ArticleThe FEBS journal2006
Major phosphorylation of SF1 on adjacent Ser-Pro motifs enhances interaction with U2AF65.
Article in The FEBS journal, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
38 citing papers in PubMed, 55 citations in OpenAlex.
- Nitric oxide drives proteomic diversity through alternative splicing.Molecular cell · 2026Article
- U2AF2 controls alternative splicing in speckle-proximal regions in an RS domain-dependent manner.Nucleic acids research · 2026Article
- UHMK1 Promotes Prostate Cancer Progression through a Positive Feedback Loop with MTHFD2.Oncology research · 2025Article
- Mobilisation of jerboa kidney gene networks during dehydration and opportunistic rehydration.iScience · 2023Article
- Regulation of Pre-mRNA Splicing: Indispensable Role of Post-Translational Modifications of Splicing Factors.Life (Basel, Switzerland) · 2023Review
- UHMK1 Is a Novel Marker for Personalized Prediction of Pancreatic Cancer Prognosis.Frontiers in oncology · 2022Article
- Identification of Nrl1 Domains Responsible for Interactions with RNA-Processing Factors and Regulation of Nrl1 Function by Phosphorylation.International journal of molecular sciences · 2021Article
- Systematic characterization of the branch point binding protein, splicing factor 1, gene family in plant development and stress responses.BMC plant biology · 2020Article
- U2AFEMBO reports · 2019Article
- Review
- The pre-mRNA splicing and transcription factor Tat-SF1 is a functional partner of the spliceosome SF3b1 subunit via a U2AF homology motif interface.The Journal of biological chemistry · 2019Article
- PUF60-activated exons uncover altered 3' splice-site selection by germline missense mutations in a single RRM.Nucleic acids research · 2018Article
- Cancer-Associated Mutations Mapped on High-Resolution Structures of the U2AF2 RNA Recognition Motifs.Biochemistry · 2017Article
- SF1 Phosphorylation Enhances Specific Binding to U2AFBiophysical journal · 2016Article
- Unmasking the U2AF homology motif family: a bona fide protein-protein interaction motif in disguise.RNA (New York, N.Y.) · 2016Review
- Recognition of the 3' splice site RNA by the U2AF heterodimer involves a dynamic population shift.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- UHM-ULM interactions in the RBM39-U2AF65 splicing-factor complex.Acta crystallographica. Section D, Structural biology · 2016Article
- Mammalian splicing factor SF1 interacts with SURP domains of U2 snRNP-associated proteins.Nucleic acids research · 2015Article
- Diverse regulation of 3' splice site usage.Cellular and molecular life sciences : CMLS · 2015Review
- SR protein kinases promote splicing of nonconsensus introns.Nature structural & molecular biology · 2015Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 4 institutions in 2 countries.
Funding
Abstract
Protein phosphorylation ensures the accurate and controlled expression of the genome, for instance by regulating the activities of pre-mRNA splicing factors. Here we report that splicing factor 1 (SF1), which is involved in an early step of intronic sequence recognition, is highly phosphorylated in mammalian cells on two serines within an SPSP motif at the junction between its U2AF65 and RNA binding domains. We show that SF1 interacts in vitro with the protein kinase KIS, which possesses a 'U2AF homology motif' (UHM) domain. The UHM domain of KIS is required for KIS and SF1 to interact, and for KIS to efficiently phosphorylate SF1 on the SPSP motif. Importantly, SPSP phosphorylation by KIS increases binding of SF1 to U2AF65, and enhances formation of the ternary SF1-U2AF65-RNA complex. These results further suggest that this phosphorylation event has an important role for the function of SF1, and possibly for the structural rearrangements associated with spliceosome assembly and function.
Indexed as
Identifiers
What OpenQuestion holds
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.