Ask about this productRelated genes to: FXR2 antibody
- Gene:
- FXR2 NIH gene
- Name:
- FMR1 autosomal homolog 2
- Previous symbol:
- FMR1L2
- Synonyms:
- -
- Chromosome:
- 17p13.1
- Locus Type:
- gene with protein product
- Date approved:
- 1999-05-17
- Date modifiied:
- 2019-04-23
Related products to: FXR2 antibody
Related articles to: FXR2 antibody
- N-methyladenosine (mA) modification constitutes a crucial layer of post-transcriptional regulations, but the landscape of its downstream readout effects remains less comprehensively understood. Therefore, we systematically assess the readout effects of mA on mRNA half-life, translation efficiency, and alternative splicing across five cell lines (A549, HEK293T, HUVEC, JURKAT, and human embryonic stem cells (hESCs)) using actinomycin D-disrupted temporal transcriptome, ribosome sequencing, and ultra-high-depth transcriptome sequencing, respectively. Our analysis, coupled with the integration of public and newly profiled mA methylome data, reveals high cell type specificity in mA readouts where mA level alone is insufficient to predict mA readouts. Nonetheless, machine learning models focusing on RNA-binding protein (RBP) binding context can effectively predict the readouts and prioritize four novel mA-associated proteins (FUBP3, FXR2, L1TD1, and DDX6). Their mA-binding ability is validated by mA RNA pull-down, transcriptome-wide binding site mapping, and electrophoretic mobility shift assay, while FUBP3 and L1TD1 are further suggested as mA readers regulating mRNA stability based on half-life profiling of knockout cells. Finally, FUBP3, FXR2, and L1TD1 are demonstrated to regulate hESC differentiation without affecting self-renewal. Together, this study bridges the gap in understanding mA functional readouts and lays the groundwork for future research on mA-mediated stem cell fate decisions. - Source: PubMed
Publication date: 2026/01/20
Huang ZhouLiu RucongWubulikasimu ZibaguliZhao WanqingHuang JiaqiWang JiaxuanZhang TianyuanFan RuiKong WeiCui QinghuaLi YangZhou Yuan - Trained immunity confers innate immune memory via metabolic and epigenetic reprogramming, yet the intercellular mediators regulating this process in host defense remain largely elusive. Here, through plasma exosomal profiling of tuberculosis (TB)-resistant individuals, we identify a trained immunity-inducing long non-coding RNA (lncRNA), termed tuberculosisresister-derived CLOCK regulator 1 (TRCR1). Mechanistically, exosome-derived TRCR1 collaborates with the RNA-binding protein FXR2 to stabilize CLOCK mRNA by forming lncRNA-protein-mRNA complexes in monocytes, thus enhancing circadian regulator CLOCK expression and promoting CLOCK-mediated histone H3 acetylation (K9/K14) at immune gene promoters, ultimately establishing epigenetic memory-mediated antimicrobial activity. We further reveal that Mycobacterium tuberculosis (Mtb)-secreted protein MPT53 induces lung epithelial cells to release TRCR1-enriched exosomes. In mice, TRCR1 training strengthens host anti-Mtb immunity and improves Bacille Calmette-Guérin (BCG) vaccine efficacy. Collectively, our findings unveil an intercellular TRCR1-FXR2-CLOCK axis driving trained immunity at the lung-systemic immune interface, providing a strategy for refining BCG vaccination and preventing infectious diseases. - Source: PubMed
Publication date: 2025/12/30
Yu ShanshanChai QiyaoLu ZheQiu ChanggenZhong YanzhaoWang YiruLei ZehuiQiang LihuaFang YingxuZhang XinwenLi BingxiGao MengqiuZhang LingqiangCheng GongWang JingLiu Cui HuaPang Yu - Loss of isozyme diversity (LID) refers to the selective dependency on a single isozyme following the functional collapse of its redundant counterparts, uncovering a metabolic vulnerability. This metabolic liability establishes LID as a novel framework for precision targeting strategy in cancer therapy. - Source: PubMed
Publication date: 2025/12/12
Ding RuiYu Tian-JianJiang Yi-ZhouXiao YiShao Zhi-Ming - Members of the fragile X protein (FXP) family (FMR1, FXR1 and FXR2) are differentially expressed in most types of cancer and major neurodegenerative diseases. While increased expression of FXR1 in cancer has been linked to senescence evasion and consequently tumor initiation and progression, decreased expression of FXPs in neurodegeneration may contribute to pathogenic protein aggregation and death of vulnerable neurons. However, due the causal role in fragile x syndrome, most data are available about loss of FMR1 in neurons while functions of FXR1 and especially FXR2 remain largely unexplored. To address this knowledge gap, and to directly compare functions of the FXPs, we used proteomics of CRISPR/Cas9 edited HAP1 cells carrying knockouts of the individual FXPs for identification of cellular mechanisms associated with these proteins. Further exploration of proteomic findings suggests roles of the FXPs in ribosome biogenesis, autophagy and mitochondrial health linked to organismal aging, and cellular senescence. Validation of FXP induced defects relevant for neurodegenerative diseases in neuroblastoma cell line SH-SY5Y upon FXP knockdown revealed high cell type specificity of individual FXP functions. Overall, we provide a comprehensive overview and comparison of cellular mechanisms related to the individual FXPs, as well as starting points for further studying this protein family in respective cell types of FXP associated diseases, and in aging in general. - Source: PubMed
Publication date: 2025/10/21
Menge SonjaSegura InmaculadaHartmann MaxDecker LorenaKiran SelinDanzer Karin MIben SebastianHarbauer Angelika BOeckl PatrickFreischmidt Axel - Ataxin-2 (ATXN2), a key RNA-binding protein, regulates RNA metabolism, stress granule formation, and neuronal homeostasis, with dysregulated phosphorylation contributing to Spinocerebellar Ataxia type 2 (SCA2), amyotrophic lateral sclerosis (ALS), and cancer. This review integrates structural biology, phosphoproteomics, and interactome analyses to map six critical phosphosites (S772, T741, S624, S684, S784, S889) within ATXN2's intrinsically disordered regions. Modulated by kinases GSK3β and CDK13 and phosphatases like INPP5F, these sites orchestrate interactions with RNA-binding partners (e.g., ATXN2L, FXR2, STAU2) and co-regulated proteins (e.g., TP53BP1, NUP153), driving pathogenesis through disrupted autophagy, nucleocytoplasmic transport, and stress granule dynamics. We propose targeted therapies, including GSK3β inhibitors for ALS, antisense oligonucleotides for SCA2, and MTOR modulators for cancer, to restore ATXN2 function. By elucidating phosphocode of ATXN2, this work highlights novel avenues for precision medicine in neurodegenerative and oncogenic diseases. - Source: PubMed
Publication date: 2025/08/30
Kalasa Anil Kumar Apoorva PaiSubair SuhailBasthikoppa Shivamurthy PrathikUmmar SamseeraRajeev Athira CRaju Rajesh