ArticleMolecular and cellular biology2001
Domains in human splicing factors SF3a60 and SF3a66 required for binding to SF3a120, assembly of the 17S U2 snRNP, and prespliceosome formation.
Article in Molecular and cellular biology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed, 54 citations in OpenAlex.
- Pharmacological targeting of SF3a1-MDM4 splicing vulnerability in ovarian cancer with rifaximin and antisense oligonucleotide.Journal of translational medicine · 2026Article
- Integrating CORUM and co-fractionation mass spectrometry to create enhanced benchmarks for protein complex predictions.Briefings in bioinformatics · 2025Article
- Article
- Review
- Structural insights into branch site proofreading by human spliceosome.Nature structural & molecular biology · 2024Article
- SF3A2 promotes progression and cisplatin resistance in triple-negative breast cancer via alternative splicing of MKRN1.Science advances · 2024Article
- Phylogenetic Analysis of Spliceosome SF3a2 in Different Plant Species.International journal of molecular sciences · 2023Article
- Structural basis for the interaction between the first SURP domain of the SF3A1 subunit in U2 snRNP and the human splicing factor SF1.Protein science : a publication of the Protein Society · 2022Article
- Splicing of branchpoint-distant exons is promoted by Cactin, Tls1 and the ubiquitin-fold-activated Sde2.Nucleic acids research · 2022Article
- Sequence-specific RNA recognition by an RGG motif connects U1 and U2 snRNP for spliceosome assembly.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- The integral spliceosomal component CWC15 is required for development in Arabidopsis.Scientific reports · 2020Article
- Identification of a noncanonical RNA binding domain in the U2 snRNP protein SF3A1.RNA (New York, N.Y.) · 2019Article
- The Sm-core mediates the retention of partially-assembled spliceosomal snRNPs in Cajal bodies until their full maturation.Nucleic acids research · 2018Article
- Protein interaction network of alternatively spliced NudCD1 isoforms.Scientific reports · 2017Article
- Structure of a pre-catalytic spliceosome.Nature · 2017Article
- Mammalian splicing factor SF1 interacts with SURP domains of U2 snRNP-associated proteins.Nucleic acids research · 2015Article
- Age-related nuclear translocation of P2X6 subunit modifies splicing activity interacting with splicing factor 3A1.PloS one · 2015Article
- Stem-loop 4 of U1 snRNA is essential for splicing and interacts with the U2 snRNP-specific SF3A1 protein during spliceosome assembly.Genes & development · 2014Article
- Proteins associated with SF3a60 in T. brucei.PloS one · 2014Article
- Limiting of the innate immune response by SF3A-dependent control of MyD88 alternative mRNA splicing.PLoS genetics · 2013Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The active 17S U2 small nuclear ribonucleoprotein particle (snRNP), which binds to the intron branch site during the formation of the prespliceosome, is assembled in vitro by sequential interactions of the essential splicing factors SF3b and SF3a with the 12S U2 snRNP. We have analyzed the function of individual subunits of human SF3a (SF3a60, SF3a66, and SF3a120) by testing recombinant proteins, expressed in insect cells, in various in vitro assays. The recombinant subunits readily form the SF3a heterotrimer, where SF3a60 and SF3a66 interact with SF3a120, but not with each other. All SF3a subunits are essential for the formation of the mature 17S U2 snRNP and the prespliceosome. Single subunits engage in interactions with the 15S U2 snRNP (consisting of the 12S U2 snRNP and SF3b), and SF3a60 appears to play a major role in recruiting SF3a120 into the U2 particle. Analysis of functional domains in SF3a60 and SF3a66 identified interaction sites for SF3a120 in their N-terminal portions. C(2)H(2)-type zinc finger domains mediate the integration of SF3a60 and SF3a66 into the U2 snRNP, and we propose a model in which protein-protein interactions between the zinc finger domains and the Sm proteins, common to all spliceosomal snRNPs, contribute to the assembly of the 17S U2 snRNP. Finally, we demonstrate that all domains required for interactions within the SF3a heterotrimer and the formation of the 17S U2 snRNP are also necessary to assemble the prespliceosome.
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