Ask about this productRelated genes to: SNRPD3 antibody
- Gene:
- SNRPD3 NIH gene
- Name:
- small nuclear ribonucleoprotein D3 polypeptide
- Previous symbol:
- -
- Synonyms:
- SMD3, Sm-D3
- Chromosome:
- 22q11.23
- Locus Type:
- gene with protein product
- Date approved:
- 1995-04-26
- Date modifiied:
- 2015-11-09
Related products to: SNRPD3 antibody
Related articles to: SNRPD3 antibody
- Alternative splicing (AS) serves as a pivotal post-transcriptional regulatory mechanism that drives tumorigenesis. Small nuclear ribonucleoprotein D3 (SNRPD3), an indispensable component of the spliceosome, is aberrantly expressed in multiple malignancies. Nevertheless, its biological functions and underlying mechanisms in the pathobiology of endometrial cancer (EC) remains unknown. We demonstrated that SNRPD3 was significantly upregulated in human EC tissues. Knockdown of SNRPD3 markedly inhibited EC cell proliferation, migration, and invasion in vitro and suppressed tumor growth in subcutaneous xenograft models. Mechanistically, silencing SNRPD3 increased intron retention in SREBF1 mRNA. Furthermore, depletion of SREBF1 abolished the enhanced proliferative capacity and lipid metabolism in both parental EC cells and SNRPD3-overexpressing EC cells. Notably, antisense oligonucleotides (ASOs)-mediated silencing of SNRPD3 markedly repressed EC cell growth and metastatic potential in vitro, and effectively impeded tumor progression in patient-derived xenograft (PDX) models. Collectively, our findings reveal that SNRPD3 serves as an oncogenic splicing factor that promotes EC proliferation and metastasis by regulating SREBF1 mRNA splicing. Given its potent antitumor efficacy in preclinical PDX models, ASO-targeted SNRPD3 may represent a promising therapeutic strategy for endometrial cancer. - Source: PubMed
Publication date: 2026/03/20
Li ZhaoChen ZhongshaoWu XuZhenJiang WenwenJin Ping - To identify novel marker genes to predict potential gestational diabetes mellitus (GDM) patients. - Source: PubMed
Publication date: 2025/10/21
Yu ShashaTan Huayun - Protein arginine methyltransferase 5 (PRMT5) catalyzes symmetric arginine dimethylation (Rme2s) of RNA-binding proteins and influences RNA splicing and gene expression. However, how PRMT5 couples splicing to productive transcript output remains unclear. We show that a major function of PRMT5 is to promote chromatin escape of mRNAs, designated as genomically retained incompletely processed polyadenylated transcripts (GRIPPs). Using nascent and spike-in normalized fractionated transcriptomics with proteomics, we find that PRMT5 inhibition in mammalian cells causes polyadenylated mRNA and Smith antigen (Sm) protein accumulation on chromatin. These retained transcripts are intron rich and splice slowly. PRMT5 inhibition and isogenic SNRPB mutants demonstrate that Sm tail methylation is essential to prevent RNA detention on chromatin. Biochemical assays reveal that the SMN Tudor domain competes with nucleic acid binding of methylated Sm tails. We conclude that PRMT5 ensures mRNA processing and nuclear export by preventing aberrant chromatin retention, highlighting arginine methylation as a key regulator of RNA-chromatin dynamics. - Source: PubMed
Publication date: 2025/10/13
DeAngelo Joseph DMaron Maxim IRoth Jacob SHegde SubraySilverstein Aliza MGupta VarunStransky StephanieBasken JoelAzofeifa JoeyQuery Charles CSidoli SimoneGamble Matthew JShechter David - ADAR is highly expressed and correlated with poor prognosis in hepatocellular carcinoma (HCC), yet the role of its constitutive isoform ADARp110 in tumorigenesis remains elusive. We investigated the role of ADARp110 in HCC and underlying mechanisms using clinical samples, a hepatocyte-specific knock-in mouse model, and engineered cell lines. ADARp110 is overexpressed and associated with poor survival in both human and mouse HCC. It creates an immunosuppressive microenvironment by inhibiting total immune cells, particularly cytotoxic GZMBCD8 T cells infiltration, while augmenting Treg cells, MDSCs, and exhausted CD8 T cells ratios. Mechanistically, ADARp110 interacts with SNRPD3 and RNPS1 to stabilize CD24 mRNA by inhibiting STAU1-mediated mRNA decay. CD24 protects HCC cells from two indispensable mechanisms: macrophage phagocytosis and oxidative stress. Genetic knockdown or monoclonal antibody treatment of CD24 inhibits ADARp110-overexpressing tumor growth. Our findings unveil different mechanisms for ADARp110 modulation of tumor immune microenvironment and identify CD24 as a promising therapeutic target for HCCs. - Source: PubMed
Publication date: 2025/01/14
Sun LiangzhanHu PengchaoYang HuiRen JunHu RongWu ShashaWang YanchenDu YuyangZheng JingyiWang FenfenGao HanYan JingsongYuan Yun-FeiGuan Xin-YuanXiao JiaLi Yan - Protein Arginine Methyltransferase 5 (PRMT5) regulates RNA splicing and transcription by symmetric dimethylation of arginine residues (Rme2s/SDMA) in many RNA binding proteins. However, the mechanism by which PRMT5 couples splicing to transcriptional output is unknown. Here, we demonstrate that a major function of PRMT5 activity is to promote chromatin escape of a novel, large class of mRNAs that we term Genomically Retained Incompletely Processed Polyadenylated Transcripts (GRIPPs). Using nascent and total transcriptomics, spike-in controlled fractionated cell transcriptomics, and total and fractionated cell proteomics, we show that PRMT5 inhibition and knockdown of the PRMT5 SNRP (Sm protein) adapter protein pICln (CLNS1A) -but not type I PRMT inhibition-leads to gross detention of mRNA, SNRPB, and SNRPD3 proteins on chromatin. Compared to most transcripts, these chromatin-trapped polyadenylated RNA transcripts have more introns, are spliced slower, and are enriched in detained introns. Using a combination of PRMT5 inhibition and inducible isogenic wildtype and arginine-mutant SNRPB, we show that arginine methylation of these snRNPs is critical for mediating their homeostatic chromatin and RNA interactions. Overall, we conclude that a major role for PRMT5 is in controlling transcript processing and splicing completion to promote chromatin escape and subsequent nuclear export. - Source: PubMed
Publication date: 2024/08/12
DeAngelo Joseph DMaron Maxim IRoth Jacob SSilverstein Aliza MGupta VarunStransky StephanieBasken JoelAzofeifa JoeySidoli SimoneGamble Matthew JShechter David