ArticleAdvanced science (Weinheim, Baden-Wurttemberg, Germany)2025
Phosphorylation of POU3F3 Mediated Nuclear Translocation Promotes Proliferation in Non-Small Cell Lung Cancer through Accelerating ATP5PF Transcription and ATP Production.
Article in Advanced science (Weinheim, Baden-Wurttemberg, Germany), 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
What it found
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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
5 citing papers in PubMed.
- Comprehensive identification of three key genes and three key DNA methylation CpG sites associated with prognosis and prediction in colon adenocarcinoma.Discover oncology · 2026Article
- Exploratory identification of coding and splicing-related SNV variants in A1A1 and A2A2 β-casein Holstein dairy cows.Journal of animal science · 2026Article
- The application of nanotechnology in regulating mitochondrial function in tumor microenvironment for cancer therapy.Theranostics · 2026Review
- Phosphorylation of POU3F3 Mediated Nuclear Translocation Promotes Proliferation in Non-Small Cell Lung Cancer through Accelerating ATP5PF Transcription and ATP Production.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- A multi-cohort validated OXPHOS signature predicts survival and immune profiles in grade II/III glioma patients.Frontiers in immunology · 2025Article
Corrections and comments
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Authors and funding
15 authors.
Funding
Abstract
Targeting oxidative phosphorylation (OXPHOS) through inhibiting the electron transport chain (ETC) has shown promising pre-clinical efficacy in cancer therapy. Although aerobic glycolysis is a hallmark of cancer, emerging evidence suggest OXPHOS is frequently enhanced, providing metabolic advantages for cell proliferation, metastasis, and drug resistance in a variety of aggressive cancer types including non-small cell lung cancer (NSCLC), yet the underlying molecular mechanisms remain elusive. Here it is reported that POU-domain containing family protein POU3F3 is translocated into the nuclei of NSCLC cell lines harboring mutant RAS, where it activates transcription of ATP5PF, an essential component of mitochondrial ATP synthase and consequent ATP production, leading to enhanced NSCLC proliferation and migration. Moreover, it is further found out that ERK1 phosphorylates POU3F3 at the S393 site in the cytoplasm and promotes the nuclear translocation of POU3F3 via receptor importin β1 in RAS mutant NSCLC cells. Mechanistically, RNA sequencing analysis combined with chromatin immunoprecipitation (ChIP) assay revealed that POU3F3 binds to the promoter of ATP5PF, leading to enhanced ATP5PF transcription and ATP production. Together, this study uncovers a novel RAS-POU3F3-ATP5PF axis in facilitating NSCLC progression, providing a new perspective on the understanding of molecular mechanisms for NSCLC progression.
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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.