Identifying an Abnormal Phosphorylated Adaptor by Viral Kinase Using Mass Spectrometry.

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  • Author(s): Su C;Su C; Su C; Su C; Zheng C; Zheng C
  • Source:
    Methods in molecular biology (Clifton, N.J.) [Methods Mol Biol] 2025; Vol. 2854, pp. 29-34.
  • Publication Type:
    Journal Article
  • Language:
    English
  • Additional Information
    • Source:
      Publisher: Humana Press Country of Publication: United States NLM ID: 9214969 Publication Model: Print Cited Medium: Internet ISSN: 1940-6029 (Electronic) Linking ISSN: 10643745 NLM ISO Abbreviation: Methods Mol Biol Subsets: MEDLINE
    • Publication Information:
      Publication: Totowa, NJ : Humana Press
      Original Publication: Clifton, N.J. : Humana Press,
    • Subject Terms:
    • Abstract:
      Mass spectrometers are widely used to identify protein phosphorylation sites. The process usually involves selective isolation of phosphoproteins and subsequent fragmentation to identify both the peptide sequence and phosphorylation site. Immunoprecipitation could capture and purify the protein of interest, greatly reducing sample complexity before submitting it for mass spectrometry analysis. This chapter describes a method to identify an abnormal phosphorylated site of the adaptor protein by a viral kinase through immunoprecipitation followed by LC-MS/MS.
      (© 2025. The Author(s), under exclusive license to Springer Science+Business Media, LLC, part of Springer Nature.)
    • References:
      Zhou Y, He C, Wang L, Ge B (2017) Post-translational regulation of antiviral innate signaling. Eur J Immunol 47(9):1414–1426. https://doi.org/10.1002/eji.201746959. (PMID: 10.1002/eji.201746959287448517163624)
      Liu J, Qian C, Cao X (2016) Post-translational modification control of innate immunity. Immunity 45(1):15–30. https://doi.org/10.1016/j.immuni.2016.06.020. (PMID: 10.1016/j.immuni.2016.06.02027438764)
      Jin X, Wang W, Zhao X, Jiang W, Shao Q, Chen Z, Huang C (2023) The battle between the innate immune cGAS-STING signaling pathway and human herpesvirus infection. Front Immunol 14:1235590. https://doi.org/10.3389/fimmu.2023.1235590. (PMID: 10.3389/fimmu.2023.12355903760080910433641)
      Zhu H, Zheng C (2020) The race between host antiviral innate immunity and the immune evasion strategies of herpes simplex virus 1. Microbiol Mol Biol Rev 84(4). https://doi.org/10.1128/MMBR.00099-20.
      Su C, Zhan G, Zheng C (2016) Evasion of host antiviral innate immunity by HSV-1, an update. Virol J 13:38. https://doi.org/10.1186/s12985-016-0495-5. (PMID: 10.1186/s12985-016-0495-5269521114782282)
      Franciosa G, Locard-Paulet M, Jensen LJ, Olsen JV (2023) Recent advances in kinase signaling network profiling by mass spectrometry. Curr Opin Chem Biol 73:102260. https://doi.org/10.1016/j.cbpa.2022.102260. (PMID: 10.1016/j.cbpa.2022.10226036657259)
      Kitamura N, Galligan JJ (2023) A global view of the human post-translational modification landscape. Biochem J 480(16):1241–1265. https://doi.org/10.1042/BCJ20220251. (PMID: 10.1042/BCJ2022025137610048)
      Lin JS, Lai EM (2017) Protein-protein interactions: co-immunoprecipitation. Methods Mol Biol 1615:211–219. https://doi.org/10.1007/978-1-4939-7033-9_17. (PMID: 10.1007/978-1-4939-7033-9_1728667615)
      Ngounou Wetie AG, Sokolowska I, Woods AG, Roy U, Deinhardt K, Darie CC (2014) Protein-protein interactions: switch from classical methods to proteomics and bioinformatics-based approaches. Cell Mol Life Sci 71(2):205–228. https://doi.org/10.1007/s00018-013-1333-1. (PMID: 10.1007/s00018-013-1333-123579629)
      Wang S, Wu R, Lu J, Jiang Y, Huang T, Cai YD (2022) Protein-protein interaction networks as miners of biological discovery. Proteomics 22(15–16):e2100190. https://doi.org/10.1002/pmic.202100190. (PMID: 10.1002/pmic.20210019035567424)
      Wang K, Ni L, Wang S, Zheng C (2014) Herpes simplex virus 1 protein kinase US3 hyperphosphorylates p65/RelA and dampens NF-kappaB activation. J Virol 88(14):7941–7951. https://doi.org/10.1128/JVI.03394-13. (PMID: 10.1128/JVI.03394-13248077164097809)
      Wang S, Wang K, Lin R, Zheng C (2013) Herpes simplex virus 1 serine/threonine kinase US3 hyperphosphorylates IRF3 and inhibits beta interferon production. J Virol 87(23):12814–12827. https://doi.org/10.1128/JVI.02355-13. (PMID: 10.1128/JVI.02355-13240491793838156)
      You H, Lin Y, Lin F, Yang M, Li J, Zhang R, Huang Z, Shen Q, Tang R, Zheng C (2020) Beta-catenin is required for the cGAS/STING signaling pathway but antagonized by the herpes simplex virus 1 US3 protein. J Virol 94(5). https://doi.org/10.1128/JVI.01847-19.
    • Contributed Indexing:
      Keywords: A signaling adaptor; Immunoprecipitation; LC-MS/MS; Phosphorylation; Viral kinase
    • Accession Number:
      0 (Phosphoproteins)
    • Publication Date:
      Date Created: 20240827 Date Completed: 20240827 Latest Revision: 20240827
    • Publication Date:
      20240828
    • Accession Number:
      10.1007/978-1-0716-4108-8_4
    • Accession Number:
      39192115