ArticleThe Journal of biological chemistry2011
Interaction domains and nuclear targeting signals in subunits of the U2 small nuclear ribonucleoprotein particle-associated splicing factor SF3a.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 14 citations in OpenAlex.
- SF3A2: a promising therapeutic target and predictive biomarker for immunotherapy in colorectal cancer.International journal of medical sciences · 2026Article
- Review
- 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
- 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
- Tyramide signal amplification mass spectrometry (TSA-MS) ratio identifies nuclear speckle proteins.The Journal of cell biology · 2020Article
- Identification of a noncanonical RNA binding domain in the U2 snRNP protein SF3A1.RNA (New York, N.Y.) · 2019Article
- Mammalian splicing factor SF1 interacts with SURP domains of U2 snRNP-associated proteins.Nucleic acids research · 2015Article
- Limiting of the innate immune response by SF3A-dependent control of MyD88 alternative mRNA splicing.PLoS genetics · 2013Article
- Structure and assembly of the SF3a splicing factor complex of U2 snRNP.The EMBO journal · 2012Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Human splicing factor SF3a is a component of the mature U2 small nuclear ribonucleoprotein particle (snRNP) and its three subunits of 60, 66, and 120 kDa are essential for splicing in vitro and in vivo. The SF3a heterotrimer forms in the cytoplasm and enters the nucleus independently of the U2 snRNP. Here, we have analyzed domains required for in vitro interactions between the SF3a subunits. Our results indicate that the SF3a66-SF3a120 interaction is mediated by a 27-amino acid region in SF3a120 C-terminal to the second suppressor-of-white-apricot and prp21/spp91 domain and amino acids 108-210 of SF3a66. Neither of these sequences contains known structural motifs, suggesting that the interaction domains are novel. Moreover, an ∼100-amino acid region, including the SURP2 domain of SF3a120 but extending into neighboring regions, is sufficient for binding to SF3a60. Analysis of determinants for nuclear import of SF3a demonstrates that SF3a120 provides the major nuclear localization signal and SF3a60 contributes to nuclear import.
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