ArticleNucleic acids research2013
The RNA helicase Ddx5/p68 binds to hUpf3 and enhances NMD of Ddx17/p72 and Smg5 mRNA.
Article in Nucleic acids research, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 39 citations in OpenAlex.
- METTL1-modulated LSM14A facilitates proliferation and migration in glioblastoma via the stabilization of DDX5.iScience · 2024Article
- Modulatory role of RNA helicases in MBNL-dependent alternative splicing regulation.Cellular and molecular life sciences : CMLS · 2023Article
- Hypoxia-mediated regulation of DDX5 through decreased chromatin accessibility and post-translational targeting restricts R-loop accumulation.Molecular oncology · 2023Article
- Synthetic lethal interactions of DEAD/H-box helicases as targets for cancer therapy.Frontiers in oncology · 2022Review
- DDX5 and DDX17-multifaceted proteins in the regulation of tumorigenesis and tumor progression.Frontiers in oncology · 2022Review
- RNA Helicase DDX17 Inhibits Hepatitis B Virus Replication by Blocking Viral Pregenomic RNA Encapsidation.Journal of virology · 2021Article
- De novo missense variants disrupting protein-protein interactions affect risk for autism through gene co-expression and protein networks in neuronal cell types.Molecular autism · 2020Article
- Intragenic recruitment of NF-κB drives splicing modifications upon activation by the oncogene Tax of HTLV-1.Nature communications · 2020Article
- The DDX5/Dbp2 subfamily of DEAD-box RNA helicases.Wiley interdisciplinary reviews. RNA · 2019Review
- P68 RNA helicase promotes invasion of glioma cells through negatively regulating DUSP5.Cancer science · 2019Article
- The proline-arginine repeat protein linked to C9-ALS/FTD causes neuronal toxicity by inhibiting the DEAD-box RNA helicase-mediated ribosome biogenesis.Cell death & disease · 2018Article
- The RNA helicase DDX17 controls the transcriptional activity of REST and the expression of proneural microRNAs in neuronal differentiation.Nucleic acids research · 2018Article
- Kruppel-like factor 4-dependent Staufen1-mediated mRNA decay regulates cortical neurogenesis.Nature communications · 2018Article
- Nol12 is a multifunctional RNA binding protein at the nexus of RNA and DNA metabolism.Nucleic acids research · 2017Article
- Regulation of the U3-, U8-, and U13snoRNA Expression by the DEAD Box Proteins Ddx5/Ddx17 with Consequences for Cell Proliferation and Survival.Non-coding RNA · 2016Article
- MicroRNA 433 regulates nonsense-mediated mRNA decay by targeting SMG5 mRNA.BMC molecular biology · 2016Article
- The multiple functions of RNA helicases as drivers and regulators of gene expression.Nature reviews. Molecular cell biology · 2016Review
- Mechanism and regulation of the nonsense-mediated decay pathway.Nucleic acids research · 2016Review
- The expression of RNA helicase DDX5 is transcriptionally upregulated by calcitriol through a vitamin D response element in the proximal promoter in SiHa cervical cells.Molecular and cellular biochemistry · 2015Article
- Unzippers, resolvers and sensors: a structural and functional biochemistry tale of RNA helicases.International journal of molecular sciences · 2015Review
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Non-sense-mediated mRNA decay (NMD) is a mechanism of translation-dependent mRNA surveillance in eukaryotes: it degrades mRNAs with premature termination codons (PTCs) and contributes to cellular homeostasis by downregulating a number of physiologically important mRNAs. In the NMD pathway, Upf proteins, a set of conserved factors of which Upf1 is the central regulator, recruit decay enzymes to promote RNA cleavage. In mammals, the degradation of PTC-containing mRNAs is triggered by the exon-junction complex (EJC) through binding of its constituents Upf2 and Upf3 to Upf1. The complex formed eventually induces translational repression and recruitment of decay enzymes. Mechanisms by which physiological mRNAs are targeted by the NMD machinery in the absence of an EJC have been described but still are discussed controversially. Here, we report that the DEAD box proteins Ddx5/p68 and its paralog Ddx17/p72 also bind the Upf complex by physical interaction with Upf3, thereby interfering with the binding of EJC. By activating the NMD machinery, Ddx5 is shown to regulate the expression of its own, Ddx17 and Smg5 mRNAs. For NMD triggering, the adenosine triphosphate-binding activity of Ddx5 and the 3'-untranslated region of substrate mRNAs are essential.
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