% IMPORTANT: The following is UTF-8 encoded. This means that in the presence
% of non-ASCII characters, it will not work with BibTeX 0.99 or older.
% Instead, you should use an up-to-date BibTeX implementation like “bibtex8” or
% “biber”.
@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},
}