Key result
Structural advances in ADAR1 clarify its catalytic mechanism and role in suppressing immune signaling.
Why the study?
Recent structural and mechanistic advances have illuminated ADAR1 architecture and its roles in RNA editing and immune regulation, warranting a synthesis of current knowledge and therapeutic implications.
This review provides insights into the structural and mechanistic principles of ADAR1-mediated RNA editing and its role in immune regulation.
Does not yet alter clinical practice; leaves open mechanistic refinement of ADAR1-targeted interventions in cardiology research.
Adenosine deaminase acting on RNA 1 (ADAR1) is a central regulator of innate immunity. By binding to and catalyzing adenosine-to-inosine deamination within double-stranded RNAs, ADAR1 mitigates the immunogenicity of self-derived RNAs and preserves cellular homeostasis. In this review, we summarize recent structural and mechanistic advances that illuminate key features of ADAR1 architecture, including how its multi-domains engage dsRNA substrates and contribute to substrate selectivity. Integrated with decades of biochemical and genetic studies, these insights refine our understanding of ADAR1's catalytic mechanism, domain-specific activities, and roles in suppressing immune signaling. We further highlight emerging knowledge on ADAR1's RNA substrate landscape, its interactions with protein partners, and the mechanistic principles that underlie its broad RNA editing and immune regulatory functions, with implications for disease pathogenesis and therapeutic RNA editing.
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Deng et al. (2026) reported a review. ADAR1 was evaluated. Recent structural and mechanistic advances illuminate key features of ADAR1 architecture, refining our understanding of its catalytic mechanism and roles in suppressing immune signaling.
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