ArticleNucleic acids research2020
Structural basis of UCUU RNA motif recognition by splicing factor RBM20.
Article in Nucleic acids research, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 26 citations in OpenAlex.
- Novel Truncating Variant c.1222DupC inCirculation. Genomic and precision medicine · 2026Article
- Dilated cardiomyopathy-associated RNA-binding motif protein 20 regulates long pre-mRNAs in neurons.eLife · 2026Article
- Identification of RNA processing factor LSM5 as a new adverse biomarker in nasopharyngeal carcinoma.Scientific reports · 2025Article
- Transcriptomic analysis implicates the involvement of RBM20 in Fuchs' endothelial corneal dystrophy with TCF4 repeat expansion.PloS one · 2025Article
- N-terminal domain of polypyrimidine-tract binding protein is a dynamic folding platform for adaptive RNA recognition.Nucleic acids research · 2024Article
- RNA-Binding Proteins in Cardiomyopathies.Journal of cardiovascular development and disease · 2024Review
- [Research progress on the expression of theZhongguo dang dai er ke za zhi = Chinese journal of contemporary pediatrics · 2023Review
- Article
- RBM22, a Key Player of Pre-mRNA Splicing and Gene Expression Regulation, Is Altered in Cancer.Cancers · 2022Review
- RBM20, a Therapeutic Target to Alleviate Myocardial StiffnessFrontiers in cardiovascular medicine · 2022Review
- Structural basis of PETISCO complex assembly during piRNA biogenesis inGenes & development · 2021Article
- New Insights in RBM20 Cardiomyopathy.Current heart failure reports · 2020Review
- ARIAweb: a server for automated NMR structure calculation.Nucleic acids research · 2020Article
- Alternative Splicing and CaV-Associated Channelopathies.Wiley interdisciplinary reviews. RNAReview
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Authors and funding
2 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The vertebrate splicing factor RBM20 (RNA binding motif protein 20) regulates protein isoforms important for heart development and function, with mutations in the gene linked to cardiomyopathy. Previous studies have identified the four nucleotide RNA motif UCUU as a common element in pre-mRNA targeted by RBM20. Here, we have determined the structure of the RNA Recognition Motif (RRM) domain from mouse RBM20 bound to RNA containing a UCUU sequence. The atomic details show that the RRM domain spans a larger region than initially proposed in order to interact with the complete UCUU motif, with a well-folded C-terminal helix encoded by exon 8 critical for high affinity binding. This helix only forms upon binding RNA with the final uracil, and removing the helix reduces affinity as well as specificity. We therefore find that RBM20 uses a coupled folding-binding mechanism by the C-terminal helix to specifically recognize the UCUU RNA motif.
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