ArticleScientific reports2018
Characterization of the multimeric structure of poly(A)-binding protein on a poly(A) tail.
Article in Scientific reports, 2018. 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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Who cites it
22 citing papers in PubMed, 48 citations in OpenAlex.
- Enhanced Intracellular Stability and Translation Efficiency of mRNA Drugs by a 2-arm mRNA Platform.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Cytoplasmic poly-adenosine binding proteins modulate susceptibility of mRNAs to Pumilio-mediated decay.Nucleic acids research · 2026Article
- Cytoplasmic poly-adenosine binding proteins modulate susceptibility of mRNAs to RNA-binding protein-directed decay.bioRxiv : the preprint server for biology · 2025Article
- Characterization of nuclease stability and poly(A)-binding protein binding activity of chemically modified poly(A) tail forRSC chemical biology · 2025Article
- Structural mechanism of LINE-1 target-primed reverse transcription.Science (New York, N.Y.) · 2025Article
- Branched chemically modified poly(A) tails enhance the translation capacity of mRNA.Nature biotechnology · 2025Article
- CARF regulates the alternative splicing and piwi/piRNA complexes during mouse spermatogenesis through PABPC1.Acta biochimica et biophysica Sinica · 2024Article
- LINC01197 inhibits influenza A virus replication by serving as a PABPC1 decoy.Veterinary research · 2024Article
- Germline DNA Damage Repair Gene Alterations in Patients with Metachronous Breast and Colorectal Cancer.International journal of molecular sciences · 2024Article
- PABPC1 mediates degradation ofiScience · 2024Article
- Uncovering a mammalian neural-specific poly(A) binding protein with unique properties.Genes & development · 2023Article
- Cytidine-containing tails robustly enhance and prolong protein production of synthetic mRNA in cell andMolecular therapy. Nucleic acids · 2022Article
- Molecular Insights into mRNA Polyadenylation and Deadenylation.International journal of molecular sciences · 2022Review
- Chemically Modified Poly(A) Analogs Targeting PABP: Structure Activity Relationship and Translation Inhibitory Properties.Chemistry (Weinheim an der Bergstrasse, Germany) · 2022Article
- A MademoiseLLE domain binding platform links the key RNA transporter to endosomes.PLoS genetics · 2022Article
- Nuclear and cytoplasmic poly(A) binding proteins (PABPs) favor distinct transcripts and isoforms.Nucleic acids research · 2022Article
- Paip2A inhibits translation by competitively binding to the RNA recognition motifs of PABPC1 and promoting its dissociation from the poly(A) tail.The Journal of biological chemistry · 2022Article
- Local Protein Translation and RNA Processing of Synaptic Proteins in Autism Spectrum Disorder.International journal of molecular sciences · 2021Review
- The mTOR regulated RNA-binding protein LARP1 requires PABPC1 for guided mRNA interaction.Nucleic acids research · 2021Article
- Influenza A Virus NS1 Protein Binds as a Dimer to RNA-Free PABP1 but Not to the PABP1·Poly(A) RNA Complex.Biochemistry · 2020Article
Corrections and comments
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Authors and funding
9 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Eukaryotic mature mRNAs possess a poly adenylate tail (poly(A)), to which multiple molecules of poly(A)-binding protein C1 (PABPC1) bind. PABPC1 regulates translation and mRNA metabolism by binding to regulatory proteins. To understand functional mechanism of the regulatory proteins, it is necessary to reveal how multiple molecules of PABPC1 exist on poly(A). Here, we characterize the structure of the multiple molecules of PABPC1 on poly(A), by using transmission electron microscopy (TEM), chemical cross-linking, and NMR spectroscopy. The TEM images and chemical cross-linking results indicate that multiple PABPC1 molecules form a wormlike structure in the PABPC1-poly(A) complex, in which the PABPC1 molecules are linearly arrayed. NMR and cross-linking analyses indicate that PABPC1 forms a multimer by binding to the neighbouring PABPC1 molecules via interactions between the RNA recognition motif (RRM) 2 in one molecule and the middle portion of the linker region of another molecule. A PABPC1 mutant lacking the interaction site in the linker, which possesses an impaired ability to form the multimer, reduced the in vitro translation activity, suggesting the importance of PABPC1 multimer formation in the translation process. We therefore propose a model of the PABPC1 multimer that provides clues to comprehensively understand the regulation mechanism of mRNA translation.
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