SART3 antibody - middle region (ARP34329_P050)
- Known as:
- SART3 (anti-) - middle region (ARP34329_P050)
- Catalog number:
- arp34329_p050
- Product Quantity:
- USD
- Category:
- -
- Supplier:
- Aviva Systems Biology
- Gene target:
- SART3 antibody - middle region (ARP34329_P050)
Related genes to: SART3 antibody - middle region (ARP34329_P050)
- Gene:
- SART3 NIH gene
- Name:
- spliceosome associated factor 3, U4/U6 recycling protein
- Previous symbol:
- -
- Synonyms:
- KIAA0156, RP11-13G14, TIP110, p110
- Chromosome:
- 12q23.3
- Locus Type:
- gene with protein product
- Date approved:
- 2001-12-17
- Date modifiied:
- 2019-04-23
Related products to: SART3 antibody - middle region (ARP34329_P050)
Related articles to: SART3 antibody - middle region (ARP34329_P050)
- Head and Neck Squamous Cell Carcinomas (HNSCC) are a heterogeneous collection of malignancies of the head and neck region. Transforming growth factor beta (TGF-β)-regulated long non-coding RNAs (lncRNAs) modulate several aspects of tumor development, including proliferation, invasion, epithelial-to-mesenchymal transition (EMT), metastasis, stemness, and drug resistance. However, global expression patterns and functional contributions of TGF-β-regulated lncRNAs have not been well explored in HNSCC. We identified several differentially expressed lncRNAs upon TGF-β treatment in HNSCC cells using whole-transcriptome sequencing. We show that TGF-β signalling induces lncRNA LASTR expression, and it promotes TGF-β signalling by enhancing TGFβR1 expression. LASTR expression is significantly up-regulated in HNSCC tissues and is associated with poor overall survival in HNSCC patients. LASTR knockdown inhibits cell proliferation, migration, invasion, and TGF-β-induced EMT in HNSCC cells. Moreover, LASTR depletion induces apoptosis and suppresses tumor growth in the xenograft mouse model. Mechanistically, LASTR suppresses miR-34a-5p biogenesis by sequestering the RNA-binding protein SART3 and also acts as a competing endogenous RNA (ceRNA) for miR-34a-5p, thereby up-regulating TGFβR1 expression. Our findings suggest that induction of LASTR by TGF-β modulates the miR-34a-5p/TGFβR1 axis to potentiate TGF-β signalling, highlighting its potential as a therapeutic target in HNSCC. - Source: PubMed
Publication date: 2026/03/10
Swati Joshi VandanaBanerjee TonmoyNeve Arya UdaySengar SuryanshSen DharaniChowdhury ShibasishBiswas SwatiSharma Vivek - Diabetic foot ulcer (DFU) is one of the most common and severe complications of diabetes, with vascular changes, neuropathy, and infections being the primary pathological mechanisms. Disulfidptosis, a recently identified form of programmed cell death, might be involved in the development of diabetic complications. This study aims to identify and validate potential disulfidptosis biomarkers associated with DFU through bioinformatics and machine learning analysis. - Source: PubMed
Publication date: 2025/10/08
Li JIeShi HongshuoCao Yemin - Cisplatin resistance remains a major barrier to effective lung cancer treatment. In this study, we identified that SART3 is upregulated in cisplatin-resistant non-small cell lung cancer (NSCLC) cells and promotes DNA damage repair. SART3 deletion sensitized cells to cisplatin, whereas re-expression restored resistance. Mechanistically, SART3 enhanced DNA repair mainly through the PARP pathway rather than ATM or DNA-PK, and its deletion increased gH2AX levels and reduced BrdU incorporation. Metabolic analysis revealed that SART3-driven resistance relied on elevated fatty acid (FA) β-oxidation rather than glycolysis. SART3 promoted FA uptake by upregulating CD36, resulting in increased oxidative phosphorylation, ATP production, and enhanced DNA repair. Targeting FA metabolism with CPT1A inhibitors or CD36 antagonists, or blocking PARP activity, significantly reversed SART3-mediated resistance. Further, SART3 recruited FOXM1 to activate CD36 transcription by modulating H2b deubiquitination. , inhibition of the SART3-CD36-PARP axis effectively suppressed tumor growth and restored cisplatin sensitivity. Collectively, our findings reveal that SART3-driven metabolic reprogramming and DNA repair underpin cisplatin resistance, providing potential therapeutic strategies to overcome drug resistance in NSCLC. - Source: PubMed
Publication date: 2025/10/10
Huang WenhuiBi BinHuang QilanWu HaijingCheng XinghanPan Li - Human spliceosome-associated factor 3, SART3, is a key factor in spliceosome recycling and engages with U6 small nuclear RNA (snRNA) to promote the formation of the U4/U6 small nuclear ribonucleoprotein complex. Unlike its counterpart U4/U6 snRNA-associated-splicing factor PRP24 (Prp24) from Saccharomyces cerevisiae, which uses four RNA recognition motifs (RRMs) for the U6 snRNA interaction, SART3 has two RRMs at its C terminus. Here, we demonstrate that SART3 binds U6 snRNA as a dimer, and four RRM subunits recognize the asymmetric bulge of U6 snRNA. SART3 RRMs adopt a tandem βαββαβ motif of the canonical RRM fold to interact with the U6 bulge region via a conserved electropositive surface. We identified the cognate U6 elements that specifically bind SART3 RRM1, which is distinct from the Prp24-U6 interactions in yeast. Our findings suggest a divergent RRM binding mechanism for U6 snRNA recognition during spliceosome assembly and recycling. - Source: PubMed
Publication date: 2025/10/05
Kim IktaeBang Kyeong-MiAn So YoungPark ChangkonShin Ji-YeonKim YoungimSong Hyun KyuSuh Jeong-YongKim Nak-Kyoon - The regulatory SNPs (rSNPs) that disturb the binding of transcription factors (TFs) and alter the transcription levels of genes play a paramount role in the formation of different traits and are associated with many pathologies. The search for allele-specific events in RNA-seq and ChIP-seq data is a powerful genome-wide approach to detect rSNPs. Using this approach, we have identified the T → A rs2072580 substitution in the bidirectional / promoter as a potential rSNP and demonstrated its association with colorectal cancer, relying on International Cancer Genome Consortium data. The goal of this work was to identify the TF binding site that is affected by the T → A substitution and to study the effect of this substitution on reporter gene expression in different plasmid constructs. - Source: PubMed
Publication date: 2025/06/17
Degtyareva ArinaAntontseva ElenaEvseenko AnastasiaOrishchenko KonstantinMerkulova Tatiana