Ask about this productRelated genes to: RBM45 antibody
- Gene:
- RBM45 NIH gene
- Name:
- RNA binding motif protein 45
- Previous symbol:
- -
- Synonyms:
- DRB1, FLJ44612
- Chromosome:
- 2q31.2
- Locus Type:
- gene with protein product
- Date approved:
- 2007-07-26
- Date modifiied:
- 2014-11-19
Related products to: RBM45 antibody
Related articles to: RBM45 antibody
- RNA-binding motif protein 45 (RBM45) is an RNA-binding protein crucial for brain development and plays a key role in RNA metabolism and disease. Its RNA recognition motif (RRM) domains can recognize GAC-containing motifs, with or without N6-methyladenosine (mA) modification. While its RRM domains individually do not preferentially recognize mA, RBM45 preferentially recognizes mA motifs over unmodified motifs. In this study, we used molecular dynamics (MD) simulations to investigate the binding of a series of RNAs in complex with different RRM domains individually and in complex with RRM3 in the context of the full-length protein. Our study complies with previous experiments and provides in-depth biophysical insights into the binding of unmodified and mA-modified GACG, GACU, and GACA RNA motifs in complex with all RRMs individually. While GACA and GACU bind unfavorably to the individual RRM3 domain, we suggest that they bind favorably to RRM3 in the context of the full-length protein. Importantly, in the context of the entire protein, we present for the first time how RRM3, in combination with additional residues in different RRM domains and linker domains, can synergistically cooperate for mA preferential binding over adenine in the context of GACA and GACU motifs, uncovering the preferential binding of full-length RBM45 for mA observed in previous experiments. The presence of the mA methyl group provides further stability to the RNA, as well as strengthens the particular interactions between RNA and protein, while contributing to additional stabilization of the C-terminal domain with the linker domain between RRM2 and homo-oligomer assembly (HOA). Our simulations highlight the role of various other domains beyond RRMs (i.e., the C-terminal, HOA, and linkers between different RRMs) in the interaction of RBM45 with RNA, particularly mA-modified RNA. Overall, our study elucidated how an RRM class of proteins can preferentially bind mA in the context of its common motif written by methyltransferases. We consider that our study presents the first mechanistic insights into how an RRM domain binds directly and preferentially recognizes mA over adenine in synergy with other domains, which include intrinsically disordered regions. - Source: PubMed
Publication date: 2026/05/14
Park RaeyeonContreras Lydia MTamamis Phanourios - Non-small cell lung cancer (NSCLC) is one of the leading causes of cancer-related mortality worldwide. Its high incidence and poor prognosis are closely associated with complex molecular mechanisms. Circular RNAs (circRNAs), a class of non-coding RNAs, play significant regulatory roles in tumorigenesis and progression. However, their specific functions and mechanisms in lung cancer remain largely unclear. This study aims to elucidate the expression pattern and molecular mechanisms of circ0515 in lung cancer, particularly its roles in tumor proliferation, migration, and metabolism. The study revealed that circ0515 is significantly upregulated in lung cancer tissues and cell lines, specific knockdown of circ0515 using short hairpin RNA (shRNA) or antisense oligonucleotide (ASO) significantly inhibits lung cancer cell proliferation, migration, and xenograft tumor formation. On one hand, circ0515 acts as a molecular sponge for miRNA-328-3p, upregulating its downstream target gene YWHAZ, thereby activating the AKT signaling pathway and significantly promoting lung cancer cell proliferation and migration. On the other hand, circ0515 recruited RNA binding motif protein 45 (RBM45) to stabilize SDHB mRNA, promoting SDHB expression and mitochondrial oxidative phosphorylation and succinate metabolism, leading to increased cisplatin resistance in lung cancer cells. These findings not only advance our understanding of the functional roles of circ0515 in lung cancer but also provide a theoretical basis for considering circ0515 as a potential therapeutic target for NSCLC. - Source: PubMed
Publication date: 2025/07/05
Yuan YixiaoWu YueLi ChunhongHuang ZuotianPeng DadiWu ZhongjunJiang Xiulin - The cellular thermal shift assay (CETSA) and isothermal dose-response fingerprint assay (ITDRF ) have been introduced as powerful tools for investigating target engagement by measuring ligand-triggered thermodynamic stabilization of cellular target proteins. Yet, these techniques have rarely been used to evaluate the thermal stability of RNA-binding proteins (RBPs) when exposed to ligands. Here, we present an adjusted approach using CETSA and ITDRF to determine the interaction between enasidenib and RBM45. Our assay is sensitive and time-efficient and can potentially be adapted for studying the interactions of RBM45 protein with other potential candidates. Key features • This protocol builds upon the method developed by Molina et al. and extends its application to new protein classes, such as RBPs. - Source: PubMed
Publication date: 2024/08/05
Du DanyuYuan ShengtaoXiong Jing - RBM45 is an RNA-binding protein with roles in neural development by regulating RNA splicing. Its dysfunction and aggregation are associated with neurodegenerative diseases such as amyotrophic lateral sclerosis (ALS) and frontotemporal lobar dementia (FTLD). RBM45 harbors three RRM domains that potentially bind RNA. While the recognitions of RNA by its N-terminal tandem RRM domains (RRM1 and RRM2) have been well understood, the RNA-binding property of its C-terminal RRM (RRM3) remains unclear. In this work, we identified that the RRM3 of the RBM45 sequence specifically binds RNA with a GACG sequence, similar but not identical to those recognized by the RRM1 and RRM2. Further, we determined the crystal structure of RBM45 in complex with a GACG sequence-containing single-stranded DNA. Our structural results, together with the RNA-binding assays of mutants at key amino acid residues, revealed the molecular mechanism by which RBM45 recognizes an RNA sequence. Our finding on the RNA-binding property of the individual RRM module of RBM45 provides the foundation for unraveling the RNA-binding characteristics of full-length RBM45 and for understanding the biological functions of RBM45. - Source: PubMed
Publication date: 2024/08/08
Chen XiWei QinghaoYang ZhongmeiChen XiaoleiGuo ShuoxuanJiang MeiyuWang Mingzhu - The F11 receptor (F11R) gene encoding junctional adhesion molecule A has been associated with gastric cancer (GC) and colorectal cancer (CRC), in which its role and regulation remain to be further elucidated. Recently F11R was also identified as a potential target of adenosine-to-inosine (A-to-I) mediated by the adenosine deaminases acting on RNA (ADARs). Herein, using RNA-Seq and experimental validation, our current study revealed an F11R RNA trinucleotide over-edited by ADAR, with its regulation of gene expression and clinical significance in four GC and three CRC cohorts. Our results found an over-edited AAA trinucleotide in an AluSg located in the F11R 3'-untranslated region (3'-UTR), which showed editing levels correlated with elevated ADAR expression across all GC and CRC cohorts in our study. Overexpression and knockdown of ADAR in GC and CRC cells, followed by RNA-Seq and Sanger sequencing, confirmed the ADAR-mediated F11R 3'-UTR trinucleotide editing, which potentially disrupted an RBM45 binding site identified by crosslinking immunoprecipitation sequencing (CLIP-seq) and regulated F11R expression in luciferase reporter assays. Moreover, the F11R trinucleotide editing showed promising predictive performance for diagnosing GC and CRC across GC and CRC cohorts. Our findings thus highlight both the potential biological and clinical significance of an ADAR-edited F11R trinucleotide in GC and CRC, providing new insights into its application as a novel diagnostic biomarker for both cancers. - Source: PubMed
Publication date: 2024/06/01
Bao ChuanqingFeng Jun-JieCui JingGuo TaoHe Yu-ShanWei Zhi-YuanQian Cheng-JiaJin Yun-YunChen Jian-Huan