Ask about this productRelated genes to: RBM38 antibody
- Gene:
- RBM38 NIH gene
- Name:
- RNA binding motif protein 38
- Previous symbol:
- RNPC1
- Synonyms:
- HSRNASEB, SEB4D, seb4B, dJ800J21.2
- Chromosome:
- 20q13.31
- Locus Type:
- gene with protein product
- Date approved:
- 2001-09-17
- Date modifiied:
- 2014-11-19
Related products to: RBM38 antibody
Related articles to: RBM38 antibody
- RNA-binding proteins (RBPs) regulate RNA metabolism at multiple levels and are essential mediators of post-transcriptional gene regulation in a wide range of physiological and pathological processes. The Rbm24/38 family is a conserved group of RRM-containing RBPs. In invertebrates, Rbm24/38 homologs are generally present as single-copy genes, whereas vertebrates possess two paralogs, Rbm24 and Rbm38, reflecting the progressive elaboration of posttranscriptional regulatory networks during evolution. Functional evidence for non-vertebrate Rbm24/38 homologs remains limited; the nematode protein SUP-12 has been primarily implicated in the regulation of pre-mRNA splicing during myogenesis. By contrast, vertebrate Rbm24 and Rbm38 exhibit broader spatial expression patterns across multiple tissues. Although their expression domains partially overlap, they also display clear gene- and species-specific differences. Functionally, vertebrate Rbm24 and Rbm38 contribute to multilayered post-transcriptional regulation through mechanisms such as alternative splicing, mRNA stability control, and alternative polyadenylation. In addition, regulatory features including isoform diversity, phase-separation potential, and post-translational modifications may further expand their functional versatility, enabling them to coordinate cell fate decisions and tissue homeostasis in distinct physiological contexts. In this review, we summarize recent advances in the evolution, structure, expression, molecular regulation, and biological functions of the Rbm24/38 family. We highlight its conserved features and functional diversification, as well as key unresolved questions regarding its evolution and specialization across metazoans. - Source: PubMed
Zhang XiangminZhang AilongBai ZongbaoLi Hongyan - Mutations in BRCA1 are key drivers of breast cancer by impairing homologous recombination. While these tumors are often sensitive to PARP inhibitors, resistance frequently emerges, highlighting the need to identify additional molecular vulnerabilities. HORMAD1 is frequently overexpressed in triple-negative breast cancer and associated with genomic instability, yet its role in therapy response in BRCA1-deficient tumors remains unclear. Here, transcriptomic profiling of BRCA1-mutant breast cancer identified as one of the most upregulated and alternatively spliced genes. The splicing inhibitor isoginkgetin globally altered alternative splicing patterns in BRCA1-mutant cells, promoting exon 4 inclusion. We found that RNA-binding protein RBM38 is correlated with exon 4 inclusion, and RBM38 knockdown further sensitized BRCA1-mutant cells to inhibition. Together, these findings define an RBM38-HORMAD1 signaling as a potential therapeutic vulnerability in BRCA1-mutant breast cancer and suggest that targeting splicing regulation may represent a promising strategy to enhance treatment efficacy. - Source: PubMed
Publication date: 2026/08/17
Sun ChenyanLuo HuachengZhang Jing - Serine/threonine-proline (S/T-P) phosphorylation is a fundamental mechanism maintaining cellular homeostasis. Although glycogen synthase kinase 3β (GSK3β) is a key regulator in ischemic stroke, the contribution of its proline-directed kinase activity to cellular dysfunction and disease progression remains unclear. Here, we developed Nb.29E9, a nanobody that selectively targets the proline-directed kinase domain of GSK3β. Under ischemic conditions, Nb.29E9 inhibited S/T-P phosphorylation of key substrates, including RNA-binding motif protein 38 (RBM38), HIF1α, and p53, thereby enhancing neuronal and microglial viability while reducing oxidative stress and neuroinflammation. Phosphoproteomic analysis revealed broad reprogramming of S/T-P phosphorylation networks. In mice after ischemic injury, Nb.29E9 delivered via a brain-penetrant, MMP-9-responsive nanoparticle reduced infarct volume, restored neurovascular integrity, and improved motor function. Mechanistically, Nb.29E9 corrected pathological hyperphosphorylation of SMAD2/3-Thr8 (TGFβ signaling), calcium/calmodulin-dependent protein kinase kinase 2 (CAMKK2)-Ser495 (AMPK pathway), and AKT1 substrate 1 (AKT1S1)-Ser183 (mTORC1 regulation). These findings demonstrate that GSK3β's intrinsic proline-directed kinase activity drives ischemic neurodegeneration, establishing its pathogenic role in vivo. - Source: PubMed
Publication date: 2026/06/09
Li LanLi MuyangSun LeiYang YingWu YuanshunYin ZiyiWang AnniZhou PeiyangLuo ShaoxiangChen JianQin JunAi ZhibingYuan ZilongDong ZhiqiangZhang Min - RNA-binding proteins (RBPs) are critical regulators of mRNAs controlling all processes such as RNA transcription, transport, localization, translation, mRNA:ncRNA interactions, and decay. Cellular differentiation is driven by temporally and spatially regulated expression of proteins needed for the optimal function of individual cells, tissues and organs. Lens fiber cell differentiation is marked by high levels of expression of crystallin genes encoding critical proteins for lens transparency and light refraction. Herein we performed proteomic and transcriptomic analyses of RBPs in differentiating mouse lenses to identify the most abundant RBPs and establish dynamic changes of their expression in differentiating lenses. Expression analyses showed highly abundant RBPs, including Carhsp1, Igf2bp1/ZBP1, Ybx1, Pabpc1, Ddx39, and Rbm38. Binding sites of Carhsp1, the most abundant lens RBP, were predicted in various crystallin and β-actin mRNAs. Immunoprecipitations using Carhsp1-specific antibodies confirmed interactions of Carhsp1 with crystallin mRNAs in newborn lens. A combination of single molecule RNA FISH (smFISH) and immunofluorescence was used to probe in vivo interactions of Carhsp1 with αA-, αB-crystallin, and β-actin mRNAs in cytoplasm and nucleoplasm of cultured mouse lens epithelial cells. These experiments favor a working model of direct association of Carhsp1 mediated by multiple candidate binding sites within both αA-, αB-crystallin mRNAs. Together, these results open new avenues to perform comprehensive genetic, cell, and molecular biology studies of individual RBPs in the lens. - Source: PubMed
Publication date: 2026/04/28
Rayêe DanielleHwang Dong-WooChang William KKarp Ilana NCoomson Sarah YZhao YilinBowman TeresaLachke Salil ASinger Robert HEliscovich CarolinaCvekl Ales - - Source: PubMed