ADAR1 RNA editing enzyme regulates R-loop formation and genome stability at telomeres in cancer cells.


Journal

Nature communications
ISSN: 2041-1723
Titre abrégé: Nat Commun
Pays: England
ID NLM: 101528555

Informations de publication

Date de publication:
12 03 2021
Historique:
received: 28 05 2020
accepted: 19 02 2021
entrez: 13 3 2021
pubmed: 14 3 2021
medline: 2 4 2021
Statut: epublish

Résumé

ADAR1 is involved in adenosine-to-inosine RNA editing. The cytoplasmic ADAR1p150 edits 3'UTR double-stranded RNAs and thereby suppresses induction of interferons. Loss of this ADAR1p150 function underlies the embryonic lethality of Adar1 null mice, pathogenesis of the severe autoimmune disease Aicardi-Goutières syndrome, and the resistance developed in cancers to immune checkpoint blockade. In contrast, the biological functions of the nuclear-localized ADAR1p110 remain largely unknown. Here, we report that ADAR1p110 regulates R-loop formation and genome stability at telomeres in cancer cells carrying non-canonical variants of telomeric repeats. ADAR1p110 edits the A-C mismatches within RNA:DNA hybrids formed between canonical and non-canonical variant repeats. Editing of A-C mismatches to I:C matched pairs facilitates resolution of telomeric R-loops by RNase H2. This ADAR1p110-dependent control of telomeric R-loops is required for continued proliferation of telomerase-reactivated cancer cells, revealing the pro-oncogenic nature of ADAR1p110 and identifying ADAR1 as a promising therapeutic target of telomerase positive cancers.

Identifiants

pubmed: 33712600
doi: 10.1038/s41467-021-21921-x
pii: 10.1038/s41467-021-21921-x
pmc: PMC7955049
doi:

Substances chimiques

RNA-Binding Proteins 0
DNA 9007-49-2
ADAR protein, human EC 3.5.4.37
ADAR1 protein, mouse EC 3.5.4.4
Adenosine Deaminase EC 3.5.4.4

Types de publication

Journal Article Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

1654

Subventions

Organisme : NCI NIH HHS
ID : P30 CA010815
Pays : United States
Organisme : NCI NIH HHS
ID : R01 CA175058
Pays : United States
Organisme : NIGMS NIH HHS
ID : R01 GM040536
Pays : United States
Organisme : NIGMS NIH HHS
ID : R01 GM130716
Pays : United States

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Auteurs

Yusuke Shiromoto (Y)

The Wistar Institute, Philadelphia, PA, USA.

Masayuki Sakurai (M)

The Wistar Institute, Philadelphia, PA, USA.
Research Institute for Biomedical Sciences, Tokyo University of Science, Chiba, Japan.

Moeko Minakuchi (M)

The Wistar Institute, Philadelphia, PA, USA.

Kentaro Ariyoshi (K)

The Wistar Institute, Philadelphia, PA, USA.
Integrated Center for Science and Humanities, Fukushima Medical University, Fukushima, Japan.

Kazuko Nishikura (K)

The Wistar Institute, Philadelphia, PA, USA. kazuko@wistar.org.

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Classifications MeSH