Ask about this productRelated genes to: RNPS1 antibody
- Gene:
- RNPS1 NIH gene
- Name:
- RNA binding protein with serine rich domain 1
- Previous symbol:
- -
- Synonyms:
- -
- Chromosome:
- 16p13.3
- Locus Type:
- gene with protein product
- Date approved:
- 1999-09-28
- Date modifiied:
- 2016-04-14
Related products to: RNPS1 antibody
Related articles to: RNPS1 antibody
- Accurate quantification of relative gene expression by RT-qPCR requires the selection of appropriate reference genes for data normalization. Recently, extracellular vesicle components, particularly exosomal RNAs, have recently emerged as promising biomarkers for Alzheimer's disease (AD). Among these, mRNAs from astrocyte-derived exosomes (ADEs) hold particular significance for AD diagnosis and prognosis due to their high in vivo stability and capacity to cross the blood-brain barrier, thereby faithfully reflecting cerebral pathological changes in AD patients. However, suitable reference genes for normalizing target gene expression in ADEs have not been systematically identified. In this study, we comprehensively evaluated the expression stability of candidate reference genes in plasma ADEs across cognitively unimpaired (CU), mild cognitive impairment (MCI), and AD patients using five robust algorithms, including Genorm, Bestkeeper, ΔC method, Normfinder, and RefFinder. Our results revealed that YWHAE and RNPS1 exhibited superior expression stability across all three groups, whereas GAPDH, a conventionally used reference gene, demonstrated inadequate stability. Collectively, our work provides the first systematic validation of reference genes for mRNA quantification in plasma ADEs, establishing a methodological foundation for ADE-based AD biomarker development. - Source: PubMed
Publication date: 2026/03/19
Guo GuiguiQu YiwenWang QiyaoXiao ZhihuaLiu QinZeng XianfeiChen Shouwen - Ferroptosis plays a crucial role in regulating tumor growth and represents a promising therapeutic target for nonsmall cell lung cancer (NSCLC). RNA-binding protein with serine-rich domain 1 (RNPS1) has been closely associated with the development of various cancer types, but its role in NSCLC remains unclear. In this study, we used lentiviral vectors to silence or overexpress RNPS1 in NSCLC cells and then assessed cell proliferation along with ferroptosis markers, such as lipid reactive oxygen species (ROS). Bioinformatics analysis revealed that RNPS1 was upregulated in clinical NSCLC samples. Consistently, functional experiments showed that overexpression of RNPS1 promoted cell proliferation, while RNPS1 knockdown inhibited cell proliferation. Furthermore, RNPS1 overexpression attenuated erastin-triggered ferroptosis by suppressing the accumulation of lipid ROS and malondialdehyde, as well as by preventing the depletion of glutathione. Mechanistic investigations identified that RNPS1 stabilized ETS variant transcription factor 4 (ETV4) mRNA. Importantly, blocking ETV4 expression partially reversed RNPS1 overexpression-mediated suppression of ferroptosis. Collectively, these results support the notion that RNPS1 acts as a novel suppressor of ferroptosis in NSCLC progression. - Source: PubMed
Publication date: 2026/01/06
Wang LinglingMao ShitaoSun YueZhang NaLi XiayunQi YuanDong HanXin Ping - The Exon-Junction Complex (EJC) is essential for post-transcriptional gene regulation, with MAGOH as one of its core components, known for its involvement in mRNA surveillance and translation. In this study, we characterize an evolutionarily conserved, alternatively spliced isoform of MAGOH, i.e. MAGOH-Δ37, which has remained largely unexplored until now. Our study reveals that, unlike canonical MAGOH, MAGOH-Δ37 does not interact with known EJC proteins such as EIF4A3, RBM8A, RNPS1, or SAP18, suggesting a distinct functional role independent of the EJC. Intriguingly, both MAGOH and MAGOH-Δ37 associate with proteins implicated in neurodegenerative disorders, suggesting EJC-independent interactions. Furthermore, MAGOH and its isoform MAGOH-Δ37 interact with ubiquitin and were found to be upregulated upon proteasomal inhibition. The association of the isoforms with a distinct polyubiquitin signature suggests a potential role in the ubiquitin-proteasome system, either as targets or binding partners. These findings provide new insights into the roles of MAGOH isoforms in stress-related pathways, with implications for their involvement in neurodegenerative conditions. - Source: PubMed
Publication date: 2025/08/25
Rehman AyushiTamilselvan RajaBaeta HenriqueChatterjee GourabSingh Kusum Kumari - Increased expression of lnc-FANCI-2, a newly discovered long noncoding RNA, is associated with cervical lesion progression from cervical intraepithelial neoplasia stage 1 (CIN1, low grade), CIN2-3 (high grade), to cervical cancer. Viral oncoprotein E7 of high-risk human papillomaviruses (HR-HPVs) and host transcription factor YY1 are two major factors promoting lnc-FANCI-2 expression. Using CRISPR-Cas9 technology, we knocked out the expression of in the HPV16-positive cervical cancer cell line, CaSki cells. The selected knockout (KO) single-cell clones displayed altered cell morphology and proliferation with changes of cellular soluble receptors, but normal HPV16 E6 and E7 expression. Relative to the parental cells, lnc-FANCI-2 KO cells exhibited significantly increased RAS signaling and epithelial-mesenchymal transition, but decreased response to IFN signaling, along with increased p-Akt and p-Erk1/2 (two RAS signaling effectors), IGFBP3, MCAM, VIM, and CCND2 (cyclin D2) and decreased expression of RAC3. lnc-FANCI-2 in CaSki interacts with cellular proteins H13, HNRH1, K1H1, MAP4K4, and RNPS1. MAP4K4 knockdown led to enhance the expression of p-Erk1/2 and p-Akt. High lnc-FANCI-2 and low MCAM levels in cervical cancer tissues were found to be associated with patients' survival. A key function of lnc-FANCI-2 intrinsically regulates RAS signaling to impact cervical lesion progression and cervical cancer prognosis. - Source: PubMed
Publication date: 2025/08/29
Liu HaibinYu LuluMajerciak VladimirMeyer Thomas JYi MingJohnson Peter FCam MaggieLowy Douglas RZheng Zhi-Ming - SF3B4, a splicing factor known to regulate mRNA expression and function, is upregulated in various cancers. Despite its potential significance, the mechanisms through which SF3B4 regulates nonsense-mediated mRNA decay (NMD) and cancer cell senescence remain poorly understood. This study explores the underlying mechanisms by which SF3B4 modulates mRNA stability through the NMD pathway and elucidates its role in switching cancer cells between growth and senescence. We demonstrate that SF3B4 deficiency leads to decreased cancer cell proliferation, increased senescence-associated β-galactosidase (SA-β-Gal) activity, p53-independent upregulation of p21 expression, and ultimate induction of cell senescence. We further show that SF3B4 recruits essential NMD factors, including UPF1, MAGOH, and RNPS1, which facilitate mRNA decay of the crucial senescence regulator, p21. Conversely, SF3B4 depletion results in the dissociation of these factors from the 3'UTR of p21 mRNA, thereby enhancing its stability. Collectively, our results suggest that SF3B4 critically regulates p21 expression at the post-transcriptional level, providing insights into the novel role of SF3B4 in regulating p21 mRNA stability, interacting with key NMD factors, and modulating cancer cell senescence. - Source: PubMed
Publication date: 2025/02/15
Kang DongheeSung Jee YoungHwang Hyun JungBaek YurimKim Min-JiLim Ga-EunKim Yong-NyunCha Jong-HoLee Jae-Seon