ArticleNature structural & molecular biology2014
RBFOX and SUP-12 sandwich a G base to cooperatively regulate tissue-specific splicing.
Article in Nature structural & molecular biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers, 1 of them a synthesis that pooled it.
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Who cites it
15 citing papers in PubMed, 1 synthesis or guideline pooled it, 32 citations in OpenAlex.
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- The Rbfox1/LASR complex controls alternative pre-mRNA splicing by recognition of multipart RNA regulatory modules.Genes & development · 2025Article
- Rbm38 Reduces the Transcription Elongation Defect of theInternational journal of molecular sciences · 2020Article
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- mRNA Editing, Processing and Quality Control inGenetics · 2020Review
- The combinatorial control of alternative splicing in C. elegans.PLoS genetics · 2017Article
- RBM24 promotes U1 snRNP recognition of the mutated 5' splice site in theRNA (New York, N.Y.) · 2017Article
- Protein 4.1R Exon 16 3' Splice Site Activation Requires Coordination among TIA1, Pcbp1, and RBM39 during Terminal Erythropoiesis.Molecular and cellular biology · 2017Article
- Splicing factors control C. elegans behavioural learning in a single neuron by producing DAF-2c receptor.Nature communications · 2016Article
- Article
- Evidence for cooperative tandem binding of hnRNP C RRMs in mRNA processing.RNA (New York, N.Y.) · 2015Article
- Evolutionary Conservation and Functional Diversification of the Rbm24/38 Family in Metazoans.Wiley interdisciplinary reviews. RNAReview
- Article
Corrections and comments
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Authors and funding
15 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Tissue-specific alternative pre-mRNA splicing is often cooperatively regulated by multiple splicing factors, but the structural basis of cooperative RNA recognition is poorly understood. In Caenorhabditis elegans, ligand binding specificity of fibroblast growth factor receptors (FGFRs) is determined by mutually exclusive alternative splicing of the sole FGFR gene, egl-15. Here we determined the solution structure of a ternary complex of the RNA-recognition motif (RRM) domains from the RBFOX protein ASD-1, SUP-12 and their target RNA from egl-15. The two RRM domains cooperatively interact with the RNA by sandwiching a G base to form the stable complex. Multichromatic fluorescence splicing reporters confirmed the requirement of the G and the juxtaposition of the respective cis elements for effective splicing regulation in vivo. Moreover, we identified a new target for the heterologous complex through an element search, confirming the functional significance of the intermolecular coordination.
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