Ask about this productRelated genes to: HNRNPU antibody
- Gene:
- HNRNPU NIH gene
- Name:
- heterogeneous nuclear ribonucleoprotein U
- Previous symbol:
- HNRPU, HNRNPU-AS1, C1orf199, NCRNA00201
- Synonyms:
- SAF-A, hnRNPU, FLJ37978, FLJ30202
- Chromosome:
- 1q44
- Locus Type:
- gene with protein product
- Date approved:
- 1997-08-28
- Date modifiied:
- 2016-06-03
Related products to: HNRNPU antibody
Related articles to: HNRNPU antibody
- BACKGROUND Retinopathy of prematurity is characterized by retinal vascular ischemia and hypoxia that lead to neovascularization, potentially causing retinal detachment and blindness. This study aimed to explore target genes involved in oxygen-induced retinopathy (OIR) through comprehensive single-cell RNA sequencing (scRNA-seq) data analysis. MATERIAL AND METHODS ScRNA-seq data of retinal tissues obtained from mice under normoxic and OIR conditions were retrieved from the Gene Expression Omnibus (GEO; accession number GSE150703). A suite of bioinformatics tools was used for data processing, cell clustering, cell type annotation, differential gene expression analysis, gene set enrichment analysis, and protein-protein interaction network prediction to identify key hub genes associated with OIR. RESULTS Analysis of GSE150703 OIR mouse data identified 10 retinal cell types. These findings were supported by pathway enrichment analyses, including Gene Ontology and Kyoto Encyclopedia of Genes and Genomes, which indicated significant upregulation of Hnrnpu, Vamp2, Ybx1, Ywhab, and Csnk1a1, and downregulation of Xist and mt-Co1, among others. Interacting proteins from protein-protein interaction network studies identified major hub genes involving Srsf1, Srsf11, Sf3b1, and Hnrnpu, among others. Moreover, the research explored how mutations of Chchd10 and Sf3b1 influence the development of the disease and downregulation of mitochondrial-associated genes, such as lncRNA-Xist, Ndufs5, and mt-Co1, which may provide further insight into their roles in the pathogenesis of OIR. CONCLUSIONS The single-cell data analysis suggests that Hnrnpu, Vamp2, Ybx1, Ywhab, Csnk1a1, Pfkp, Rho, Srsf1, Srsf11, Mt1, Tpr, Hnrnpc, Chchd10, Sf3b1, Xist, Ndufs5, and mt-Co1 may be potential target genes in OIR in retinopathy of prematurity. - Source: PubMed
Publication date: 2026/06/11
Wang XinheWang LijieJu Yanhong - The SAF-A/HNRNPU gene encodes an abundant nuclear protein conserved throughout vertebrates, and is mutated in individuals with HNRNPU syndrome, a neurological human disease. SAF-A is important for maintaining lncRNA localization, splicing, and gene expression state. The mechanistic role of SAF-A in each of these processes is likely coordinated by one or more of its functional domains, which include an N-terminal SAP domain, a central ATPase domain, and a RGG domain defined by a series of C-terminal RGG/RG repeats embedded within a low-complexity region. However, a comprehensive analysis to identify which SAF-A domains are required for each cellular function is lacking. Here we use an allelic reconstitution strategy to investigate the role of the SAF-A ATPase and RGG domains in lncRNA localization, nuclear dynamics, transcription, splicing, and cell viability. We show that both the ATPase and RGG domains control SAF-A nuclear dynamics, and that SAF-A interacts with nascent RNA Pol II transcripts through the RGG domain. The SAF-A ATPase and RGG domains were required for maintaining XIST RNA and facultative heterochromatin marks on the inactive X chromosome, but did not affect X-linked gene silencing. The SAF-A ATPase and RGG domains were both required for proper mRNA splicing, but not for gene expression. Importantly, we found that the SAF-A ATPase and RGG domains are required for cell proliferation, arguing that these domains are each linked to the essential cellular functions of SAF-A. Collectively, our findings highlight the importance of the SAF-A SAP, ATPase and RGG domains in vital functions of nuclear biology. - Source: PubMed
Publication date: 2026/06/03
Sharp Judith AThomas RachaelSparago EmilyAlimenti KaitlynWang WeiBlower Michael D - Pulmonary hypertension (PH) is a fatal disease characterized by pulmonary vascular remodeling, primarily driven by excessive proliferation of pulmonary arterial smooth muscle cells (PASMCs). Although noncoding RNAs, such as circular RNAs, have been implicated in PH, the role of tRNA-derived small RNA remains poorly understood. Among them, i-tRF (internal tRNA-derived fragment)-Asp represents a novel tRNA-derived small RNA whose function in hypoxic PH is unknown. This study aims to investigate whether i-tRF-Asp contributes to PASMC proliferation and vascular remodeling in hypoxic PH. - Source: PubMed
Publication date: 2026/05/28
Yuan HaoChen BoGao DanniZhang LixinBai JuneSun HanliangMei JianOu LanglinGuan XiaoyuWang ShanshanMa CuiXing YanWang ShuangYu HangZhu Daling - Cervical cancer remains a major global health burden, yet the molecular mechanisms driving its metabolic reprogramming are incompletely understood. Here, we identify heterogeneous nuclear ribonucleoprotein U (HNRNPU) as a novel non-histone substrate of lysine lactylation that links lactate accumulation to serine metabolism and tumor progression. We demonstrate that lactylation at lysine 181 (K181) stabilizes HNRNPU, enhances its binding to PHGDH mRNA, and maintains the exon 1-containing PHGDH transcript and mRNA stability, thereby sustaining PHGDH expression and activating the serine biosynthesis pathway. This metabolic rewiring promotes redox homeostasis, nucleotide synthesis, and cervical cancer cell proliferation both in vitro and in vivo. Mechanistically, we reveal a competitive interplay between lactylation and NAA50-mediated acetylation at K181, establishing a dynamic post-translational modification switch that fine-tunes HNRNPU function. Importantly, pharmacological inhibition of HNRNPU K181 lactylation by Pazopanib suppresses PHGDH expression and tumor growth, underscoring its translational potential. Collectively, our findings uncover a lactate-driven regulatory axis in which HNRNPU K181 lactylation integrates metabolic signaling with post-transcriptional regulation to promote cervical cancer progression, providing a promising therapeutic avenue for targeting metabolic vulnerabilities in malignancies. - Source: PubMed
Publication date: 2026/05/27
Zhang ChangMeng QingfeiJiao HuiLiu HuixinWang XiangchaoZhou HonglanWang Yishu - Tumor metastasis is the leading cause of cancer-related mortality, yet the contribution of keratins to this process remains incompletely understood. Here, integrated single-cell and bulk transcriptomic analyses identify keratin 19 (KRT19) within a migration-activated epithelial program as a gene of potential functional relevance. Clinical datasets and tissue microarrays show that KRT19 expression is markedly elevated in gastric cancer and is strongly associated with aggressive pathological features. Functional assays demonstrate that KRT19 depletion impairs cellular migration, invasion, and three-dimensional spheroid infiltration, while while intrasplenic injection of KRT19-silenced cells into male BALB/c nude mice significantly reduces hepatic metastatic colonization, as monitored by serial bioluminescent imaging. Mechanistically, nuclear KRT19 interacts with hnRNPU to facilitate β-TrCP-mediated ubiquitination and degradation of IκBα, thereby sustaining NF-κB activity. Activated NF-κB directly engages the FSCN1 promoter and enhances its transcription, and FSCN1 restoration partially rescues the migratory and metastatic deficits caused by KRT19 knockdown. Together, these findings define a signaling cascade in which an intermediate filament rewires transcriptional programs to control cytoskeletal remodeling and motility, providing mechanistic insight into gastric cancer dissemination and highlighting epithelial structural proteins as underappreciated drivers of metastasis. - Source: PubMed
Publication date: 2026/05/25
Zhou JiajieZi MengliXu ZijieCheng YifanLi RuiqiZhao ShuaiWang JieFu YayanSun LongheTian ZhenZhang ChenkaiFang DengyangZhou YiqiangLi BenSun QiannanRen JunWang Daorong