The role of RNA editing enzyme ADAR1 in human disease.
ADAR1
AGS
RNA editing
human disease
innate immunity
Journal
Wiley interdisciplinary reviews. RNA
ISSN: 1757-7012
Titre abrégé: Wiley Interdiscip Rev RNA
Pays: United States
ID NLM: 101536955
Informations de publication
Date de publication:
01 2022
01 2022
Historique:
revised:
02
03
2021
received:
18
09
2020
accepted:
22
04
2021
pubmed:
10
6
2021
medline:
28
1
2022
entrez:
9
6
2021
Statut:
ppublish
Résumé
Adenosine deaminase acting on RNA (ADAR) catalyzes the posttranscriptional conversion of adenosine to inosine in double-stranded RNA (dsRNA), which can lead to the creation of missense mutations in coding sequences. Recent studies show that editing-dependent functions of ADAR1 protect dsRNA from dsRNA-sensing molecules and inhibit innate immunity and the interferon-mediated response. Deficiency in these ADAR1 functions underlie the pathogenesis of autoinflammatory diseases such as the type I interferonopathies Aicardi-Goutieres syndrome and dyschromatosis symmetrica hereditaria. ADAR1-mediated editing of endogenous coding and noncoding RNA as well as ADAR1 editing-independent interactions with DICER can also have oncogenic or tumor suppressive effects that affect tumor proliferation, invasion, and response to immunotherapy. The combination of proviral and antiviral roles played by ADAR1 in repressing the interferon response and editing viral RNAs alters viral morphogenesis and cell susceptibility to infection. This review analyzes the structure and function of ADAR1 with a focus on its position in human disease pathways and the mechanisms of its disease-associated effects. This article is categorized under: RNA in Disease and Development > RNA in Disease RNA Processing > RNA Editing and Modification RNA Interactions with Proteins and Other Molecules > Protein-RNA Interactions: Functional Implications.
Identifiants
pubmed: 34105255
doi: 10.1002/wrna.1665
pmc: PMC8651834
mid: NIHMS1752144
doi:
Substances chimiques
RNA, Double-Stranded
0
RNA-Binding Proteins
0
Inosine
5A614L51CT
ADAR protein, human
EC 3.5.4.37
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
Review
Langues
eng
Sous-ensembles de citation
IM
Pagination
e1665Subventions
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
Informations de copyright
© 2021 Wiley Periodicals LLC.
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