ArticleGenes & development2006
RS domains contact splicing signals and promote splicing by a common mechanism in yeast through humans.
Article in Genes & development, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 70 papers.
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Who cites it
70 citing papers in PubMed, 155 citations in OpenAlex.
- Alternative Splicing of Pre-mRNA Matters in Oral Diseases.Current gene therapy · 2025Review
- PDGFRα signaling regulates Srsf3 transcript binding to affect PI3K signaling and endosomal trafficking.eLife · 2024Article
- RNA-Binding Protein-Mediated Alternative Splicing Regulates Abiotic Stress Responses in Plants.International journal of molecular sciences · 2024Review
- PDGFRα signaling regulates Srsf3 transcript binding to affect PI3K signaling and endosomal trafficking.bioRxiv : the preprint server for biology · 2024Article
- RNA export through the nuclear pore complex is directional.Nature communications · 2022Article
- Expansion and functional analysis of the SR-related protein family across the domains of life.RNA (New York, N.Y.) · 2022Article
- SRSF6 Regulates the Alternative Splicing of the Apoptotic Fas Gene by Targeting a Novel RNA Sequence.Cancers · 2022Article
- Exon-independent recruitment of SRSF1 is mediated by U1 snRNP stem-loop 3.The EMBO journal · 2022Article
- Article
- The RNA-binding profile of the splicing factor SRSF6 in immortalized human pancreatic β-cells.Life science alliance · 2021Article
- Relative strength of 5' splice-site strength defines functions of SRSF2 and SRSF6 in alternative splicing of Bcl-x pre-mRNA.BMB reports · 2021Article
- Structure of SRSF1 RRM1 bound to RNA reveals an unexpected bimodal mode of interaction and explains its involvement in SMN1 exon7 splicing.Nature communications · 2021Article
- Interplay Between CMGC Kinases Targeting SR Proteins and Viral Replication: Splicing and Beyond.Frontiers in microbiology · 2021Review
- Systematic characterization of the branch point binding protein, splicing factor 1, gene family in plant development and stress responses.BMC plant biology · 2020Article
- A splice site-sensing conformational switch in U2AF2 is modulated by U2AF1 and its recurrent myelodysplasia-associated mutation.Nucleic acids research · 2020Article
- Genome-wide evolution of wobble base-pairing nucleotides of branchpoint motifs with increasing organismal complexity.RNA biology · 2020Article
- Genome-wide identification and expression analysis of the SR gene family in longan (Dimocarpus longan Lour.).PloS one · 2020Article
- The mechanisms of a mammalian splicing enhancer.Nucleic acids research · 2018Article
- PhysiologicalBlood · 2018Article
- Integration of mRNP formation and export.Cellular and molecular life sciences : CMLS · 2017Review
10 more citing papers are in PubMed but not listed here.
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Serine-arginine (SR) proteins are general metazoan splicing factors that contain an essential arginine-serine-rich (RS) domain. We have previously found that mammalian spliceosome assembly involves a series of sequential interactions between RS domains and two splicing signals: the branchpoint and the 5' splice site. Here we study how RS domains are directed to specifically contact splicing signals, and how this interaction promotes splicing. The yeast Saccharomyces cerevisiae lacks SR proteins. However, we show that tethering a mammalian RS domain to a yeast actin pre-mRNA rescues splicing of certain branchpoint or 5' splice site mutants in which U snRNA base-pairing has been decreased. Conversely, on a mammalian pre-mRNA, a normally essential SR protein becomes dispensable when the complementarity of a splicing signal to a U snRNA is increased. We find that in the absence of other splicing factors an RS domain tethered to a pre-mRNA selectively contacts a double-stranded RNA region and enhances RNA-RNA base-pairing. Significantly, all of these activities require phosphorylation of the RS domain. Based on these results, we propose that RS domains selectively contact splicing signals because, due to transient U snRNA base-pairing, they are partially double-stranded. The RS domain-splicing signal interaction, in turn, promotes (or stabilizes) base-pairing between the U snRNA and pre-mRNA substrate, thereby enhancing splicing. Our results reveal a common mechanism of RS domain function in yeast through humans.
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Registered trials
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.