ArticleNature communications2016
An extended U2AF(65)-RNA-binding domain recognizes the 3' splice site signal.
Article in Nature communications, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.
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Who cites it
46 citing papers in PubMed, 76 citations in OpenAlex.
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- Genome-scale functional mapping of the mammalian whole brain with in vivo Perturb-seq.bioRxiv : the preprint server for biology · 2026Article
- Genome-wide modulation of alternative splicing by a predicted alpha helix in U2AF2.Nucleic acids research · 2025Article
- Recurrent Neurodevelopmentally Associated Variants of the Pre-mRNA Splicing Factor U2AF2 Alter RNA Binding Affinities and Interactions.Biochemistry · 2024Article
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- Splicing of branchpoint-distant exons is promoted by Cactin, Tls1 and the ubiquitin-fold-activated Sde2.Nucleic acids research · 2022Article
- The Role of RNA-Binding Proteins in Hematological Malignancies.International journal of molecular sciences · 2022Review
- Modulation of pre-mRNA structure by hnRNP proteins regulates alternative splicing ofScience advances · 2022Article
- Pre-mRNA splicing factor U2AF2 recognizes distinct conformations of nucleotide variants at the center of the pre-mRNA splice site signal.Nucleic acids research · 2022Article
- Review
- Precision analysis of mutant U2AF1 activity reveals deployment of stress granules in myeloid malignancies.Molecular cell · 2022Article
- Evolution of the Early Spliceosomal Complex-From Constitutive to Regulated Splicing.International journal of molecular sciences · 2021Review
- Interleukin enhancer-binding factor 2 promotes cell proliferation and DNA damage response in metastatic melanoma.Clinical and translational medicine · 2021Article
- A synthetic small molecule stalls pre-mRNA splicing by promoting an early-stage U2AF2-RNA complex.Cell chemical biology · 2021Article
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
Abstract
How the essential pre-mRNA splicing factor U2AF(65) recognizes the polypyrimidine (Py) signals of the major class of 3' splice sites in human gene transcripts remains incompletely understood. We determined four structures of an extended U2AF(65)-RNA-binding domain bound to Py-tract oligonucleotides at resolutions between 2.0 and 1.5 Å. These structures together with RNA binding and splicing assays reveal unforeseen roles for U2AF(65) inter-domain residues in recognizing a contiguous, nine-nucleotide Py tract. The U2AF(65) linker residues between the dual RNA recognition motifs (RRMs) recognize the central nucleotide, whereas the N- and C-terminal RRM extensions recognize the 3' terminus and third nucleotide. Single-molecule FRET experiments suggest that conformational selection and induced fit of the U2AF(65) RRMs are complementary mechanisms for Py-tract association. Altogether, these results advance the mechanistic understanding of molecular recognition for a major class of splice site signals.
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