ArticleNucleic acids research2010
An internal ribosomal entry site mediates redox-sensitive translation of Nrf2.
Article in Nucleic acids research, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 68 papers.
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Who cites it
68 citing papers in PubMed, 114 citations in OpenAlex.
- Review
- Article
- Translational regulation in stress biology.Nature cell biology · 2025Review
- Targeting Cancer Translational Plasticity: IRES-Driven Metabolism and Survival Within the Tumor Microenvironment.Cancers · 2025Review
- Stress response regulation of mRNA translation: Implications for antioxidant enzyme expression in cancer.Proceedings of the National Academy of Sciences of the United States of America · 2024Review
- Article
- Quantitative proteomic analyses uncover regulatory roles of Nrf2 in human endothelial cells.Cell stress & chaperones · 2023Article
- Acute Oxidative Stress Can Paradoxically Suppress Human NRF2 Protein Synthesis by Inhibiting Global Protein Translation.Antioxidants (Basel, Switzerland) · 2023Article
- How to deal with frenemy NRF2: Targeting NRF2 for chemoprevention and cancer therapy.Journal of food and drug analysis · 2023Review
- The Regulation of Ferroptosis by Noncoding RNAs.International journal of molecular sciences · 2023Review
- Roles of Oxidative Stress and Nrf2 Signaling in Pathogenic and Non-Pathogenic Cells: A Possible General Mechanism of Resistance to Therapy.Antioxidants (Basel, Switzerland) · 2023Review
- CRISPR/Cas9-Based Screening of FDA-Approved Drugs for NRF2 Activation: A Novel Approach to Discover Therapeutics for Non-Alcoholic Fatty Liver Disease.Antioxidants (Basel, Switzerland) · 2023Article
- The Complex Genetic and Epigenetic Regulation of the Nrf2 Pathways: A Review.Antioxidants (Basel, Switzerland) · 2023Review
- Stress Activated MAP Kinases and Cyclin-Dependent Kinase 5 Mediate Nuclear Translocation of Nrf2 via Hsp90α-Pin1-Dynein Motor Transport Machinery.Antioxidants (Basel, Switzerland) · 2023Review
- Fresh Medium or L-Cystine as an Effective Nrf2 Inducer for Cytoprotection in Cell Culture.Cells · 2023Article
- Signal amplification in the KEAP1-NRF2-ARE antioxidant response pathway.Redox biology · 2022Review
- Reversal of G-Quadruplexes' Role in Translation Control When Present in the Context of an IRES.Biomolecules · 2022Review
- HACE1-mediated NRF2 activation causes enhanced malignant phenotypes and decreased radiosensitivity of glioma cells.Signal transduction and targeted therapy · 2021Article
- Nrf2 for cardiac protection: pharmacological options against oxidative stress.Trends in pharmacological sciences · 2021Review
- Epigenetics/Epigenomics and Prevention of Early Stages of Cancer by Isothiocyanates.Cancer prevention research (Philadelphia, Pa.) · 2021Review
8 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
8 authors at 4 institutions in 3 countries.
Funding
Abstract
Nrf2 plays pivotal roles in coordinating the antioxidant response and maintaining redox homeostasis. Nrf2 expression is exquisitely regulated; Nrf2 expression is suppressed under unstressed conditions but strikingly induced under oxidative stress. Previous studies showed that stress-induced Nrf2 up-regulation results from both the inhibition of Nrf2 degradation and enhanced Nrf2 translation. In the present study, we elucidate the mechanism underlying translational control of Nrf2. An internal ribosomal entry site (IRES) was identified within the 5' untranslated region of human Nrf2 mRNA. The IRES(Nrf2) contains a highly conserved 18S rRNA binding site (RBS) that is required for internal initiation. This IRES(Nrf2) also contains a hairpin structured inhibitory element (IE) located upstream of the RBS. Deletion of this IE remarkably enhanced translation. Significantly, treatment of cells with hydrogen peroxide (H(2)O(2)) and phyto-oxidant sulforaphane further stimulated IRES(Nrf2)-mediated translation initiation despite the attenuation of global protein synthesis. Polyribosomal profile assay confirmed that endogenous Nrf2 mRNAs were recruited into polysomal fractions under oxidative stress conditions. Collectively, these data demonstrate that Nrf2 translation is suppressed under normal conditions and specifically enhanced upon oxidant exposure by internal initiation, and provide a mechanistic explanation for translational control of Nrf2 by oxidative stress.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.