ArticleMolecular biology of the cell2001
The human but not the Xenopus RNA-editing enzyme ADAR1 has an atypical nuclear localization signal and displays the characteristics of a shuttling protein.
Article in Molecular biology of the cell, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 66 papers.
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Who cites it
66 citing papers in PubMed, 115 citations in OpenAlex.
- ADAR1 Regulates Alternative Splicing Through an RNA Editing-Independent Mechanism.International journal of molecular sciences · 2026Article
- 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
- Stereo-random oligonucleotides enable efficient recruitment of ADAR in vitro and in vivo.Nature communications · 2025Article
- Autocrine interferon poisoning mediates ADAR1-dependent synthetic lethality in BRCA1/2-mutant cancers.Nature communications · 2025Article
- ADARs: pleiotropy in function, versatility in application.Nucleic acids research · 2025Review
- ncRNA Editing: Functional Characterization and Computational Resources.Methods in molecular biology (Clifton, N.J.) · 2025Article
- Distinct interactomes of ADAR1 nuclear and cytoplasmic protein isoforms and their responses to interferon induction.Nucleic acids research · 2024Article
- Induction of Viral Mimicry Upon Loss of DHX9 and ADAR1 in Breast Cancer Cells.Cancer research communications · 2024Article
- Novel insights into double-stranded RNA-mediated immunopathology.Nature reviews. Immunology · 2024Review
- The role of ADAR1 through and beyond its editing activity in cancer.Cell communication and signaling : CCS · 2024Review
- Harnessing ADAR-Mediated Site-Specific RNA Editing in Immune-Related Disease: Prediction and Therapeutic Implications.International journal of molecular sciences · 2023Review
- Induction of viral mimicry upon loss of DHX9 and ADAR1 in breast cancer cells.bioRxiv : the preprint server for biology · 2023Article
- The ADAR1 editome reveals drivers of editing-specificity for ADAR1-isoforms.Nucleic acids research · 2023Article
- ADAR1 and ZBP1 in innate immunity, cell death, and disease.Trends in immunology · 2023Review
- The effects of RNA editing in cancer tissue at different stages in carcinogenesis.RNA biology · 2021Review
- Deciphering the Biological Significance of ADAR1-Z-RNA Interactions.International journal of molecular sciences · 2021Review
- ADAR1 restricts ZBP1-mediated immune response and PANoptosis to promote tumorigenesis.Cell reports · 2021Article
- RNA editing at a limited number of sites is sufficient to prevent MDA5 activation in the mouse brain.PLoS genetics · 2021Article
- Transportin-1: A Nuclear Import Receptor with Moonlighting Functions.Frontiers in molecular biosciences · 2021Review
- Programmable System of Cas13-Mediated RNA Modification and Its Biological and Biomedical Applications.Frontiers in cell and developmental biology · 2021Review
6 more citing papers are in PubMed but not listed here.
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The RNA-editing enzyme ADAR1 (adenosine deaminase that acts on RNA) is a bona fide nuclear enzyme that has been cloned from several vertebrate species. Putative nuclear localization signals (NLSs) have been identified in the aminoterminal regions of both human and Xenopus ADAR1. Here we show that neither of these predicted NLSs is biologically active. Instead, we could identify a short basic region located upstream of the RNA-binding domains of Xenopus ADAR1 to be necessary and sufficient for nuclear import. In contrast, the homologous region in human ADAR1 does not display NLS activity. Instead, we could map an NLS in human ADAR1 that overlaps with its third double-stranded RNA-binding domain. Interestingly, the NLS activity displayed by this double-stranded RNA-binding domain does not depend on RNA binding, therefore showing a dual function for this domain. Furthermore, nuclear accumulation of human (hs) ADAR1 is transcription dependent and can be stimulated by LMB, an inhibitor of Crm1-dependent nuclear export, indicating that hsADAR1 can move between the nucleus and cytoplasm. Regulated nuclear import and export of hsADAR1 can provide an excellent mechanism to control nuclear concentration of this editing enzyme thereby preventing hyperediting of structured nuclear RNAs.
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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.