ArticleNucleic acids research2014
The RNA helicase RHAU (DHX36) suppresses expression of the transcription factor PITX1.
Article in Nucleic acids research, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.
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Who cites it
53 citing papers in PubMed, 81 citations in OpenAlex.
- DHX36 is a regulatory switch in the interferon-mediated antiviral response.Science advances · 2026Article
- Characterizations of G-Quadruplex RNA-Protein Interactions in Living Cells.Analytical chemistry · 2026Article
- DHX36 plays an oncogenic role in breast cancer progression and invasiveness.Scientific reports · 2025Article
- Review
- Exploring the Interactions Between RHAU Peptide and G-Quadruplex Dimers Based on Chromatographic Retention Behaviors.Molecules (Basel, Switzerland) · 2024Article
- The shaping of mRNA translation plasticity by RNA G-quadruplexes in cancer progression and therapy resistance.NAR cancer · 2024Review
- Expanding the horizons of targeted protein degradation: A non-small molecule perspective.Acta pharmaceutica Sinica. B · 2024Review
- Structural insights into the N-terminal APHB domain of HrpA: mediating canonical and i-motif recognition.Nucleic acids research · 2024Article
- RHAU Peptides Specific for Parallel G-Quadruplexes: Potential Applications in Chemical Biology.Molecular biotechnology · 2023Review
- Study on the Interaction of a Peptide Targeting Specific G-Quadruplex Structures Based on Chromatographic Retention Behavior.International journal of molecular sciences · 2023Article
- PITX1 plays essential functions in cancer.Frontiers in oncology · 2023Review
- G-quadruplexes and associated proteins in aging and Alzheimer's disease.Frontiers in aging · 2023Review
- DNA and RNA Binding Proteins: From Motifs to Roles in Cancer.International journal of molecular sciences · 2022Review
- Action and function of helicases on RNA G-quadruplexes.Methods (San Diego, Calif.) · 2022Review
- Review
- RNA G-quadruplex structures control ribosomal protein production.Scientific reports · 2021Article
- G3BP1 binds to guanine quadruplexes in mRNAs to modulate their stabilities.Nucleic acids research · 2021Article
- G-quadruplex DNA: a novel target for drug design.Cellular and molecular life sciences : CMLS · 2021Review
- Transcription, translation, and DNA repair: new insights from emerging noncanonical substrates of RNA helicases.Biological chemistry · 2021Review
- Biological relevance and therapeutic potential of G-quadruplex structures in the human noncoding transcriptome.Nucleic acids research · 2021Review
Corrections and comments
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Authors and funding
10 authors at 1 institution in 1 country.
Funding
Abstract
RNA Helicase associated with AU-rich element (RHAU) (DHX36) is a DEAH (Aspartic acid, Glumatic Acid, Alanine, Histidine)-box RNA helicase that can bind and unwind G4-quadruplexes in DNA and RNA. To detect novel RNA targets of RHAU, we performed an RNA co-immunoprecipitation screen and identified the PITX1 messenger RNA (mRNA) as specifically and highly enriched. PITX1 is a homeobox transcription factor with roles in both development and cancer. Primary sequence analysis identified three probable quadruplexes within the 3'-untranslated region of the PITX1 mRNA. Each of these sequences, when isolated, forms stable quadruplex structures that interact with RHAU. We provide evidence that these quadruplexes exist in the endogenous mRNA; however, we discovered that RHAU is tethered to the mRNA via an alternative non-quadruplex-forming region. RHAU knockdown by small interfering RNA results in significant increases in PITX1 protein levels with only marginal changes in mRNA, suggesting a role for RHAU in translational regulation. Involvement of components of the microRNA machinery is supported by similar and non-additive increases in PITX1 protein expression on Dicer and combined RHAU/Dicer knockdown. We also demonstrate a requirement of argonaute-2, a key RNA-induced silencing complex component, to mediate RHAU-dependent changes in PITX1 protein levels. These results demonstrate a novel role for RHAU in microRNA-mediated translational regulation at a quadruplex-containing 3'-untranslated region.
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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.