ArticleNucleic acids research2016
Human nonsense-mediated mRNA decay factor UPF2 interacts directly with eRF3 and the SURF complex.
Article in Nucleic acids research, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.
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Who cites it
40 citing papers in PubMed, 60 citations in OpenAlex.
- Mechanistic insights into recruitment and regulation of the RNA helicase UPF1 in replication-dependent histone mRNA decay.Nature communications · 2026Article
- Nonsense-mediated mRNA decay and associated splicing patterns in neurodevelopmental disorders.Frontiers in molecular biosciences · 2026Review
- Synergistic Methods to Investigate Eukaryotic Translation and Its Quality Control.Journal of molecular biology · 2025Review
- RBM8A promotes gastric cancer progression by binding with UPF3B to induce BBC3 mRNA degradation.International journal of molecular medicine · 2025Article
- Nonsense-Mediated mRNA Decay in Human Health and Diseases: Current Understanding, Regulatory Mechanisms and Future Perspectives.Molecular biotechnology · 2025Review
- Dynamic RNA binding and unfolding by nonsense-mediated mRNA decay factor UPF2.RNA (New York, N.Y.) · 2025Article
- Modulation of UPF1 catalytic activity upon interaction of SARS-CoV-2 Nucleocapsid protein with factors involved in nonsense mediated-mRNA decay.Nucleic acids research · 2024Article
- Disrupted Post-Transcriptional Regulation of Gene Expression as a Hallmark of Fatty Liver Progression.International journal of molecular sciences · 2024Article
- A systematic search for RNA structural switches across the human transcriptome.Nature methods · 2024Article
- Therapeutic Nonsense Suppression Modalities: From Small Molecules to Nucleic Acid-Based Approaches.Biomedicines · 2024Review
- Characterization of the mIF4G Domains in the RNA Surveillance Protein Upf2p.Current issues in molecular biology · 2023Article
- Translation-coupled mRNA quality control mechanisms.The EMBO journal · 2023Review
- Emerging Personalized Opportunities for Enhancing Translational Readthrough in Rare Genetic Diseases and Beyond.International journal of molecular sciences · 2023Review
- Nonsense-Mediated mRNA Decay Factor Functions in Human Health and Disease.Biomedicines · 2023Review
- Modulation of RNA-binding properties of the RNA helicase UPF1 by its activator UPF2.RNA (New York, N.Y.) · 2023Article
- Ribosome-bound Upf1 forms distinct 80S complexes and conducts mRNA surveillance.RNA (New York, N.Y.) · 2022Article
- Features and factors that dictate if terminating ribosomes cause or counteract nonsense-mediated mRNA decay.The Journal of biological chemistry · 2022Review
- Diverse Roles of the Exon Junction Complex Factors in the Cell Cycle, Cancer, and Neurodevelopmental Disorders-Potential for Therapeutic Targeting.International journal of molecular sciences · 2022Review
- No-nonsense: insights into the functional interplay of nonsense-mediated mRNA decay factors.The Biochemical journal · 2022Review
- Structure-guided design enables development of a hyperpolarized molecular probe for the detection of aminopeptidase N activity in vivo.Science advances · 2022Article
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Authors and funding
12 authors at 5 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Nonsense-mediated mRNA decay (NMD) is an mRNA degradation pathway that regulates gene expression and mRNA quality. A complex network of macromolecular interactions regulates NMD initiation, which is only partially understood. According to prevailing models, NMD begins by the assembly of the SURF (SMG1-UPF1-eRF1-eRF3) complex at the ribosome, followed by UPF1 activation by additional factors such as UPF2 and UPF3. Elucidating the interactions between NMD factors is essential to comprehend NMD, and here we demonstrate biochemically and structurally the interaction between human UPF2 and eukaryotic release factor 3 (eRF3). In addition, we find that UPF2 associates with SURF and ribosomes in cells, in an UPF3-independent manner. Binding assays using a collection of UPF2 truncated variants reveal that eRF3 binds to the C-terminal part of UPF2. This region of UPF2 is partially coincident with the UPF3-binding site as revealed by electron microscopy of the UPF2-eRF3 complex. Accordingly, we find that the interaction of UPF2 with UPF3b interferes with the assembly of the UPF2-eRF3 complex, and that UPF2 binds UPF3b more strongly than eRF3. Together, our results highlight the role of UPF2 as a platform for the transient interactions of several NMD factors, including several components of SURF.
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