ArticleScientific reports2017
DDX3 regulates endoplasmic reticulum stress-induced ATF4 expression.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed, 54 citations in OpenAlex.
- Article
- RK-33 inhibits the OC43 coronavirus and induces stress granules via DDX3X-independent mechanisms.RNA (New York, N.Y.) · 2026Article
- Regulation of Translation of ATF4 mRNA: A Focus on Translation Initiation Factors and RNA-Binding Proteins.Cells · 2026Review
- DDX3X acts as a selective dual switch regulator of mRNA translation in acute ER stress.Cell reports · 2025Article
- DDX3X promotes endoplasmic reticulum protein reprogramming via interaction with ERN1 to amplify cerebral ischemia/reperfusion injury.European journal of medical research · 2025Article
- Article
- The cytoplasmic-nuclear transport of DDX3X promotes immune-mediated liver injury in mice regulated by endoplasmic reticulum stress.Cell death & disease · 2024Article
- The RNA Demethylases ALKBH5 and FTO Regulate the Translation of ATF4 mRNA in Sorafenib-Treated Hepatocarcinoma Cells.Biomolecules · 2024Article
- Combined transcriptomics and proteomics unveil the impact of vitamin C in modulating specific protein abundance in the mouse liver.Biological research · 2024Article
- Secondary structures that regulate mRNA translation provide insights for ASO-mediated modulation of cardiac hypertrophy.Nature communications · 2023Article
- Secondary structures that regulate mRNA translation provide insights for ASO-mediated modulation of cardiac hypertrophy.bioRxiv : the preprint server for biology · 2023Article
- Parkinson's disease: From genetics to molecular dysfunction and targeted therapeutic approaches.Genes & diseases · 2023Review
- The translational landscape as regulated by the RNA helicase DDX3.BMB reports · 2022Review
- The human DEAD-box helicase DDX3X as a regulator of mRNA translation.Frontiers in cell and developmental biology · 2022Review
- UVB-induced eIF2α phosphorylation in keratinocytes depends on decreased ATF4, GADD34 and CReP expression levels.Life sciences · 2021Article
- Genetic depletion of the RNA helicase DDX3 leads to impaired elongation of translating ribosomes triggering co-translational quality control of newly synthesized polypeptides.Nucleic acids research · 2021Article
- Level of Murine DDX3 RNA Helicase Determines Phenotype Changes of Hepatocytes In Vitro and In Vivo.International journal of molecular sciences · 2021Article
- RNA Helicase DDX3: A Double-Edged Sword for Viral Replication and Immune Signaling.Microorganisms · 2021Review
- DDX3 depletion represses translation of mRNAs with complex 5' UTRs.Nucleic acids research · 2021Article
- ONC201 induces the unfolded protein response (UPR) in high- and low-grade ovarian carcinoma cell lines and leads to cell death regardless of platinum sensitivity.Cancer medicine · 2021Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
Accumulation of unfolded and potentially toxic proteins in the endoplasmic reticulum (ER) activates a cell stress adaptive response, which involves a reprogramming of general gene expression. ATF4 is a master stress-induced transcription factor that orchestrates gene expression in cells treated with various ER stress inducers including those used to treat cancers. ER stress-induced ATF4 expression occurs mainly at the translational level involving the activity of the phosphorylated (P) translation initiation factor (eIF) eIF2α. While it is well established that under ER stress PeIF2α drives ATF4 expression through a specialised mode of translation re-initiation, factors (e.g. RNA-binding proteins and specific eIFs) involved in PeIF2α-mediated ATF4 translation remain unknown. Here we identified the RNA-binding protein named DDX3 as a promotor of ATF4 expression in cancer cells treated with sorafenib, an ER stress inducer used as a chemotherapeutic. Depletion experiments showed that DDX3 is required for PeIF2α-mediated ATF4 expression. Luciferase and polyribosomes assays showed that DDX3 drives ER stress-induced ATF4 mRNA expression at the translational level. Protein-interaction assays showed that DDX3 binds the eIF4F complex, which we found to be required for ER stress-induced ATF4 expression. This study thus showed that PeIF2α-mediated ATF4 mRNA translation requires DDX3 as a part of the eIF4F complex.
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