun Wang", "Ying Wang", "Man Zhao", "Yanhong Zhang", "Tao Xu", "Jianping Dou", "Jingmei Liu", "Quanbin Xu", "Xiang He", "Congwen Wei", "Hui Zhong"], "doi"=>["https://dx.doi.org/10.1371/journal.pone.0041687.g001"], "stats"=>{"downloads"=>0, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_MAVS_undergoes_tyrosine_phosphorylation_in_response_to_virus_infection_/273319", "title"=>"MAVS undergoes tyrosine phosphorylation in response to virus infection.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-02-20 01:52:47"}
  • {"files"=>["https://ndownloader.figshare.com/files/602981"], "description"=>"<p>(A) Expression of wild-type (WT) and mutant MAVS proteins was assessed by Western-blotting in HEK293T cells. (B–C) HEK293T cells (B) or MCF-7 cells (C) were transfected with expression vector encoding Flag-MAVS WT or Flag-MAVS mutants together with IFN-β-LUC or NF-κB-LUC. The LUC activity was measured 24 h later and normalized for transfection efficiency. Results are expressed as fold-increases of luciferase levels relatively to Flag-vector transfected cells. (D) HEK293T cells were transfected with a vector encoding Flag-MAVS or Flag-MAVS mutants and endogenous IFN-β mRNA expression was analyzed by qRTPCR. Results were expressed as fold-increase of IFN-β mRNA level normalized with β-actin level and relatively to Y9F MAVS-transfected cells. (E) Using the supernatants collected from the samples shown in panel B, IL6 release was measured by ELISA. From B to E, Data are mean of three independent experiments ± SEM done in triplicate.(F) HEK293T cells were transfected with expression vector encoding Flag-MAVS WT (WT) or Flag-MAVS Y9F mutant (Y9F). Whole cell lysates were analyzed by immunoblotting with anti-IRF3, anti-p-IRF3 or anti-Flag antibody, anti-Tubulin was used as equal loading control. (G) EMSA was performed using <sup>32</sup>P-labeled consensus NF-κB probe and nuclear proteins extracted from HEK293T cells transfected with Flag-MAVS WT (WT) or Flag-MAVS Y9F mutant (Y9F).</p>", "links"=>[], "tags"=>["y9f", "impairs", "mavs-mediated", "innate"], "article_id"=>273462, "categories"=>["Biological Sciences", "Biochemistry", "Immunology"], "users"=>["Chaoyang Wen", "Zhifeng Yan", "Xiaoli Yang", "Kai Guan", "Changzhi Xu", "Ting Song", "Zirui Zheng", "Wenjun Wang", "Ying Wang", "Man Zhao", "Yanhong Zhang", "Tao Xu", "Jianping Dou", "Jingmei Liu", "Quanbin Xu", "Xiang He", "Congwen Wei", "Hui Zhong"], "doi"=>["https://dx.doi.org/10.1371/journal.pone.0041687.g002"], "stats"=>{"downloads"=>0, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_MAVS_Y9F_impairs_MAVS_mediated_innate_immune_signaling_/273462", "title"=>"MAVS Y9F impairs MAVS-mediated innate immune signaling.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-02-20 01:53:38"}
  • {"files"=>["https://ndownloader.figshare.com/files/603128"], "description"=>"<p>(A) Hela cells were transfected with expression vector encoding Flag-MAVS WT (WT) or Flag-MAVS Y9F mutant (Y9F), cells were then stained with anti-Flag antibody and imaged by confocal microscopy. The mitochondria were stained with Mito Tracker. The yellow staining in the overlay image indicates co-localization of MAVS and Mito Tracker. (B) HEK293T cells were transfected with expression vector encoding Flag-MAVS (WT) or Flag-MAVS Y9F mutant (Y9F), mitochondria, cytoplasm and nucleus fractions were analyzed by immunoblotting with anti-Flag, anti-HSP60, anti-Lamin B and anti-Tubulin antibodies. (C–E and G) HEK293T cells were cotransfected with Flag-WT or Flag-Y9F together with Myc-tagged RIG-I 2Card (E) or Myc-tagged STING (G). After 48 h, cell lysates were immunoprecipitated with anti-Flag antibody, followed by immunoblotting with anti-Flag, anti-TRAF3 (C), anti-TRAF6 (D) and anti-Myc antibodies. (F) HEK293T cells were cotransfected with Flag-WT or Y9F and Myc-WT or Y9F. After 48 h, cell lysates were immunoprecipitated with anti-Flag antibody, followed by immunoblotting with anti-Flag (lower panel) and anti-Myc (upper panel) antibodies. From C–G, Each blot is a representative example of at least three independent experiments with similar results. Numbers below certain Western blots indicate relative levels determined by software-based quantitation of the representative experiment shown.</p>", "links"=>[], "tags"=>["y9f", "affects", "traf3", "traf6", "binding"], "article_id"=>273599, "categories"=>["Biological Sciences", "Biochemistry", "Immunology"], "users"=>["Chaoyang Wen", "Zhifeng Yan", "Xiaoli Yang", "Kai Guan", "Changzhi Xu", "Ting Song", "Zirui Zheng", "Wenjun Wang", "Ying Wang", "Man Zhao", "Yanhong Zhang", "Tao Xu", "Jianping Dou", "Jingmei Liu", "Quanbin Xu", "Xiang He", "Congwen Wei", "Hui Zhong"], "doi"=>["https://dx.doi.org/10.1371/journal.pone.0041687.g003"], "stats"=>{"downloads"=>0, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_MAVS_Y9F_affects_TRAF3_and_TRAF6_binding_to_MAVS_/273599", "title"=>"MAVS Y9F affects TRAF3 and TRAF6 binding to MAVS.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-02-20 01:54:29"}
  • {"files"=>["https://ndownloader.figshare.com/files/603236"], "description"=>"<p>(A–B) HEK293T cells were transfected with expression vector encoding Flag-MAVS (WT) or Flag-MAVS Y9F mutant (Y9F). After 24 h, cells were infected with VSV at a MOI of 0.002 for 30 min (A) or at a different MOI (B) for 30 min. Anti-Flag immunoprecipitates were analyzed by immunoblotting with anti-P-Tyr or anti-MAVS antibody. (C) HEK293T cells were cotransfected with Myc-WT or Myc-Y9F together with Flag-tagged TRAF3 in the presence of VSV infection at a MOI of 0.002 for the indicated times, cell lysates were immunoprecipitated with anti-Flag antibody, followed by immunoblotting with anti-Flag and anti-Myc antibodies. (D) MAVS−/− MEF cells were transfected with expression vector encoding Flag-MAVS or Flag-MAVS Y9F mutant. After 24 h, cells were infected with VSV at a multiplicity of infection (MOI) of 0.002 for 20 h; endogenous IFN-β mRNA expression was analyzed by qRTPCR. Results are expressed as fold-increase of IFN-β mRNA level normalized with β-actin level and relatively to Y9F MAVS-transfected cells. (E) Using the supernatants collected from samples shown in panel D, IFN-β release was measured by ELISA. (F) Two individually transfected mixed clones with WT MAVS or Y9F MAVS in MAVS−/−MEFs were infected with VSV at a multiplicity of infection (MOI) of 0.002. Virus yields in the supernatants at 20 h after infection were determined by plaque assay. From D to F, Data are mean of three independent experiments ± SEM done in triplicate.</p>", "links"=>[], "tags"=>["y9f", "alters", "mavs-dependent", "antiviral", "responses"], "article_id"=>273706, "categories"=>["Biological Sciences", "Biochemistry", "Immunology"], "users"=>["Chaoyang Wen", "Zhifeng Yan", "Xiaoli Yang", "Kai Guan", "Changzhi Xu", "Ting Song", "Zirui Zheng", "Wenjun Wang", "Ying Wang", "Man Zhao", "Yanhong Zhang", "Tao Xu", "Jianping Dou", "Jingmei Liu", "Quanbin Xu", "Xiang He", "Congwen Wei", "Hui Zhong"], "doi"=>["https://dx.doi.org/10.1371/journal.pone.0041687.g004"], "stats"=>{"downloads"=>0, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_MAVS_Y9F_alters_MAVS_dependent_antiviral_responses_to_virus_infection_/273706", "title"=>"MAVS Y9F alters MAVS-dependent antiviral responses to virus infection.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-02-20 01:55:08"}
  • {"files"=>["https://ndownloader.figshare.com/files/603364"], "description"=>"<p>(A) HEK293T cells were transfected with increasing amount of Flag-vector, Flag-WT or Flag-Y9F mutant. Cells were harvested for Trypan Blue counting 48 h post-transfection. Data are mean of three independent experiments ± SEM done in triplicate. (B) HEK293T cells were transfected with 1.0 µg expression vector encoding Flag-vector, Flag-WT or Flag-Y9F mutant. Annexin V assays were performed 48 hours post-transfection.</p>", "links"=>[], "tags"=>["y9f", "dispensable", "mavs-induced"], "article_id"=>273840, "categories"=>["Biological Sciences", "Biochemistry", "Immunology"], "users"=>["Chaoyang Wen", "Zhifeng Yan", "Xiaoli Yang", "Kai Guan", "Changzhi Xu", "Ting Song", "Zirui Zheng", "Wenjun Wang", "Ying Wang", "Man Zhao", "Yanhong Zhang", "Tao Xu", "Jianping Dou", "Jingmei Liu", "Quanbin Xu", "Xiang He", "Congwen Wei", "Hui Zhong"], "doi"=>["https://dx.doi.org/10.1371/journal.pone.0041687.g005"], "stats"=>{"downloads"=>0, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_MAVS_Y9F_is_dispensable_for_MAVS_induced_apoptosis_/273840", "title"=>"MAVS Y9F is dispensable for MAVS-induced apoptosis.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-02-20 01:55:53"}

PMC Usage Stats | Further Information

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Relative Metric

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