Back

Disruption of Z-RNA-binding of ADAR1 induces Aicardi-Goutieres syndrome-like encephalopathy in mice

Nakahama, T.; Kato, Y.; Shibuya, T.; Kim, J. I.; Vongpipatana, T.; Todo, H.; Xing, Y.; Kawahara, Y.

2020-12-16 immunology
10.1101/2020.12.16.422984 bioRxiv
Show abstract

ADAR1 p150 is an enzyme responsible for adenosine-to-inosine RNA editing. Deletion of ADAR1 p150 results in embryonic lethality with a type I interferon (IFN) signature, caused by aberrant MDA5 sensing unedited transcripts. ADAR1 p150 contains a unique Z-DNA/RNA-binding domain (Z); however, the role of this domain remains unknown. A mutation has been identified in this domain in patients with Aicardi-Goutieres syndrome (AGS), an inherited interferonopathy, suggesting an essential role in avoiding MDA5 activation. Here, we show that a mutation in the Z domain reduces the editing activity of ADAR1 p150 by comparing activity between wild-type and mutated isoforms expressed in Adar1/Adar2 knockout cells. Furthermore, we created Z domain-mutated knock-in mice, which displayed severe growth retardation with abnormal organ development, including AGS-like encephalopathy with a type I IFN signature. These abnormalities were ameliorated by the concurrent deletion of MDA5. Collectively, Z-RNA-recognition contributes to ADAR1 p150-mediated RNA editing, which prevents MDA5 activation.

Matching journals

The top 4 journals account for 50% of the predicted probability mass.

50% of probability mass above

"Similar papers" are the closest papers from that journal in the model's embedding space. They show what the match is built on, but the ranking comes mostly from a classifier over the whole training set, not from these examples alone.