Home > Publications Database > TRIM23 mediates cGAS-induced autophagy in anti-HSV defense. > print

001     278654
005     20250601001324.0
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037 _ _ |a DZNE-2025-00610
041 _ _ |a English
082 _ _ |a 500
100 1 _ |a Acharya, Dhiraj
|b 0
245 _ _ |a TRIM23 mediates cGAS-induced autophagy in anti-HSV defense.
260 _ _ |a [London]
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|b Springer Nature
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520 _ _ |a 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.
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650 _ 7 |a Nucleotidyltransferases
|0 EC 2.7.7.-
|2 NLM Chemicals
650 _ 7 |a Protein Serine-Threonine Kinases
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650 _ 7 |a Membrane Proteins
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650 _ 7 |a cGAS protein, human
|0 EC 2.7.7.-
|2 NLM Chemicals
650 _ 7 |a TBK1 protein, human
|0 EC 2.7.11.1
|2 NLM Chemicals
650 _ 7 |a STING1 protein, human
|2 NLM Chemicals
650 _ 7 |a Ubiquitin-Protein Ligases
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650 _ 7 |a cGAS protein, mouse
|0 EC 2.7.7.-
|2 NLM Chemicals
650 _ 2 |a Autophagy: immunology
|2 MeSH
650 _ 2 |a Humans
|2 MeSH
650 _ 2 |a Nucleotidyltransferases: metabolism
|2 MeSH
650 _ 2 |a Nucleotidyltransferases: genetics
|2 MeSH
650 _ 2 |a Nucleotidyltransferases: immunology
|2 MeSH
650 _ 2 |a Herpesvirus 1, Human: immunology
|2 MeSH
650 _ 2 |a Herpesvirus 1, Human: physiology
|2 MeSH
650 _ 2 |a Protein Serine-Threonine Kinases: metabolism
|2 MeSH
650 _ 2 |a Protein Serine-Threonine Kinases: genetics
|2 MeSH
650 _ 2 |a Membrane Proteins: metabolism
|2 MeSH
650 _ 2 |a Membrane Proteins: genetics
|2 MeSH
650 _ 2 |a Animals
|2 MeSH
650 _ 2 |a Phosphorylation
|2 MeSH
650 _ 2 |a Fibroblasts: metabolism
|2 MeSH
650 _ 2 |a Fibroblasts: virology
|2 MeSH
650 _ 2 |a Mice
|2 MeSH
650 _ 2 |a Ubiquitin-Protein Ligases: metabolism
|2 MeSH
650 _ 2 |a Ubiquitin-Protein Ligases: genetics
|2 MeSH
650 _ 2 |a Herpes Simplex: immunology
|2 MeSH
650 _ 2 |a Herpes Simplex: virology
|2 MeSH
650 _ 2 |a HEK293 Cells
|2 MeSH
650 _ 2 |a Signal Transduction
|2 MeSH
650 _ 2 |a Ubiquitination
|2 MeSH
700 1 _ |a Sayyad, Zuberwasim
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700 1 _ |a Hoenigsperger, Helene
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700 1 _ |a Hirschenberger, Maximilian
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700 1 _ |a Zurenski, Matthew
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700 1 _ |a Balakrishnan, Kannan
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700 1 _ |a Zhu, Junji
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700 1 _ |a Gableske, Sebastian
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700 1 _ |a Kato, Jiro
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700 1 _ |a Zhang, Shen-Ying
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700 1 _ |a Casanova, Jean-Laurent
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700 1 _ |a Moss, Joel
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700 1 _ |a Sparrer, Konstantin M J
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700 1 _ |a Gack, Michaela U
|0 0000-0002-2163-2598
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773 _ _ |a 10.1038/s41467-025-59338-5
|g Vol. 16, no. 1, p. 4418
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|t Nature Communications
|v 16
|y 2025
|x 2041-1723
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