ArticlePloS one2014
Eukaryotic initiation factor 4G suppresses nonsense-mediated mRNA decay by two genetically separable mechanisms.
Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers, 1 of them a synthesis that pooled it.
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Who cites it
28 citing papers in PubMed, 1 synthesis or guideline pooled it, 48 citations in OpenAlex.
- PABPC1--mRNA stability, protein translation and tumorigenesis.Frontiers in oncology · 2022Pooled it
- Eukaryotic translation initiation factor 4F: functional properties and physiological role.Nucleic acids research · 2025Review
- Eukaryotic initiation factors eIF4F and eIF4B promote translation termination upon closed-loop formation.Nucleic acids research · 2025Article
- Differences in gene expression between high and low tolerance rainbow trout (Oncorhynchus mykiss) to acute thermal stress.PloS one · 2025Article
- EIF4A3-mediated biogenesis of circSTX6 promotes bladder cancer metastasis and cisplatin resistance.Journal of experimental & clinical cancer research : CR · 2024Article
- Features and factors that dictate if terminating ribosomes cause or counteract nonsense-mediated mRNA decay.The Journal of biological chemistry · 2022Review
- Gene Variants Involved in Nonsense-Mediated mRNA Decay Suggest a Role in Autism Spectrum Disorder.Biomedicines · 2022Article
- Tethered Function Assays to Elucidate the Role of RNA-Binding Proteins.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Human NMD ensues independently of stable ribosome stalling.Nature communications · 2020Article
- UPF1-Mediated RNA Decay-Danse Macabre in a Cloud.Biomolecules · 2020Review
- The Interactome analysis of the Respiratory Syncytial Virus protein M2-1 suggests a new role in viral mRNA metabolism post-transcription.Scientific reports · 2019Article
- Article
- Quality and quantity control of gene expression by nonsense-mediated mRNA decay.Nature reviews. Molecular cell biology · 2019Review
- Nonsense-Mediated mRNA Decay Begins Where Translation Ends.Cold Spring Harbor perspectives in biology · 2019Review
- New insights into the interplay between the translation machinery and nonsense-mediated mRNA decay factors.Biochemical Society transactions · 2018Review
- Dissecting the functions of SMG5, SMG7, and PNRC2 in nonsense-mediated mRNA decay of human cells.RNA (New York, N.Y.) · 2018Article
- Arc 3' UTR Splicing Leads to Dual and Antagonistic Effects in Fine-Tuning Arc Expression Upon BDNF Signaling.Frontiers in molecular neuroscience · 2018Article
- Embraced by eIF3: structural and functional insights into the roles of eIF3 across the translation cycle.Nucleic acids research · 2017Article
- Transcript-specific characteristics determine the contribution of endo- and exonucleolytic decay pathways during the degradation of nonsense-mediated decay substrates.RNA (New York, N.Y.) · 2017Article
- Harnessing short poly(A)-binding protein-interacting peptides for the suppression of nonsense-mediated mRNA decay.Scientific reports · 2016Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Nonsense-mediated mRNA decay (NMD), which is best known for degrading mRNAs with premature termination codons (PTCs), is thought to be triggered by aberrant translation termination at stop codons located in an environment of the mRNP that is devoid of signals necessary for proper termination. In mammals, the cytoplasmic poly(A)-binding protein 1 (PABPC1) has been reported to promote correct termination and therewith antagonize NMD by interacting with the eukaryotic release factors 1 (eRF1) and 3 (eRF3). Using tethering assays in which proteins of interest are recruited as MS2 fusions to a NMD reporter transcript, we show that the three N-terminal RNA recognition motifs (RRMs) of PABPC1 are sufficient to antagonize NMD, while the eRF3-interacting C-terminal domain is dispensable. The RRM1-3 portion of PABPC1 interacts with eukaryotic initiation factor 4G (eIF4G) and tethering of eIF4G to the NMD reporter also suppresses NMD. We identified the interactions of the eIF4G N-terminus with PABPC1 and the eIF4G core domain with eIF3 as two genetically separable features that independently enable tethered eIF4G to inhibit NMD. Collectively, our results reveal a function of PABPC1, eIF4G and eIF3 in translation termination and NMD suppression, and they provide additional evidence for a tight coupling between translation termination and initiation.
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