UPF1 antibody - middle region (ARP36350_P050)
- Known as:
- UPF1 (anti-) - middle region (ARP36350_P050)
- Catalog number:
- arp36350_p050
- Product Quantity:
- USD
- Category:
- -
- Supplier:
- Aviva Systems Biology
- Gene target:
- UPF1 antibody - middle region (ARP36350_P050)
Related genes to: UPF1 antibody - middle region (ARP36350_P050)
- Gene:
- UPF1 NIH gene
- Name:
- UPF1 RNA helicase and ATPase
- Previous symbol:
- RENT1
- Synonyms:
- HUPF1, KIAA0221, NORF1, pNORF1, smg-2
- Chromosome:
- 19p13.11
- Locus Type:
- gene with protein product
- Date approved:
- 1997-02-11
- Date modifiied:
- 2019-01-25
Related products to: UPF1 antibody - middle region (ARP36350_P050)
Related articles to: UPF1 antibody - middle region (ARP36350_P050)
- C/EBPβ regulates oncogene-induced senescence (OIS) and the senescence-associated secretory phenotype (SASP) through activation by ERK1/2 and CK2. In tumor cells, C/EBPβ activity is suppressed by its 3'UTR via a mechanism termed 3'UTR regulation of protein activity (UPA), which spatially segregates transcripts from kinase-rich perinuclear endosomes. Here, we identify kinase-proximal mRNA decay as the underlying mechanism. The mRNA decay factors UPF1 and STAU1/2 localize to perinuclear endosomes and promote degradation of transcripts, thereby preventing C/EBPβ phosphorylation and activation. Disruption of this pathway restores C/EBPβ activity and induces senescence. , deletion of a G/U-rich regulatory element (GRE) in the 3'UTR impairs the progression of Kras-driven lung tumors and biases cells toward an AT2-like differentiation state with reduced EMT-associated transcriptional reprogramming. RAS-expressing fibroblasts show enhanced OIS that requires upregulation of the pro-senescent cytokine S100a9. These findings identify perinuclear mRNA decay as a mechanism suppressing C/EBPβ activity and senescence in cancer. - Source: PubMed
Publication date: 2026/08/04
Salotti JacquelineAsif NidaBasu SrikantaDas AniruddhaHu LinshanYang MeiKarim BaktiarSaylor KarenMartin NancyScheiblin David AMisra SwetaLuke Brian TAndresson ThorkellYi MingGalloux MélissaLockett StephenTessarollo LinoJohnson Peter F - The RNA lariat debranching enzyme DBR1 is essential for intron turnover and RNA metabolism, yet its broader impact on transcriptome regulation remains incompletely defined. To elucidate the consequences of DBR1 depletion, we performed transcriptome-wide RNA sequencing of DBR1-knockdown and wild-type HEK293 cells. Differential expression analysis revealed widespread perturbations in pathways linked to RNA splicing, mRNA surveillance, translational control, and stress-granule biology. Many of the most significantly altered transcripts encode splicing factors and RNA quality-control components, underscoring DBR1's influence on post-transcriptional regulation. Alternative splicing analysis showed changes across multiple event types, with exon skipping accounting for >50% of events, followed by mutually exclusive exons, alternative 5' and 3' splice sites, and retained introns, indicating that DBR1 depletion induces pervasive splicing defects. Direct spliceosome inhibition using isoginkgetin (blocks tri-snRNP recruitment) and pladienolide B (targets SF3B1) reproduced the DBR1-KD mis-splicing patterns of cell signaling genes and factors involved in RNA metabolism, supporting a functional link between DBR1 activity and alternative splicing. Notably, DBR1 knockdown revealed a subset of transcripts that are both NMD-sensitive and enriched within stress granules. Consistent with this observation, G3BP1 immunopurification and confocal microscopy further support a role for DBR1 and UPF1 in stress-granule dynamics, suggesting that these factors may participate at distinct stages to influence mRNA fate under stress conditions. Together, these findings indicate that DBR1 functions beyond lariat RNA turnover as a common regulator of RNA processing, transcriptome stability, and stress granule homeostasis, revealing intricate crosstalk between RNA splicing and RNA quality control pathways in human cells. - Source: PubMed
Publication date: 2026/08/04
Barwell TiffanyEmbree Caleb MReid RobertSingh GuramritChakrabarti Kausik - Hepatocellular carcinoma (HCC) is a leading cause of cancer death, yet immune checkpoint inhibitors (ICIs) benefit only a minority of patients-a limitation attributed to low tumor mutational burden (TMB) and an immunologically cold microenvironment. SMG1, a serine/threonine kinase of the phosphatidylinositol 3-kinase-related kinase (PIKK) superfamily, sits at the intersection of RNA surveillance, the DNA damage response, and oncogenic signaling. As the master kinase of nonsense-mediated mRNA decay (NMD), SMG1 phosphorylates UPF1 to degrade transcripts bearing premature termination codons; independently, it restrains tumor growth by phosphorylating p53 (Ser15) and promoting Cdc25A turnover. SMG1 was originally identified as a tumor-suppressive modulator of sorafenib resistance in HCC (Nam, S.W. et al., 2014), and subsequent work shows SMG1 is reduced in HCC, predicts adverse outcome, and is recurrently silenced by reversible promoter hypermethylation. Paradoxically, the same kinase conceals mutation-derived neoantigens, and its selective inhibition (e.g., KVS0001) raises HLA class I neoantigen presentation toward high-TMB levels and improves checkpoint-inhibitor efficacy in preclinical and liver-specific models. This critical review integrates SMG1 structural biology, clinicopathology, signaling, sorafenib resistance, and NMD-directed immunotherapy, grading established versus inferential mechanisms, and nominates SMG1 and NMD as dual, context-dependent targets for HCC precision oncology. - Source: PubMed
Publication date: 2026/07/31
Nam Soon Woo - The nonsense-mediated mRNA decay (NMD) pathway is a mRNA quality control mechanism which not only degrades deleterious transcripts but also orchestrates a large number of post-transcriptional regulatory programs through unproductive splicing. We have developed a robust metric derived from splicing quantification in the RNA-seq data to measure NMD efficiency at a sample level. We demonstrate that NMD efficiency varies substantially both between and within tissues, with the magnitude of the variation comparable to that observed upon knockdown of the core NMD factor UPF1. By analyzing TCGA cancer cohorts, we further show that, in many tumors, unproductive splicing events undergo coordinated changes towards either collective suppression or collective activation of NMD isoforms, which is indicative of global deregulation of the activity of the NMD pathway. Consistently, we observed a striking divergence of NMD efficiency in cancers from the tissue-specific baseline level, suggesting that tumors partially erase the NMD signature of their tissue of origin. The application of the developed metric to RNA-binding protein knockdowns made it possible to identify several novel potential regulators of NMD efficiency. In sum, this study provides a solid framework for quantifying NMD efficiency, describes its biological and clinical relevance, and opens new avenues for dissecting mechanisms of post-transcriptional gene expression regulation by the NMD pathway. - Source: PubMed
Zavileyskiy L GMironov A APervouchine D D - - Source: PubMed
Publication date: 2026/07/13
Jeong JiwonHong DawonPark Tae YoungHur JungKoo TaeyoungJeong Sunjoo