Ask about this productRelated genes to: RBM14 Blocking Peptide
- Gene:
- RBM14 NIH gene
- Name:
- RNA binding motif protein 14
- Previous symbol:
- -
- Synonyms:
- SIP, SYTIP1, COAA, DKFZp779J0927
- Chromosome:
- 11q13.2
- Locus Type:
- gene with protein product
- Date approved:
- 2001-02-06
- Date modifiied:
- 2014-11-19
Related products to: RBM14 Blocking Peptide
Related articles to: RBM14 Blocking Peptide
- Heart specialization involves nuclear programs however, chamber-specific regulation of the nuclear proteome landscape remains unknown. In this study we isolated the nucleus from four major anatomical regions of healthy mouse heart (fresh) and employed quantitative mass spectrometry-based proteomics to construct a comprehensive nuclear proteome landscape of left ventricle (LV, 2403 proteins), right ventricle (RV, 2242 proteins), left atrium (LA, 2368 proteins), right atrium (RA, 1816 proteins). This led to the discovery of nuclear regional proteome signatures [ventricular signature, 297 proteins; atrial signature, 183 proteins]; associated with oxidative metabolism and redox regulation, ferroptosis, extracellular-matrix remodeling, SUMO- and stress-responsive control and transcriptional regulation. Chamber-level analyses further identify distinct nuclear features in LV (120 proteins), LA (188 proteins), and RA (72 proteins). In addition, we defined conserved core nuclear proteome (230 proteins) shared across all anatomical regions, enriched for transcription-regulator complexes, nucleolar/ribosome-associated, RNA-processing, and chromatin-organization components. Within this core network we report 78 transcription factors/co-factors and select nuclear, chromatin and RNA export-associated proteins including 29 specific factors (e.g., Alpk3, Rbm14, Arglu1, Hmgb1, Myef2, Sf1) associated with the heart. Regionally, we verified spatial localization in heart of H2ac21 and Sun2 in LA and Ptbp2 in LV by immunofluorescence. This study provides insights into the chamber-resolved view of the nuclear proteome in the heart, establishes a framework for linking nuclear proteomic signatures to atrial and ventricular biology, unique features of the heart nuclear proteome landscape relative to other organs, and a baseline for studying nuclear remodeling in cardiac pathophysiology. - Source: PubMed
Publication date: 2026/05/14
Eslami Seyed SadeghRai AlinFang HaoyunThomas AnitaCross JonathonDonner DanielGreening David W - Metastasis is a leading cause of poor prognosis in prostate cancer (PCa), yet its underlying regulatory mechanisms remain incompletely understood. Following the establishment of highly invasive PC-3M cell lines, RBM14 expression was found to be significantly elevated in highly invasive cells. Furthermore, RBM14 was upregulated in PCa tissues and positively correlated with adverse clinicopathological features. Functional assays demonstrated that RBM14 significantly promoted PCa cell metastasis in vitro and in vivo. Mechanistically, RBM14 bound HK2 mRNA via its RRM1/2 domains to enhance HK2 stability, thereby upregulating HK2 expression. This increased HK2 level boosted PCa cells' glycolytic capacity, which in turn led to increased global lactylation, especially in histone H3 lysine 18 lactylation (H3K18la). The elevated H3K18la preferentially enriched at the promoters of metastasis-related genes, further upregulating their expression. Importantly, combining RBM14 knockdown with 2-DG exerted a synergistic inhibitory effect on PCa metastasis. Collectively, this study identifies RBM14 as a key regulator of PCa metastasis via the HK2-glycolysis-H3K18la axis, providing a potential therapeutic target for combating PCa metastasis. - Source: PubMed
Publication date: 2026/04/30
Liu ZhenhongGuo HaixinYou ZhijiaoLin HaichaoLiu WeihuiChen JiabiHe QingliuZhuang Wei - Phosphorylation of alpha-synuclein (αsyn) at serine 129 (PS129) marks aggregates in synucleinopathies but also occurs physiologically, potentially signaling protein interactions during neuronal activity. Technical barriers, including postmortem dephosphorylation, have hindered the study of physiological PS129 in the human brain. Using biotinylation by antibody recognition (BAR) on surgically resected temporal lobectomy tissues (without post-mortem interval), we mapped physiological PS129 and total αsyn interactomes. BAR identified 1,095 interactions with 513 αsyn-specific, 524 shared, and 58 PS129-specific, mostly associated with vesicles at presynaptic nerve terminals. PS129-specific interactions were uniquely associated with postsynaptic density proteins SHANK1/3, DLGAP1-4, DLGAP1-3, and DLG2-4, as well as nuclear-associated proteins HUWE1, HNRNPM, RBM14, ITCH, OGT, PHF24, and PPP2R5E. Fluorescent staining confirmed physiological PS129 proximal to dendrites and within the nucleus. Confirmation in healthy cynomolgus macaques (62% αsyn and 41% PS129 overlap) demonstrated that the interactomes were physiological rather than disease- or aggregate-associated. We conclude that physiological PS129 plays a unique and underappreciated role in postsynaptic neurons extending from the postsynaptic active zone to the nucleus. These interactomes benchmark normal αsyn biology, illuminating the transition to synucleinopathy pathology. - Source: PubMed
Publication date: 2025/11/27
Choi Solji GDuvernay Jayda BBahrami AtousaTittle TylerSani SepehrKordower Jeffrey HMuller ScottKillinger Bryan A - Radiation-induced damage to reproductive tissues presents a major clinical concern with potentially lasting functional consequences. - Source: PubMed
Publication date: 2025/11/26
Zhu LingfengZhang JianpingLiang YaoyaoCheng YuanhangLin NaDeng WenyiLin LinglingChen Jin - Metastasis serves as an indicator of malignancy and is a biological characteristic of carcinomas. Epithelial-mesenchymal transition (EMT) plays a key role in the promotion of tumor invasion and metastasis and in the enhancement of tumor cell aggressiveness. Prostaglandin E synthase 3 (p23) is a cochaperone for heat shock protein 90 (HSP90). Our previous study showed that p23 is an HSP90-independent transcription factor in cancer-associated inflammation. The effect and mechanism of action of p23 on lung cancer metastasis are tested in this study. By utilizing cell models and mouse tail vein metastasis models , the results provide solid evidence that p23 is critical for promoting lung cancer metastases by regulating downstream CXCL1 expression. Rather than acting independently, p23 forms a complex with RNA-binding motif protein 14 (RBM14) to facilitate EMT progression in lung cancer. Therefore, our study provides evidence for the potential role of the RBM14-p23-CXCL1-EMT axis in the metastasis of lung cancer. - Source: PubMed
Publication date: 2025/04/04
Zhang WenPeng YulinZhou MeirongQian LeiChe YilinChen JunlinZhang WenhaoHe ChengjianQi MinghangShu XiaohongTian ManmanTian XianggeTian YanDeng SaWang YanHuo XiaokuiYu ZhenlongMa Xiaochi