ArticleJournal of molecular biology2016
Directional Phosphorylation and Nuclear Transport of the Splicing Factor SRSF1 Is Regulated by an RNA Recognition Motif.
Article in Journal of molecular biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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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.
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Who cites it
22 citing papers in PubMed, 33 citations in OpenAlex.
- Structural basis of phosphorylation-independent nuclear import of CIRBP by TNPO3.Nature communications · 2025Article
- The splicing factor kinase, SR protein kinase 1 (SRPK1) is essential for late events in the human papillomavirus life cycle.PLoS pathogens · 2025Article
- Mycobacterial PstP impairs host RNA alternative splicing by dephosphorylation of spliceosome RBMX at S189.iMetaOmics · 2025Article
- Review
- Article
- RBM20 phosphorylation and its role in nucleocytoplasmic transport and cardiac pathogenesis.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2022Article
- Article
- Exon-independent recruitment of SRSF1 is mediated by U1 snRNP stem-loop 3.The EMBO journal · 2022Article
- AutoDock Vina 1.2.0: New Docking Methods, Expanded Force Field, and Python Bindings.Journal of chemical information and modeling · 2021Article
- CLK1 reorganizes the splicing factor U1-70K for early spliceosomal protein assembly.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- SRPK1/2 and PP1α exert opposite functions by modulating SRSF1-guided MKNK2 alternative splicing in colon adenocarcinoma.Journal of experimental & clinical cancer research : CR · 2021Article
- Accelerating AutoDock4 with GPUs and Gradient-Based Local Search.Journal of chemical theory and computation · 2021Article
- Amino Acid Composition in Various Types of Nucleic Acid-Binding Proteins.International journal of molecular sciences · 2021Review
- Structure of SRSF1 RRM1 bound to RNA reveals an unexpected bimodal mode of interaction and explains its involvement in SMN1 exon7 splicing.Nature communications · 2021Article
- Article
- Alternative Splicing in Angiogenesis.International journal of molecular sciences · 2019Review
- Distinct mechanisms govern the phosphorylation of different SR protein splicing factors.The Journal of biological chemistry · 2019Article
- Molecular interactions connecting the function of the serine-arginine-rich protein SRSF1 to protein phosphatase 1.The Journal of biological chemistry · 2018Article
- Article
- Mobilization of a splicing factor through a nuclear kinase-kinase complex.The Biochemical journal · 2018Article
Corrections and comments
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Authors and funding
9 authors at 2 institutions in 1 country.
Funding
Abstract
Multisite phosphorylation is required for the biological function of serine-arginine (SR) proteins, a family of essential regulators of mRNA splicing. These modifications are catalyzed by serine-arginine protein kinases (SRPKs) that phosphorylate numerous serines in arginine-serine-rich (RS) domains of SR proteins using a directional, C-to-N-terminal mechanism. The present studies explore how SRPKs govern this highly biased phosphorylation reaction and investigate biological roles of the observed directional phosphorylation mechanism. Using NMR spectroscopy with two separately expressed domains of SRSF1, we showed that several residues in the RNA-binding motif 2 interact with the N-terminal region of the RS domain (RS1). These contacts provide a structural framework that balances the activities of SRPK1 and the protein phosphatase PP1, thereby regulating the phosphoryl content of the RS domain. Disruption of the implicated intramolecular RNA-binding motif 2-RS domain interaction impairs both the directional phosphorylation mechanism and the nuclear translocation of SRSF1 demonstrating that the intrinsic phosphorylation bias is obligatory for SR protein biological function.
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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.