Ask about this productRelated genes to: DDX39 antibody
- Gene:
- DDX39A NIH gene
- Name:
- DExD-box helicase 39A
- Previous symbol:
- DDX39
- Synonyms:
- DDXL, BAT1L, URH49
- Chromosome:
- 19p13.12
- Locus Type:
- gene with protein product
- Date approved:
- 2002-04-19
- Date modifiied:
- 2016-09-27
Related products to: DDX39 antibody
Related articles to: DDX39 antibody
- Amyloid aggregates of α-Synuclein are hallmarks of Parkinson's disease (PD) and related neurodegenerative disorders. Literature suggests that mRNA G-quadruplexes (rG4s) bind to α-Synuclein, facilitating its amyloidogenesis. In parallel, α-Synuclein interacts with RNA-binding proteins (RBPs) within cytosolic RNA-protein granules to modulate mRNA stability. However, mechanisms by which α-Synuclein-interacting RBPs regulate its amyloidogenesis remain unexplored. Here, we report that rG4-dependent cytosolic interaction with the DEAD-box helicase DDX39A decelerates α-Synuclein amyloidogenesis. Notably, viral infections transiently elevate rG4s in the cytoplasm. Perturbing interactions between α-Synuclein and DDX39A using genomic rG4-sequences from H1N1 Influenza and SARS-CoV-2 expedites intracellular amyloidogenesis. Conversely, DDX39A overexpression alleviates α-Synuclein amyloidogenesis in SARS-CoV-2-infected primary neurons. We demonstrate that while DDX39A unwinds viral rG4s to mitigate α-Synuclein sol-gel transition, its cooperative phase separation with α-Synuclein enhances the helicase's rG4-unwinding activity. We propose that accelerated α-Synuclein amyloidogenesis reflects a trade-off within this RNA-protein equilibrium and might contribute to the viral etiology of PD. - Source: PubMed
Publication date: 2026/09/25
Jain AanchalTripathi ShreyaAgarwal CheshtaBiswas AnubhabPotharaju Poojitha SaiDe AratrikaMansuri SheminMondal ArindamHarshan Krishnan HRaychaudhuri Swasti - Lactylation, an emerging post-translational modification, modulates tumor metabolism and gene expression, thereby influencing the initiation and progression of cervical squamous cell carcinoma (CESC). This study aims to identify lactylation-associated prognostic features in CESC through the integration of transcriptomic data and single-cell RNA sequencing (scRNA-seq). - Source: PubMed
Publication date: 2026/07/22
Zheng YunuoLi YueZhang ShenghanLv QianZhang JingboZhang BeiLi Yanyu - Dysregulation of Toll-like receptor signaling and increased proportions of Th17 and other T helper cells can facilitate esophageal squamous cell carcinoma (ESCC) progression. - Source: PubMed
Publication date: 2026/05/26
Liu BoXiao JiazhouTao XuanLi Xu - PURPOSE: Esophageal squamous cell carcinoma (ESCC) is an aggressive malignancy with limited treatment options. Although radiotherapy remains a cornerstone of curative treatment, intrinsic and acquired radioresistance frequently lead to locoregional recurrence and disease progression. DDX39A, a DEAD-box RNA helicase, regulates RNA metabolism in diverse cellular contexts; however, its role in ESCC pathogenesis and therapeutic resistance remains unclear. METHODS: Bioinformatics analyses, immunohistochemistry, and functional assays were performed to characterize the role of DDX39A in ESCC. Tandem mass tag-based proteomics was used to identify downstream effectors. Mechanistic studies included RIP-qPCR, ChIP-qPCR, and dual-luciferase reporter assays. The therapeutic relevance was further validated using murine xenograft models. RESULTS: DDX39A was significantly upregulated in ESCC tissues and cell lines, and its high expression correlating with increased tumor proliferation. DDX39A knockdown suppressed malignant phenotypes and markedly enhanced radiosensitivity. Mechanistically, SP1 was prioritized from proteomic screening owing to its central role as a transcription factor regulating DNA repair gene expression. DDX39A directly binds to SP1 mRNA, stabilizing it and enhancing its translation efficiency without affecting transcription. The resulting increase in SP1 protein promotes binding to the − 223/−214 bp region of the Ku70 promoter, thereby transcriptionally activating this key component of the non-homologous end joining pathway and contributing to radioresistance. Rescue experiments confirmed that the DDX39A–SP1–Ku70 axis is both necessary and sufficient to mediate radioresistance. In vivo, DDX39A silencing enhanced radiosensitivity and improved tumor control in ESCC models. CONCLUSIONS: These findings identify DDX39A as a promising therapeutic target in ESCC radioresistance. The DDX39A–SP1–Ku70 axis provides a mechanistic rationale for the development of novel radiosensitization strategies. - Source: PubMed
Publication date: 2026/04/15
Hui BeinaHu WeibinChen XinWang YingLi JingSun YuchenSun XuanziRen Juan - - Source: PubMed
Zhang YanXue ZhiweiZhang NaibinZhu YuehuaWu YanZhaoLv MeilinZhang ZhihanMu FeiyuXing WenchenTang ZiyiWang ChunjieXue ZhiyiZhou WenjingLiu XiaofeiLi XingangBjerkvig RolfHuang BinHan MingzhiWang JianWang Donghai