Ask about this productRelated genes to: DDX39B antibody
- Gene:
- DDX39B NIH gene
- Name:
- DExD-box helicase 39B
- Previous symbol:
- BAT1
- Synonyms:
- D6S81E, UAP56
- Chromosome:
- 6p21.33
- Locus Type:
- gene with protein product
- Date approved:
- 2001-07-13
- Date modifiied:
- 2016-09-27
Related products to: DDX39B antibody
Related articles to: DDX39B antibody
- Interleukin-15 (IL-15) is expressed in various cancers, including melanoma, where it exists in distinct membrane-associated isoforms. Primary melanoma cells predominantly express the non-cleavable transmembrane form (tmbIL-15), while metastatic cells also express a cleavable membrane-bound form (mbIL-15) complexed with IL-15Rα. As tmbIL-15 is capable of reverse signaling upon IL-15Rα engagement, we investigated how this signaling axis modulates melanoma cell behavior across tumor stages. Transcriptomic analysis of melanoma patients revealed that high IL-15 expression correlates with immune activation, inflammation and epithelial-to-mesenchymal transition (EMT), along with coordinated upregulation of IL-15 receptor subunits. Proteomic profiling of melanoma cell lines stimulated with soluble IL-15Rα (sIL-15Rα) uncovered distinct, stage-specific responses. Although several proteins were commonly deregulated across cell lines, most showed opposite regulation in primary versus metastatic models, indicating that tmbIL-15 reverse signaling triggers context-dependent programs influenced by tumor progression. A stringent cross-comparison identified five proteins (PSAP, MARCKS, eEF1A1, DDX39B, and RACK1) as consistently and differentially regulated across tumor stages. Further comparison with published NK cell co-culture and EMT cytokine stimulation datasets revealed a subset of shared effectors, notably PSAP, TPM3 isoform 2 and MARCKS, suggesting that IL-15Rα-induced tmbIL-15 signaling is part of the immune editing phenomenon eliciting pro-tumoral activities complementary to the EMT process. Among these, PSAP emerged as the most robustly and consistently modulated effector, upregulated in primary melanoma cells and downregulated in metastatic ones upon sIL-15Rα stimulation. Its expression correlated positively with CD8+ T cell infiltration and negatively with NK cell infiltration, with distinct transcriptomic programs associated with high PSAP expression in primary versus metastatic settings. Altogether, these findings identify PSAP as a stage-specific mediator of tmbIL-15 reverse signaling in melanoma, integrating immune and EMT-related cues with potential implications for tumor progression and microenvironmental remodeling. - Source: PubMed
Publication date: 2026/04/15
Forcelloni SergioGiron-Michel JulienDel Boccio PieroCufaro Maria ConcettaDi Sebastiano AliceMariotti Francesca RomanaCiancaglini CeciliaChouaib SalemPadelli MaelVespa SimoneMac Giang DangEbert StefanBuart StéphanieMaggi EnricoMoretta LorenzoVacca PaolaTumino NicolaQuatrini LindaCaruana IgnazioAzzarone BrunoSantopolo Silvia - 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 - LncRNA-disease association (LDA) identification can provide valuable insights for understanding disease pathogenesis. Existing most deep learning-based LDA prediction models remain limitations in effectively fusing various features of lncRNAs and diseases and accurately classifying unknown lncRNA-disease pairs (LDPs). Here, we introduce a deep learning-based LDA prediction frame work named LDA-RMGPB based on multi-representation fusion and boosting with Gaussian process. First, a randomized singular value decomposition model is presented to extract LDP linear features. Subsequently, a masked graph autoencoder is exploited to learn LDP nonlinear features. Finally, a boosting algorithm with Gaussian process takes the concatenation of LDP linear and nonlinear features as inputs and classifies unlabeled LDPs. To measure the LDA-RMGPB performance, we performed a series of experiments. Using six evaluation metrics, under four different 5-fold cross-validation strategies (i.e., cross validations on lncRNAs, diseases, LDPs, independent lncRNAs and inde pendent diseases), LDA-RMGPB greatly surpassed seven state-of-the-art prediction methods on two LDA datasets. Further analysis, including ablation study, CeRNA theory analysis, lncRNA-related therapeutic drug analysis, and survival analysis, elucidated that LDA-RMGPB achieved superior LDA identification ability. Moreover, we predicted that lncRNAs ATP6V1G2-DDX39B and PSORS1C3 could have dense linkages with breast cancer and prostatic neoplasms, respectively. We anticipate that LDA-RMGPB contributes to the discovery of novel therapeutic molecular targets across diverse diseases. LDA-RMGPB is freely available at https://github.com/plhhnu/LDA-RMGPB. - Source: PubMed
Publication date: 2026/03/10
Liu LonglongHuang LiangliangBai ZongzhengJiang YanPeng Lihong - The nuclear export of mRNA represents a critical regulatory node in eukaryotic gene expression. This process is orchestrated by two conserved multi-subunit assemblies: the transcription-and-export complex (TREX) and TREX-2. While TREX facilitates mRNP packaging through multivalent RNA-protein interactions, the precise mechanism by which TREX-2 contributes to mRNA export has remained elusive. Here, we report a functional interaction between UAP56 and TREX-2 and resolve the structures of TREX-2 in both apo and UAP56-bound states. UAP56 engages TREX-2 via its N-terminal region, positioning its RecA domains on the V-shaped surface of the complex. A conserved loop from TREX-2 inserts between the RecA domains of UAP56, stabilizing an open conformation. Biochemical assays demonstrate that TREX-2 significantly stimulates the ATPase activity of UAP56, thereby promoting RNA release. These findings provide structural and mechanistic insights into TREX-2-mediated regulation of mRNA export through UAP56 remodeling. - Source: PubMed
Publication date: 2026/02/26
Gong XingTao RanGe XiaofeiZhu HuihuiLi MengqiChen YufangGao YongxiangHang JingZhang Xiaofeng - Recent studies have reported the overexpression of Sm proteins in several cancers, suggesting their potential as therapeutic targets; however, the specific Sm family members involved in endometrial cancer and their mechanisms remain unclear. Here, we show that the Sm protein SNRPD2 is markedly upregulated in both fresh-frozen and formalin-fixed paraffin-embedded (FFPE) endometrial cancer specimens and that its overexpression correlates with poorer clinical outcomes. In vitro and in vivo functional assays demonstrate that silencing SNRPD2 suppresses endometrial cancer cell proliferation and metastasis. Specifically, antisense oligonucleotides (ASOs) targeting SNRPD2 markedly reduced tumor growth in a patient-derived xenograft (PDX) model. Mechanistic analyses reveal that SNRPD2 knockdown induces the retention of intron 5 in DDX39B, resulting in the production of a noncoding transcript that is degraded by the nonsense-mediated decay (NMD) pathway and thereby decreases DDX39B expression. Reduced DDX39B levels permit the activation of a cryptic exon (Exon 2_3) in the CTSC mRNA, which introduces premature termination codons (PTCs) and triggers additional NMD-mediated degradation, leading to decreased CTSC expression. Thus, SNRPD2 maintains high DDX39B expression by preventing intron retention, and in turn, elevated DDX39B expression suppresses cryptic exon usage in CTSC to preserve CTSC expression, ultimately supporting malignant phenotypes of endometrial cancer. These results define a novel SNRPD2-DDX39B-CTSC regulatory axis and identify SNRPD2 as a promising therapeutic target for endometrial cancer. - Source: PubMed
Publication date: 2026/02/20
Li YingweiChen ZhongshaoLiu YanlingGao YuehanPu YingyingGao QianqianGao FengYang NingLi Peng