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@ARTICLE{Acharya:278654,
      author       = {Acharya, Dhiraj and Sayyad, Zuberwasim and Hoenigsperger,
                      Helene and Hirschenberger, Maximilian and Zurenski, Matthew
                      and Balakrishnan, Kannan and Zhu, Junji and Gableske,
                      Sebastian and Kato, Jiro and Zhang, Shen-Ying and Casanova,
                      Jean-Laurent and Moss, Joel and Sparrer, Konstantin M J and
                      Gack, Michaela U},
      title        = {{TRIM}23 mediates c{GAS}-induced autophagy in anti-{HSV}
                      defense.},
      journal      = {Nature Communications},
      volume       = {16},
      number       = {1},
      issn         = {2041-1723},
      address      = {[London]},
      publisher    = {Springer Nature},
      reportid     = {DZNE-2025-00610},
      pages        = {4418},
      year         = {2025},
      abstract     = {The cGAS-STING pathway, well-known to elicit interferon
                      (IFN) responses, is also a key inducer of autophagy upon
                      virus infection or other stimuli. Whereas the mediators for
                      cGAS-induced IFN responses are well characterized, much less
                      is known about how cGAS elicits autophagy. Here, we report
                      that TRIM23, a unique TRIM protein harboring both ubiquitin
                      E3 ligase and GTPase activity, is crucial for
                      cGAS-STING-dependent antiviral autophagy. Genetic ablation
                      of TRIM23 impairs autophagic control of HSV-1 infection.
                      HSV-1 infection or cGAS-STING stimulation induces
                      TBK1-mediated TRIM23 phosphorylation at S39, which triggers
                      TRIM23 autoubiquitination and GTPase activity and ultimately
                      elicits autophagy. Fibroblasts from a patient with herpes
                      simplex encephalitis heterozygous for a dominant-negative,
                      kinase-inactivating TBK1 mutation fail to activate autophagy
                      by TRIM23 and cGAS-STING. Our results thus identify the
                      cGAS-STING-TBK1-TRIM23 axis as a key autophagy defense
                      pathway and may stimulate new therapeutic interventions for
                      viral or inflammatory diseases.},
      keywords     = {Autophagy: immunology / Humans / Nucleotidyltransferases:
                      metabolism / Nucleotidyltransferases: genetics /
                      Nucleotidyltransferases: immunology / Herpesvirus 1, Human:
                      immunology / Herpesvirus 1, Human: physiology / Protein
                      Serine-Threonine Kinases: metabolism / Protein
                      Serine-Threonine Kinases: genetics / Membrane Proteins:
                      metabolism / Membrane Proteins: genetics / Animals /
                      Phosphorylation / Fibroblasts: metabolism / Fibroblasts:
                      virology / Mice / Ubiquitin-Protein Ligases: metabolism /
                      Ubiquitin-Protein Ligases: genetics / Herpes Simplex:
                      immunology / Herpes Simplex: virology / HEK293 Cells /
                      Signal Transduction / Ubiquitination /
                      Nucleotidyltransferases (NLM Chemicals) / Protein
                      Serine-Threonine Kinases (NLM Chemicals) / Membrane Proteins
                      (NLM Chemicals) / cGAS protein, human (NLM Chemicals) / TBK1
                      protein, human (NLM Chemicals) / STING1 protein, human (NLM
                      Chemicals) / Ubiquitin-Protein Ligases (NLM Chemicals) /
                      cGAS protein, mouse (NLM Chemicals)},
      cin          = {AG Sparrer},
      ddc          = {500},
      cid          = {I:(DE-2719)1910003},
      pnm          = {351 - Brain Function (POF4-351)},
      pid          = {G:(DE-HGF)POF4-351},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:40360474},
      pmc          = {pmc:PMC12075517},
      doi          = {10.1038/s41467-025-59338-5},
      url          = {https://pub.dzne.de/record/278654},
}