Ask about this productRelated genes to: RBM12 antibody
- Gene:
- RBM12 NIH gene
- Name:
- RNA binding motif protein 12
- Previous symbol:
- -
- Synonyms:
- HRIHFB2091, KIAA0765, SWAN
- Chromosome:
- 20q11.22
- Locus Type:
- gene with protein product
- Date approved:
- 2000-06-28
- Date modifiied:
- 2018-03-26
Related products to: RBM12 antibody
Related articles to: RBM12 antibody
- Atherosclerosis is a pathophysiological process common to a range of cardiovascular diseases. We reasoned that considering clinical presentations of atherosclerosis across the coronary, peripheral, and cerebrovasculature as a single entity would enhance statistical power to identify rare genetic variation driving pathological processes across multiple vascular beds. - Source: PubMed
Publication date: 2025/11/05
Lockhart Sam MPuri AnuradhikaZhao YajieSaudek VladimirGardner Eugene JKentistou Katherine ALam Brian Y HDay Felix RO'Rahilly StephenPerry John R BOng Ken KJackrel Meredith E - Profiling the protein interactome of specific RNA loci aids in understanding the molecular mechanisms of regulatory RNA. However, current RNA-centric methods have sufficient space for improvement in terms of efficiency and biocompatibility. Here we developed TurboID-assisted proximity labeling of targeted RNA-interacting proteins (TAPRIP), in which the proximity labeling enzyme miniTurbo is attached to an RNA-targeting element, CIRTS3, to label the targeted RNA-interacting proteins, which are then analyzed by mass spectrometry. We profiled the interactome of mCherry circular RNA (circRNA) and found that HNRNPK modulates the expression of mCherry circRNA and other endogenous circRNAs by binding their flanking introns. Targeting the BCL2 RNA G-quadruplex structure, we found that RBM12 promotes BCL2 translation by binding RNA G-quadruplexes and recruiting ribosomes. RBM12 knockdown markedly reduced proliferation and clonogenicity in MOLM-13, MV4-11 and THP-1 acute myeloid leukemia cells. These findings established the foundation for a versatile technique for analyzing the protein interactome of specific RNA sequences in live cells. - Source: PubMed
Publication date: 2025/08/07
Mo JingChen ZongguiCui ManmanFang XinLi RuihanQin ShanshanZhou ZhenlinSun MeiWu JinjunHe ChuanWang FangZhang HaojianZhou XiangWeng Xiaocheng - Biomolecular condensates segregate nuclei into discrete regions, facilitating the execution of distinct biological functions. Here, it is identified that the WW domain containing adaptor with coiled-coil (WAC) is localized to nuclear speckles via its WW domain and plays a pivotal role in regulating alternative splicing through the formation of biomolecular condensates via its C-terminal coiled-coil (CC) domain. WAC acts as a scaffold protein and facilitates the integration of RNA-binding motif 12 (RBM12) into nuclear speckles, where RBM12 potentially interacts with the spliceosomal U5 small nuclear ribonucleoprotein (snRNP). Importantly, knockdown of RBM12, or deletion of the WAC CC domain led to altered splicing outcomes, resulting in an elevated level of BECN1-S, the short splice variant of BECN1 that is shown to upregulate mitophagy. Thus, the findings reveal a previously unrecognized mechanism for the nuclear regulation of mitochondrial function through liquid-liquid phase separation (LLPS) and provide insights into the pathogenesis of WAC-related disorders. - Source: PubMed
Publication date: 2025/01/22
Wang JiaheFan YiLuo GuowenXiong LiangWang LijieWu ZhuoxuanWang JiayiPeng ZhengyingRosen Clifford JLu KefengJing JunjunYuan QuanZhang ZhenweiZhou Chenchen - Immunosuppression characterizes the tumour microenvironment in HCC, and recent studies have implicated RNA-binding proteins (RBPs) in the development of HCC. Here, we conducted a screen and identified RBM12 as a key protein that increased the expression of PD-L1, thereby driving immune evasion in HCC. Furthermore, RBM12 was found to be significantly upregulated in HCC tissues and was associated with a poor prognosis for HCC patients. Through various molecular assays and high-throughput screening, we determined that RBM12 could directly bind to the JAK1 mRNA via its 4th-RRM (RNA recognition motif) domain and recruit EIF4A2 through its 2nd-RRM domain, enhancing the distribution of ribosomes on JAK1 mRNA, which promotes the translation of JAK1 and the subsequent upregulation of its expression. As a result, the activated JAK1/STAT1 pathway transcriptionally upregulates PD-L1 expression, facilitating immune evasion in HCC. In summary, our findings provide insights into the significant contribution of RBM12 to immune evasion in HCC, highlighting its potential as a therapeutic target in the future. This graphical abstract shows that elevated expression of RBM12 in HCC can augment PD-L1-mediated tumour immune evasion by increasing the efficiency of JAK1 mRNA translation. - Source: PubMed
Publication date: 2024/08/26
Han HexuShi QianZhang YueDing MingdongHe XianzhongLiu CuixiaZhao DakunWang YifanDu YanpingZhu YichaoYuan YinWang SiliangGuo HuiminWang Qiang - Hepatocellular Carcinoma (HCC), also called hepatocellular cancer, has emerged as a highly prevalent malignancy globally. By binding to specific RNA via one or more spherical RNA Domains (RBDs) or RNA Motifs (RBMs), RNA Binding Proteins (RBPs) can affect RNA modification, splicing, localization, translation, and stability. - Source: PubMed
Publication date: 2023/10/02
Gao ChengZhu RenfeiShen JianboXu TianxinShe YongJunChen Zhong