ArticleNucleic acids research2017
SUMO conjugation to spliceosomal proteins is required for efficient pre-mRNA splicing.
Article in Nucleic acids research, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
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Who cites it
37 citing papers in PubMed, 53 citations in OpenAlex.
- Assays to Study SUMOylation of RNA Helicase DHX9.Methods in molecular biology (Clifton, N.J.) · 2027Article
- Nitric oxide drives proteomic diversity through alternative splicing.Molecular cell · 2026Article
- 2'-O-methylation-dependent installation of NNature communications · 2026Article
- HDAC11 Regulates RNA Splicing via De-Fatty Acylation of SF3B2.bioRxiv : the preprint server for biology · 2026Article
- PCID2 is essential for spermatogonial differentiation by regulating alternative splicing.Cellular and molecular life sciences : CMLS · 2026Article
- SUMO conjugation to promoter-proximal sequence elements-associated proteins impacts on snRNA transcription.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Disruption of oocyte SUMOylation impacts critical regulatory processes during folliculogenesis in mice†.Biology of reproduction · 2025Article
- Review
- Integrative analysis based on ATAC-seq and RNA-seq reveals a novel oncogene PRPF3 in hepatocellular carcinoma.Clinical epigenetics · 2024Article
- DHX9 SUMOylation is required for the suppression of R-loop-associated genome instability.Nature communications · 2024Article
- Yeast Small Ubiquitin-Like Modifier (SUMO) Protease Ulp2 is Involved in RNA Splicing.Development & reproduction · 2024Article
- SRSF1 interactome determined by proximity labeling reveals direct interaction with spliceosomal RNA helicase DDX23.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Rhes, a striatal enriched protein, regulates post-translational small-ubiquitin-like-modifier (SUMO) modification of nuclear proteins and alters gene expression.Cellular and molecular life sciences : CMLS · 2024Article
- Isoginkgetin and Madrasin are poor splicing inhibitors.PloS one · 2024Article
- Article
- Regulation of Pre-mRNA Splicing: Indispensable Role of Post-Translational Modifications of Splicing Factors.Life (Basel, Switzerland) · 2023Review
- Alternative splicing of the SUMO1/2/3 transcripts affects cellular SUMOylation and produces functionally distinct SUMO protein isoforms.Scientific reports · 2023Article
- Regulation of SUMOylation on RNA metabolism in cancers.Frontiers in molecular biosciences · 2023Review
- The Cajal body marker protein coilin is SUMOylated and possesses SUMO E3 ligase-like activity.Frontiers in RNA research · 2023Article
- SUMO conjugation regulates the activity of the Integrator complex.Nucleic acids research · 2022Article
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Authors and funding
8 authors at 5 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Pre-mRNA splicing is catalyzed by the spliceosome, a multi-megadalton ribonucleoprotein machine. Previous work from our laboratory revealed the splicing factor SRSF1 as a regulator of the SUMO pathway, leading us to explore a connection between this pathway and the splicing machinery. We show here that addition of a recombinant SUMO-protease decreases the efficiency of pre-mRNA splicing in vitro. By mass spectrometry analysis of anti-SUMO immunoprecipitated proteins obtained from purified splicing complexes formed along the splicing reaction, we identified spliceosome-associated SUMO substrates. After corroborating SUMOylation of Prp3 in cultured cells, we defined Lys 289 and Lys 559 as bona fide SUMO attachment sites within this spliceosomal protein. We further demonstrated that a Prp3 SUMOylation-deficient mutant while still capable of interacting with U4/U6 snRNP components, is unable to co-precipitate U2 and U5 snRNA and the spliceosomal proteins U2-SF3a120 and U5-Snu114. This SUMOylation-deficient mutant fails to restore the splicing of different pre-mRNAs to the levels achieved by the wild type protein, when transfected into Prp3-depleted cultured cells. This mutant also shows a diminished recruitment to active spliceosomes, compared to the wild type protein. These findings indicate that SUMO conjugation plays a role during the splicing process and suggest the involvement of Prp3 SUMOylation in U4/U6•U5 tri-snRNP formation and/or recruitment.
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