ArticleNucleic acids research2012
C6 pyridinium ceramide influences alternative pre-mRNA splicing by inhibiting protein phosphatase-1.
Article in Nucleic acids research, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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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.
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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
18 citing papers in PubMed, 29 citations in OpenAlex.
- Decoding SR protein regulation: kinases, phosphatases, and therapeutic targeting strategies.Cellular oncology (Dordrecht, Netherlands) · 2026Review
- CLCluster: A redundancy-reduction contrastive learning-based clustering method of cancer subtype based on multi-omics data.Molecular therapy. Nucleic acids · 2025Article
- Ceramide microdomains: the major influencers of the sphingolipid media platform.Biochemical Society transactions · 2024Review
- Development of Genetically Encoded Fluorescent KSR1-Based Probes to Track Ceramides during Phagocytosis.International journal of molecular sciences · 2024Article
- Neurodegenerative diseases: a hotbed for splicing defects and the potential therapies.Translational neurodegeneration · 2021Review
- Principles and Practical Considerations for the Analysis of Disease-Associated Alternative Splicing Events Using the Gateway Cloning-Based Minigene Vectors pDESTsplice and pSpliceExpress.International journal of molecular sciences · 2021Review
- Ceramide Signaling and p53 Pathways.Advances in cancer research · 2018Review
- Targeting sphingosine kinase 2 (SphK2) by ABC294640 inhibits colorectal cancer cell growth in vitro and in vivo.Journal of experimental & clinical cancer research : CR · 2015Article
- Intra-domain Cross-talk Regulates Serine-arginine Protein Kinase 1-dependent Phosphorylation and Splicing Function of Transformer 2β1.The Journal of biological chemistry · 2015Article
- Prediction of miRNA-mRNA associations in Alzheimer's disease mice using network topology.BMC genomics · 2014Article
- Recruiting a silent partner for activation of the protein kinase SRPK1.Biochemistry · 2014Article
- Functional characterization of the common c.-32-13T>G mutation of GAA gene: identification of potential therapeutic agents.Nucleic acids research · 2014Article
- Partitioning RS domain phosphorylation in an SR protein through the CLK and SRPK protein kinases.Journal of molecular biology · 2013Article
- Function of alternative splicing.Gene · 2013Review
- Phosphorylation-mediated regulation of alternative splicing in cancer.International journal of cell biology · 2013Review
- The absence of ABCD2 sensitizes mice to disruptions in lipid metabolism by dietary erucic acid.Journal of lipid research · 2012Article
- Targeting RNA splicing for disease therapy.Wiley interdisciplinary reviews. RNAReview
- PSF: nuclear busy-body or nuclear facilitator?Wiley interdisciplinary reviews. RNAReview
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
10 authors at 3 institutions in 2 countries.
Funding
Abstract
Alternative pre-mRNA processing is a central element of eukaryotic gene regulation. The cell frequently alters the use of alternative exons in response to physiological stimuli. Ceramides are lipid-signaling molecules composed of sphingosine and a fatty acid. Previously, water-insoluble ceramides were shown to change alternative splicing and decrease SR-protein phosphorylation by activating protein phosphatase-1 (PP1). To gain further mechanistical insight into ceramide-mediated alternative splicing, we analyzed the effect of C6 pyridinium ceramide (PyrCer) on alternative splice site selection. PyrCer is a water-soluble ceramide analog that is under investigation as a cancer drug. We found that PyrCer binds to the PP1 catalytic subunit and inhibits the dephosphorylation of several splicing regulatory proteins containing the evolutionarily conserved RVxF PP1-binding motif (including PSF/SFPQ, Tra2-beta1 and SF2/ASF). In contrast to natural ceramides, PyrCer promotes phosphorylation of splicing factors. Exons that are regulated by PyrCer have in common suboptimal splice sites, are unusually short and share two 4-nt motifs, GAAR and CAAG. They are dependent on PSF/SFPQ, whose phosphorylation is regulated by PyrCer. Our results indicate that lipids can influence pre-mRNA processing by regulating the phosphorylation status of specific regulatory factors, which is mediated by protein phosphatase activity.
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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.