ArticleThe Biochemical journal2015
Conserved proline-directed phosphorylation regulates SR protein conformation and splicing function.
Article in The Biochemical journal, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed, 58 citations in OpenAlex.
- Tracking cellular biomolecular condensate dynamics under proteostatic stress with middle-down phosphoproteomics.bioRxiv : the preprint server for biology · 2026Article
- Decoding SR protein regulation: kinases, phosphatases, and therapeutic targeting strategies.Cellular oncology (Dordrecht, Netherlands) · 2026Review
- Functions of SRPK, CLK and DYRK kinases in stem cells, development, and human developmental disorders.FEBS letters · 2023Review
- Towards understandings of serine/arginine-rich splicing factors.Acta pharmaceutica Sinica. B · 2023Review
- Cdc2-like kinases: structure, biological function, and therapeutic targets for diseases.Signal transduction and targeted therapy · 2023Review
- Phosphorylation mediated regulation of RNA splicing in plants.Frontiers in plant science · 2023Review
- Genome-scale analysis of Arabidopsis splicing-related protein kinase families reveals roles in abiotic stress adaptation.BMC plant biology · 2022Article
- Skeletal muscle-specific overexpression of miR-486 limits mammary tumor-induced skeletal muscle functional limitations.Molecular therapy. Nucleic acids · 2022Article
- Profiling the Human Phosphoproteome to Estimate the True Extent of Protein Phosphorylation.Journal of proteome research · 2022Article
- Phosphorylation regulates arginine-rich RNA-binding protein solubility and oligomerization.The Journal of biological chemistry · 2021Article
- Identification of Nrl1 Domains Responsible for Interactions with RNA-Processing Factors and Regulation of Nrl1 Function by Phosphorylation.International journal of molecular sciences · 2021Article
- A novel class of inhibitors that target SRSF10 and promote p53-mediated cytotoxicity on human colorectal cancer cells.NAR cancer · 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
- New Insights in RBM20 Cardiomyopathy.Current heart failure reports · 2020Review
- Arginine-Enriched Mixed-Charge Domains Provide Cohesion for Nuclear Speckle Condensation.Molecular cell · 2020Article
- Disordered protein interactions for an ordered cellular transition: Cdc2-like kinase 1 is transported to the nucleus via its Ser-Arg protein substrate.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
- Mobilization of a splicing factor through a nuclear kinase-kinase complex.The Biochemical journal · 2018Article
- Redirecting SR Protein Nuclear Trafficking through an Allosteric Platform.Journal of molecular biology · 2017Article
- The Critical Role of SRPK1 in EMT of Human Glioblastoma in the Spinal Cord.Molecular neurobiology · 2017Article
Corrections and comments
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
Abstract
The alternative splicing of human genes is dependent on SR proteins, a family of essential splicing factors whose name derives from a signature C-terminal domain rich in arginine-serine dipeptide repeats (RS domains). Although the SRPKs (SR-specific protein kinases) phosphorylate these repeats, RS domains also contain prolines with flanking serines that are phosphorylated by a second family of protein kinases known as the CLKs (Cdc2-like kinases). The role of specific serine-proline phosphorylation within the RS domain has been difficult to assign since CLKs also phosphorylate arginine-serine dipeptides and, thus, display overlapping residue specificities with the SRPKs. In the present study, we address the effects of discrete serine-proline phosphorylation on the conformation and cellular function of the SR protein SRSF1 (SR protein splicing factor 1). Using chemical tagging and dephosphorylation experiments, we show that modification of serine-proline dipeptides broadly amplifies the conformational ensemble of SRSF1. The induction of these new structural forms triggers SRSF1 mobilization in the nucleus and alters its binding mechanism to an exonic splicing enhancer in precursor mRNA. These physical events correlate with changes in the alternative splicing of over 100 human genes based on a global splicing assay. Overall, these studies draw a direct causal relationship between a specific type of chemical modification in an SR protein and the regulation of alternative gene splicing programmes.
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