ArticleThe Journal of biological chemistry2007
RNA binding-independent dimerization of adenosine deaminases acting on RNA and dominant negative effects of nonfunctional subunits on dimer functions.
Article in The Journal of biological chemistry, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 91 papers.
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Who cites it
91 citing papers in PubMed, 153 citations in OpenAlex.
- ADAR1 and ADAR2 associate with the RNA exosome and modulate RNA stability.Nucleic acids research · 2026Article
- A dual role of EZH2 in regulating A-to-I RNA editing and mRNA stability through ADAR.Nature communications · 2026Article
- ADAR1 regulates dsRNA formation in nuclear and mitochondrial transcripts through editing-dependent and -independent mechanisms.Cell reports · 2026Article
- Two codes of RNA editing by deamination in human diseases.Experimental & molecular medicine · 2026Review
- PACT suppresses PKR activation through dsRNA binding and dimerization, and is a therapeutic target for triple-negative breast cancer.RNA (New York, N.Y.) · 2025Article
- C to U RNA editing of MFN1 is regulated by ADARB1 and associates with favourable prognosis in chronic lymphocytic leukemia.Scientific reports · 2025Article
- High-speed atomic force microscopy and 3D modeling reveal the structural dynamics of ADAR1 complexes.Nature communications · 2025Article
- Computer-Aided Discovery of Natural Compounds Targeting the ADAR2 dsRBD2-RNA Interface and Computational Modeling of Full-Length ADAR2 Protein Structure.International journal of molecular sciences · 2025Article
- Biochemical profiling and structural basis of ADAR1-mediated RNA editing.Molecular cell · 2025Article
- ADAR1: from basic mechanisms to inhibitors.Trends in cell biology · 2025Review
- ADAR1 Promotes the Progression and Temozolomide Resistance of Glioma Through p62-Mediated Selective Autophagy.CNS neuroscience & therapeutics · 2025Article
- Distinct interactomes of ADAR1 nuclear and cytoplasmic protein isoforms and their responses to interferon induction.Nucleic acids research · 2024Article
- Dimerization of ADAR1 modulates site-specificity of RNA editing.Nature communications · 2024Article
- Structural perspectives on adenosine to inosine RNA editing by ADARs.Molecular therapy. Nucleic acids · 2024Review
- ADAR Family Proteins: A Structural Review.Current issues in molecular biology · 2024Review
- Novel insights into double-stranded RNA-mediated immunopathology.Nature reviews. Immunology · 2024Review
- Dissecting the basis for differential substrate specificity of ADAR1 and ADAR2.Nature communications · 2023Article
- ADAR1 links R-loop homeostasis to ATR activation in replication stress response.Nucleic acids research · 2023Article
- RNA Editing in Cancer Progression.Cancers · 2023Review
- ADAR1p150 prevents MDA5 and PKR activation via distinct mechanisms to avert fatal autoinflammation.Molecular cell · 2023Article
31 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
RNA editing that converts adenosine to inosine in double-stranded RNA (dsRNA) is mediated by adenosine deaminases acting on RNA (ADAR). ADAR1 and ADAR2 form respective homodimers, and this association is essential for their enzymatic activities. In this investigation, we set out experiments aiming to determine whether formation of the homodimer complex is mediated by an amino acid interface made through protein-protein interactions of two monomers or via binding of the two subunits to a dsRNA substrate. Point mutations were created in the dsRNA binding domains (dsRBDs) that abolished all RNA binding, as tested for two classes of ADAR ligands, long and short dsRNA. The mutant ADAR dimer complexes were intact, as demonstrated by their ability to co-purify in a sequential affinity-tagged purification and also by their elution at the dimeric fraction position on a size fractionation column. Our results demonstrated ADAR dimerization independent of their binding to dsRNA, establishing the importance of protein-protein interactions for dimer formation. As expected, these mutant ADARs could no longer perform their catalytic function due to the loss in substrate binding. Surprisingly, a chimeric dimer consisting of one RNA binding mutant monomer and a wild type partner still abolished its ability to bind and edit its substrate, indicating that ADAR dimers require two subunits with functional dsRBDs for binding to a dsRNA substrate and then for editing activity to occur.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.