ArticleJournal of molecular biology2015
The Signature of the Five-Stranded vRRM Fold Defined by Functional, Structural and Computational Analysis of the hnRNP L Protein.
Article in Journal of molecular biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 32 citations in OpenAlex.
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- N-terminal domain of polypyrimidine-tract binding protein is a dynamic folding platform for adaptive RNA recognition.Nucleic acids research · 2024Article
- The 100-protein NMR spectra dataset: A resource for biomolecular NMR data analysis.Scientific data · 2024Article
- Toward a Better Understanding of G4 Evolution in the 3 Living Kingdoms.Evolutionary bioinformatics online · 2023Article
- The Notch signaling pathway in skeletal muscle health and disease.Muscle & nerve · 2022Review
- Modulation of pre-mRNA structure by hnRNP proteins regulates alternative splicing ofScience advances · 2022Article
- Inferring RNA-binding protein target preferences using adversarial domain adaptation.PLoS computational biology · 2022Article
- RBM22, a Key Player of Pre-mRNA Splicing and Gene Expression Regulation, Is Altered in Cancer.Cancers · 2022Review
- Structural basis of the interaction between SETD2 methyltransferase and hnRNP L paralogs for governing co-transcriptional splicing.Nature communications · 2021Article
- The RNA-binding protein PTBP1 promotes ATPase-dependent dissociation of the RNA helicase UPF1 to protect transcripts from nonsense-mediated mRNA decay.The Journal of biological chemistry · 2020Article
- An autoinhibitory intramolecular interaction proof-reads RNA recognition by the essential splicing factor U2AF2.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Nonsense-mediated mRNA decay: The challenge of telling right from wrong in a complex transcriptome.Wiley interdisciplinary reviews. RNA · 2019Review
- hnRNP L-dependent protection of normal mRNAs from NMD subverts quality control in B cell lymphoma.The EMBO journal · 2019Article
- RRMdb-an evolutionary-oriented database of RNA recognition motif sequences.Database : the journal of biological databases and curation · 2019Article
- Oligomeric transition and dynamics of RNA binding by the HuR RRM1 domain in solution.Journal of biomolecular NMR · 2018Article
- HnRNP L represses cryptic exons.RNA (New York, N.Y.) · 2018Article
- Article
- Interplay between miR-574-3p and hnRNP L regulates VEGFA mRNA translation and tumorigenesis.Nucleic acids research · 2017Article
- Crystal structure of U2 snRNP SF3b components: Hsh49p in complex with Cus1p-binding domain.RNA (New York, N.Y.) · 2017Article
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Authors and funding
9 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The RNA recognition motif (RRM) is the far most abundant RNA binding domain. In addition to the typical β1α1β2β3α2β4 fold, various sub-structural elements have been described and reportedly contribute to the high functional versatility of RRMs. The heterogeneous nuclear ribonucleoprotein L (hnRNP L) is a highly abundant protein of 64 kDa comprising four RRM domains. Involved in many aspects of RNA metabolism, hnRNP L specifically binds to RNAs containing CA repeats or CA-rich clusters. However, a comprehensive structural description of hnRNP L including its sub-structural elements is missing. Here, we present the structural characterization of the RRM domains of hnRNP L and demonstrate their function in repressing exon 4 of SLC2A2. By comparison of the sub-structural elements between the two highly similar paralog families of hnRNP L and PTB, we defined signatures underlying interacting C-terminal coils (ICCs), the RRM34 domain interaction and RRMs with a C-terminal fifth β-strand, a variation we denoted vRRMs. Furthermore, computational analysis revealed new putative ICC-containing RRM families and allowed us to propose an evolutionary scenario explaining the origins of the ICC and fifth β-strand sub-structural extensions. Our studies provide insights of domain requirements in alternative splicing mediated by hnRNP L and molecular descriptions for the sub-structural elements. In addition, the analysis presented may help to classify other abundant RRM extensions and to predict structure-function relationships.
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