ArticleNature structural & molecular biology2012
The structure of the ASAP core complex reveals the existence of a Pinin-containing PSAP complex.
Article in Nature structural & molecular biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 65 papers.
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Who cites it
65 citing papers in PubMed, 97 citations in OpenAlex.
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- ADAR1 Regulates Alternative Splicing Through an RNA Editing-Independent Mechanism.International journal of molecular sciences · 2026Article
- Anticancer Activity of the Antimicrobial Myristoylated Peptide Myr-B in HeLa Cells: Cytotoxic, Membrane-Disruptive and Proteomic Insights.International journal of molecular sciences · 2026Article
- Gene regulation through exon junction complex modularity.Nature structural & molecular biology · 2025Review
- Click-linking: a cell-compatible protein crosslinking method based on click chemistry.Nature communications · 2025Article
- Next-Generation Mapping of the ACINUS-Mediated Alternative Splicing Machinery and Its Regulation by O-glycosylation inbioRxiv : the preprint server for biology · 2025Article
- The splicing factor Acin1 is essential for embryonic development but has limited effects on muscle structure and homeostasis.Scientific reports · 2025Article
- A tale of two sugars: O-GlcNAc and O-fucose orchestrate growth, development, and acclimation in plants.Trends in biochemical sciences · 2025Review
- Nucleo-cytoplasmic distribution of SAP18 reveals its dual function in splicing regulation and heat-stress response in Arabidopsis.Plant communications · 2025Article
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- Comparative analysis of dynamic transcriptomes reveals specific COVID-19 features and pathogenesis of immunocompromised populations.mSystems · 2024Article
- Exon-junction complex association with stalled ribosomes and slow translation-independent disassembly.Nature communications · 2024Article
- The exon junction complex is required for DMD gene splicing fidelity and myogenic differentiation.Cellular and molecular life sciences : CMLS · 2024Article
- Crystal structure of the RNA-recognition motif of Drosophila melanogaster tRNA (uracil-5-)-methyltransferase homolog A.Acta crystallographica. Section F, Structural biology communications · 2024Article
- A molecular brake that modulates spliceosome pausing at detained introns contributes to neurodegeneration.Protein & cell · 2023Article
- SPINDLY mediates O-fucosylation of hundreds of proteins and sugar-dependent growth in Arabidopsis.The Plant cell · 2023Article
- DAXX adds a de novo H3.3K9me3 deposition pathway to the histone chaperone network.Molecular cell · 2023Article
- Article
5 more citing papers are in PubMed but not listed here.
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Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The ASAP complex interacts with the exon-junction complex (EJC), a messenger ribonucleoprotein complex involved in post-transcriptional regulation. The three ASAP subunits (Acinus, RNPS1 and SAP18) have been individually implicated in transcriptional regulation, pre-mRNA splicing and mRNA quality control. To shed light on the basis for and consequences of ASAP's interaction with the EJC, we have determined the 1.9-Å resolution structure of a eukaryotic ASAP core complex. The RNA-recognition motif of RNPS1 binds to a conserved motif of Acinus with a recognition mode similar to that observed in splicing U2AF proteins. The Acinus-RNPS1 platform recruits the ubiquitin-like domain of SAP18, forming a ternary complex that has both RNA- and protein-binding properties. Unexpectedly, our structural analysis identified an Acinus-like motif in Pinin, another EJC-associated splicing factor. We show that Pinin physically interacts with RNPS1 and SAP18, forming an alternative ternary complex, PSAP.
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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.