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@ARTICLE{Lorenzo:289494,
      author       = {J. P. Lorenzo$^*$ and L. Molla and E. M. E. Amro$^*$ and I.
                      L. Ibarra and S. Ruf$^*$ and C. Neber$^*$ and C. Gkougkousis
                      and J. Ridani and P. G. Subramani and J. Boulais and D.
                      Harjanto and A. Vonica and J. M. Di Noia and C. Dieterich
                      and J. B. Zaugg and F. Papavasiliou$^*$},
      title        = {{APOBEC}2 safeguards skeletal muscle cell fate through
                      binding chromatin and regulating transcription of non-muscle
                      genes during myoblast differentiation.},
      journal      = {Proceedings of the National Academy of Sciences of the
                      United States of America},
      volume       = {121},
      number       = {17},
      issn         = {0027-8424},
      address      = {Washington, DC},
      publisher    = {National Acad. of Sciences},
      reportid     = {DKFZ-2024-00816},
      pages        = {e2312330121},
      year         = {2024},
      note         = {#EA:D150#LA:D150#},
      abstract     = {The apolipoprotein B messenger RNA editing enzyme,
                      catalytic polypeptide (APOBEC) family is composed of nucleic
                      acid editors with roles ranging from antibody
                      diversification to RNA editing. APOBEC2, a member of this
                      family with an evolutionarily conserved nucleic acid-binding
                      cytidine deaminase domain, has neither an established
                      substrate nor function. Using a cellular model of muscle
                      differentiation where APOBEC2 is inducibly expressed, we
                      confirmed that APOBEC2 does not have the attributed
                      molecular functions of the APOBEC family, such as RNA
                      editing, DNA demethylation, and DNA mutation. Instead, we
                      found that during muscle differentiation APOBEC2 occupied a
                      specific motif within promoter regions; its removal from
                      those regions resulted in transcriptional changes.
                      Mechanistically, these changes reflect the direct
                      interaction of APOBEC2 with histone deacetylase (HDAC)
                      transcriptional corepressor complexes. We also found that
                      APOBEC2 could bind DNA directly, in a sequence-specific
                      fashion, suggesting that it functions as a recruiter of HDAC
                      to specific genes whose promoters it occupies. These genes
                      are normally suppressed during muscle cell differentiation,
                      and their suppression may contribute to the safeguarding of
                      muscle cell fate. Altogether, our results reveal a unique
                      role for APOBEC2 within the APOBEC family.},
      keywords     = {Chromatin: genetics / Muscle Proteins: metabolism / APOBEC
                      Deaminases: genetics / Cytidine Deaminase: metabolism /
                      Muscle Fibers, Skeletal: metabolism / Cell Differentiation:
                      genetics / RNA, Messenger: genetics / Myoblasts: metabolism
                      / DNA / APOBEC-1 Deaminase: genetics / APOBEC family (Other)
                      / DNA binding (Other) / muscle differentiation (Other) /
                      safeguard factor (Other) / transcriptional regulator (Other)
                      / Chromatin (NLM Chemicals) / Muscle Proteins (NLM
                      Chemicals) / APOBEC Deaminases (NLM Chemicals) / Cytidine
                      Deaminase (NLM Chemicals) / RNA, Messenger (NLM Chemicals) /
                      DNA (NLM Chemicals) / APOBEC-1 Deaminase (NLM Chemicals)},
      cin          = {D150},
      ddc          = {500},
      cid          = {I:(DE-He78)D150-20160331},
      pnm          = {314 - Immunologie und Krebs (POF4-314)},
      pid          = {G:(DE-HGF)POF4-314},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:38625936},
      doi          = {10.1073/pnas.2312330121},
      url          = {https://inrepo02.dkfz.de/record/289494},
}