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
- 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 - Influenza B virus (IBV) is a type of influenza virus. The NS1 protein is a powerful regulatory factor during the process of viral infection of host cells and plays an important role in viral replication, virulence, and innate immunity. Protein-protein interactions play an extremely important role throughout the entire life cycle of viral infection of host cells. Identifying host proteins that interact with IBV NS1 protein is of great significance for exploring the pathogenic mechanism of IBV and screening for new antiviral drugs. In this study, the NS1 protein was purified by immobilized metal affinity chromatography (IMAC) using nickel-charged resin and the known host interactome of IBV NS1 was expanded using Pull-down combined with mass spectrometry (LC-MS/MS). Gene Ontology (GO), Kyoto Encyclopedia of Genes and Genomes (KEGG), and Protein-Protein Interaction (PPI) analyses were conducted on the candidate-interacting proteins identified in the mass spectrometry results. These identified candidate-interacting proteins are mainly involved in biological processes such as protein translation, protein folding, mRNA processing, small molecule metabolism, ribosome biogenesis, and viral processes. The heterogeneous nuclear ribonucleoprotein (hnRNPA0) and the DDX39B protein of the DEAD-box RNA helicase family were further studied. Co-IP, IFA, and BiFC all confirmed that the NS1 protein of IBV interacts with the hnRNPA0 and the DDX39B proteins. We further mapped the interaction between the NS1-RBD and NS1-ED domains of NS1 protein and the hnRNPA0-GRD domain. These data provide resources for further research on the mechanism by which NS1 protein modulates host cells. - Source: PubMed
Publication date: 2026/03/12
Zhang BeibeiWang HailiWang YanweiLiu XiaoYan WenyingZhou JingmingZhang LeiLiu YankaiChen YumeiLiang ChaoWang Aiping - Glioblastoma (GB) is a highly complex ecosystem characterized by numerous interactions between tumor cells and the surrounding tumor microenvironment (TME). Splicing factors play a pivotal role in processing nascent pre-mRNA and are important in the progression of cancer, making them promising molecular targets. In this study, we demonstrate that the DEAD-box helicase 39 A (DDX39A), a RNA helicase with several important roles in RNA metabolism and cellular processes, is significantly upregulated in GB and is primarily expressed in tumor cells, leading to an immunosuppressive macrophage polarization. Through in vitro and in vivo studies, we demonstrate that reducing DDX39A expression in GB results in reduced tumor growth and invasion. Mechanistically, through RNA-seq and RIP-seq, we identified WISP1 as a critical downstream effector of DDX39A. DDX39A stabilizes WISP1 pre-mRNA through alternative splicing regulation, thereby activating the AKT signaling pathway. We further demonstrate that WISP1, when secreted by tumor cells, functions as a paracrine signaling molecule that promotes the development of immunosuppressive tumor-associated macrophages (TAMs). Additionally, we demonstrate that Fluphenazine hydrochloride binds to and inhibits DDX39A, thereby suppressing GB growth, invasion, and the immunosuppressive function of macrophages. DDX39A thus represents a potential candidate for glioma-targeted therapy. - Source: PubMed
Publication date: 2026/03/02
Zhang YanXue ZhiweiZhang NaibinZhu YuehuaWu YanZhaoLv MeilinZhang ZhihanMu FeiyuXing WenchenTang ZiyiWang ChunjieXue ZhiyiZhou WenjingLiu XiaofeiLi XingangBjerkvig RolfHuang BinHan MingzhiWang JianWang Donghai