ArticleProceedings of the National Academy of Sciences of the United States of America2010
RNA helicase A is a DNA-binding partner for EGFR-mediated transcriptional activation in the nucleus.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 65 papers.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
65 citing papers in PubMed, 114 citations in OpenAlex.
- DHX9 sustains hematopoietic stem cell function in cooperation with H3 acetylation.Stem cell reports · 2026Article
- Liver regeneration-associated hepatocellular YAP1 activation prevents colorectal cancer liver metastasis through glutamine competition.Science advances · 2025Article
- DHX9-mediated epigenetic silencing of BECN1 contributes to impaired autophagy and tumor progression in breast cancer via recruitment of HDAC5.Cell death & disease · 2025Article
- Review
- Article
- Nuclear miR-150 enhances hepatic lipid accumulation by targeting RNA transcripts overlapping theiScience · 2023Article
- Cellular functions of eukaryotic RNA helicases and their links to human diseases.Nature reviews. Molecular cell biology · 2023Review
- DHX9-mediated pathway contributes to the malignant phenotype of myelodysplastic syndromes.iScience · 2023Article
- Sorting nexin-dependent therapeutic targeting of oncogenic epidermal growth factor receptor.Cancer gene therapy · 2023Article
- Nuclear epidermal growth factor receptor as a therapeutic target.Exploration of targeted anti-tumor therapy · 2023Review
- Nuclear export signal mutation of epidermal growth factor receptor enhances malignant phenotypes of cancer cells.American journal of cancer research · 2023Article
- RNA Helicases as Shadow Modulators of Cell Cycle Progression.International journal of molecular sciences · 2021Review
- Novel Tyrosine Kinase Targets in Urothelial Carcinoma.International journal of molecular sciences · 2021Review
- NONO phase separation enhances DNA damage repair by accelerating nuclear EGFR-induced DNA-PK activation.American journal of cancer research · 2021Article
- Tyrosine Kinase Receptors in Oncology.International journal of molecular sciences · 2020Review
- The enigmatic helicase DHX9 and its association with the hallmarks of cancer.Future science OA · 2020Review
- 2D-QSAR Modeling and Molecular Docking Studies on 1ACS omega · 2020Article
- Profiling of subcellular EGFR interactome reveals hnRNP A3 modulates nuclear EGFR localization.Oncogenesis · 2020Article
- Epidermal growth factor (EGF) triggers nuclear calcium signaling through the intranuclear phospholipase Cδ-4 (PLCδ4).The Journal of biological chemistry · 2019Article
- TRAIL Induces Nuclear Translocation and Chromatin Localization of TRAIL Death Receptors.Cancers · 2019Article
5 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
15 authors at 4 institutions in 2 countries.
Funding
Abstract
EGF induces the translocation of EGF receptor (EGFR) from the cell surface to the nucleus where EGFR activates gene transcription through its binding to an AT-rich sequence (ATRS) of the target gene promoter. However, how EGFR, without a DNA-binding domain, can bind to the gene promoter is unclear. In the present study, we show that RNA helicase A (RHA) is an important mediator for EGFR-induced gene transactivation. EGF stimulates the interaction of EGFR with RHA in the nucleus of cancer cells. The EGFR/RHA complex then associates with the target gene promoter through binding of RHA to the ATRS of the target gene promoter to activate its transcription. Knockdown of RHA expression in cancer cells abrogates the binding of EGFR to the target gene promoter, thereby reducing EGF/EGFR-induced gene expression. In addition, interruption of EGFR-RHA interaction decreases the EGFR-induced promoter activity. Consistently, we observed a positive correlation of the nuclear expression of EGFR, RHA, and cyclin D1 in human breast cancer samples. These results indicate that RHA is a DNA-binding partner for EGFR-mediated transcriptional activation in the nucleus.
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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.