ArticleMolecular and cellular biology2007
Sumoylation modulates the assembly and activity of the pre-mRNA 3' processing complex.
Article in Molecular and cellular biology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.
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Who cites it
39 citing papers in PubMed, 57 citations in OpenAlex.
- SUMO2 promotes histone pre-mRNA processing by stabilizing histone locus body interactions and facilitating U7 snRNP assembly.Genes & development · 2025Article
- 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
- Isoginkgetin and Madrasin are poor splicing inhibitors.PloS one · 2024Article
- Molecular details of the CPSF73-CPSF100 C-terminal heterodimer and interaction with Symplekin.Open biology · 2023Article
- Regulation of Pre-mRNA Splicing: Indispensable Role of Post-Translational Modifications of Splicing Factors.Life (Basel, Switzerland) · 2023Review
- Regulation of SUMOylation on RNA metabolism in cancers.Frontiers in molecular biosciences · 2023Review
- SUMO conjugation regulates the activity of the Integrator complex.Nucleic acids research · 2022Article
- Targeting the mRNA endonuclease CPSF73 inhibits breast cancer cell migration, invasion, and self-renewal.iScience · 2022Article
- Coordination of RNA Processing Regulation by Signal Transduction Pathways.Biomolecules · 2021Review
- On the Cutting Edge: Regulation and Therapeutic Potential of the mRNA 3' End Nuclease.Trends in biochemical sciences · 2021Review
- SUMO Modification of OsFKBP20-1b Is Integral to Proper Pre-mRNA Splicing upon Heat Stress in Rice.International journal of molecular sciences · 2021Article
- A Complex of U1 snRNP with Cleavage and Polyadenylation Factors Controls Telescripting, Regulating mRNA Transcription in Human Cells.Molecular cell · 2019Article
- When SUMO met splicing.RNA biology · 2018Review
- Zinc Finger-Containing Cellular Transcription Corepressor ZBTB25 Promotes Influenza Virus RNA Transcription and Is a Target for Zinc Ejector Drugs.Journal of virology · 2017Article
- SUMO conjugation to spliceosomal proteins is required for efficient pre-mRNA splicing.Nucleic acids research · 2017Article
- Roles of Sumoylation in mRNA Processing and Metabolism.Advances in experimental medicine and biology · 2017Review
- SUMO-Modification of the La Protein Facilitates Binding to mRNA In Vitro and in Cells.PloS one · 2016Article
- Efficient mRNA polyadenylation requires a ubiquitin-like domain, a zinc knuckle, and a RING finger domain, all contained in the Mpe1 protein.Molecular and cellular biology · 2014Article
- Article
- Multiple crosstalks between mRNA biogenesis and SUMO.Chromosoma · 2013Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Eukaryotic pre-mRNA 3'-end formation is catalyzed by a complex set of factors that must be intricately regulated. In this study, we have discovered a novel role for the small ubiquitin-like modifier SUMO in the regulation of mammalian 3'-end processing. We identified symplekin, a factor involved in complex assembly, and CPSF-73, an endonuclease, as SUMO modification substrates. The major sites of sumoylation in symplekin and CPSF-73 were determined and found to be highly conserved across species. A sumoylation-deficient mutant was defective in rescuing cell viability in symplekin small interfering RNA (siRNA)-treated cells, supporting the importance of this modification in symplekin function. We also analyzed the involvement of sumoylation in 3'-end processing by altering the sumoylation status of nuclear extracts. This was done by the addition of a SUMO protease, which we show interacts with both symplekin and CPSF-73, or by siRNA-mediated depletion of ubc9, the SUMO E2-conjugating enzyme. Both treatments resulted in a marked inhibition of processing. The assembly of a functional polyadenylation complex was also impaired by the SUMO protease. Our identification of two key polyadenylation factors as SUMO targets and of the role of SUMO in enhancing the assembly and activity of the 3'-end-processing complex together reveal an important function for SUMO in the processing of mRNA precursors.
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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.