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@ARTICLE{Merold:279044,
      author       = {Merold, Veronika and Bekere, Indra and Kretschmer, Stefanie
                      and Schnell, Adrian F and Kmiec, Dorota and Sivarajan, Rinu
                      and Lammens, Katja and Liu, Rou and Mergner, Julia and
                      Teppert, Julia and Hirschenberger, Maximilian and Henrici,
                      Alexander and Hammes, Sarah and Buder, Kathrin and Weitz,
                      Marcus and Hackmann, Karl and Koenig, Lars M and Pichlmair,
                      Andreas and Schwierz, Nadine and Sparrer, Konstantin M J and
                      Lee-Kirsch, Min Ae and de Oliveira Mann, Carina C},
      title        = {{S}tructural basis for {OAS}2 regulation and its antiviral
                      function.},
      journal      = {Molecular cell},
      volume       = {85},
      number       = {11},
      issn         = {1097-2765},
      address      = {[Cambridge, Mass.]},
      publisher    = {Cell Press},
      reportid     = {DZNE-2025-00674},
      pages        = {2176 - 2193.e13},
      year         = {2025},
      abstract     = {Oligoadenylate synthetase (OAS) proteins are immune sensors
                      for double-stranded RNA and are critical for restricting
                      viruses. OAS2 comprises two OAS domains, only one of which
                      can synthesize 2'-5'-oligoadenylates for RNase L activation.
                      Existing structures of OAS1 provide a model for enzyme
                      activation, but they do not explain how multiple OAS domains
                      discriminate RNA length. Here, we discover that human OAS2
                      exists in an auto-inhibited state as a zinc-mediated dimer
                      and present a mechanism for RNA length discrimination: the
                      catalytically deficient domain acts as a molecular ruler
                      that prevents autoreactivity to short RNAs. We demonstrate
                      that dimerization and myristoylation localize OAS2 to Golgi
                      membranes and that this is required for OAS2 activation and
                      the restriction of viruses that exploit the endomembrane
                      system for replication, e.g., coronaviruses. Finally, our
                      results highlight the non-redundant role of OAS proteins and
                      emphasize the clinical relevance of OAS2 by identifying a
                      patient with a loss-of-function mutation associated with
                      autoimmune disease.},
      keywords     = {2',5'-Oligoadenylate Synthetase: genetics /
                      2',5'-Oligoadenylate Synthetase: chemistry /
                      2',5'-Oligoadenylate Synthetase: metabolism / Humans / Golgi
                      Apparatus: enzymology / Golgi Apparatus: virology / Protein
                      Multimerization / HEK293 Cells / Virus Replication /
                      Mutation / RNA, Double-Stranded: metabolism / RNA,
                      Double-Stranded: genetics / HeLa Cells / Endoribonucleases:
                      metabolism / Endoribonucleases: genetics /
                      Structure-Activity Relationship / Adenine Nucleotides /
                      Oligoribonucleotides / OAS2 (Other) / RNA sensing (Other) /
                      RNase L (Other) / innate immunity (Other) / localization
                      (Other) / oligoadenylates (Other) / structural biology
                      (Other) / virus restriction (Other) / 2',5'-Oligoadenylate
                      Synthetase (NLM Chemicals) / OAS2 protein, human (NLM
                      Chemicals) / 2',5'-oligoadenylate (NLM Chemicals) / RNA,
                      Double-Stranded (NLM Chemicals) / 2-5A-dependent
                      ribonuclease (NLM Chemicals) / Endoribonucleases (NLM
                      Chemicals) / Adenine Nucleotides (NLM Chemicals) /
                      Oligoribonucleotides (NLM Chemicals)},
      cin          = {AG Sparrer},
      ddc          = {610},
      cid          = {I:(DE-2719)1910003},
      pnm          = {351 - Brain Function (POF4-351)},
      pid          = {G:(DE-HGF)POF4-351},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:40412389},
      doi          = {10.1016/j.molcel.2025.05.001},
      url          = {https://pub.dzne.de/record/279044},
}