Ask about this productRelated genes to: WTAP antibody
- Gene:
- WTAP NIH gene
- Name:
- WT1 associated protein
- Previous symbol:
- -
- Synonyms:
- KIAA0105, MGC3925, Mum2
- Chromosome:
- 6q25.3
- Locus Type:
- gene with protein product
- Date approved:
- 2003-05-19
- Date modifiied:
- 2017-02-28
Related products to: WTAP antibody
Related articles to: WTAP antibody
- Lung cancer remains the leading cause of cancer-related mortality worldwide, largely due to therapeutic resistance and tumor progression. Mitochondrial ribosomal proteins (MRPs), particularly MRPS23, have recently emerged as critical regulators of cancer progression in various malignancies, while N6-methyladenosine (mA) modification has been established as a key epigenetic mechanism driving tumorigenesis. However, whether MRPS23 is regulated by mA modification and contributes to lung cancer pathogenesis remains completely unexplored. Here, we identified MRPS23 as a critical oncogenic driver in non-small cell lung cancer (NSCLC). MRPS23 expression was significantly upregulated in NSCLC tissues and cell lines, and high MRPS23 levels correlated with poor patient prognosis. Mechanistically, we demonstrated that WTAP-mediated mA methylation and subsequent IGF2BP3 recognition stabilized MRPS23 mRNA. Functionally, MRPS23 promoted lung cancer progression both in vitro and in vivo. Further mechanistic studies revealed that MRPS23 exerted its oncogenic effects through physical interaction with the molecular chaperone HSPA8, and this interaction was functionally associated with activation of the RAS-RAF-MEK-ERK signaling cascade. However, the precise molecular steps linking the MRPS23-HSPA8 complex to ERK phosphorylation remain to be fully defined. Collectively, our findings unveil a previously unrecognized mA-dependent MRPS23/HSPA8/ERK regulatory axis in NSCLC progression, highlighting MRPS23 and its associated components as promising prognostic biomarkers and therapeutic targets. - Source: PubMed
Publication date: 2026/08/13
Le SihongLe YitaoSha XianshenQiu FengZhang Ling - Diabetic cataract (DC) is a lens-opacity complication of diabetes driven by hyperglycemia-related oxidative, apoptotic, metabolic, and epithelial-mesenchymal transition (EMT) pathways. This review evaluated the expression and mechanistic roles of long non-coding RNAs (lncRNAs) and lncRNA-related epitranscriptomic regulators in DC. - Source: PubMed
Publication date: 2026/08/12
Chen Kai-YangChan Hoi-ChunChan Chi-Ming - Osteoarthritis (OA) arises from chondrocyte senescence driven by intertwined oxidative stress and abnormal m6A methylation, with few treatments targeting both pathological pathways. Lycopene, an antioxidant, is limited by poor bioavailability, whereas Wilms tumor 1-associating protein (WTAP), a core m6A methyltransferase, has no specific inhibitors. Herein, we fabricated cartilage-targeted HPcLW nanoparticles (∼250 nm) via electrostatic self-assembly of human serum albumin (HSA) and poly-L-lysine (PLL) with collagen II-binding peptide, co-loaded with lycopene and WTAP siRNA. The targeting modification extended joint fluorescence retention to 10 days after intra-articular injection with good serum stability and biosafety. In aged mice and medial meniscus (DMM)-induced OA mouse models, intra-articular HPcLW attenuated cartilage degeneration, restored COL2 expression, and suppressed MMP13 levels. Mechanistically, WTAP siRNA suppressed m6A modification to downregulate PAI-1 expression, while lycopene scavenged ROS and protected siRNA integrity, cooperatively disrupting the WTAP/PAI-1 axis and alleviating mitochondrial dysfunction. By integrating antioxidant and epigenetic strategies, HPcLW counteracts the senescence loop, establishing the WTAP/PAI-1 axis as a therapeutic target and highlighting co-delivery nanomedicine for age-related joint diseases. - Source: PubMed
Publication date: 2026/07/31
An XueyingCai HantaoWu WenshuCai MinyiBen YuShen TaoZhang PanChen JianmeiXu ZhihongJiang Qing - N-methyladenosine (mA) RNA modification plays critical roles in physiological and pathological processes. Our prior study demonstrated that IGFBP5 expression is upregulated in the ischemic limb, whereas endothelial-specific IGFBP5 knockout (Igfbp5) protects against hind limb ischemia by enhancing angiogenesis. Here, we show that IGFBP5 deficiency elevates global mA levels and upregulates the expression of mA methyltransferase complex components METTL3, METTL14 and WTAP in endothelial cells. We further identified a direct interaction between IGFBP5 and the MT-A70 domain of METTL14. Knockdown of METTL14, METTL3 or WTAP attenuated the pro-angiogenic effects of IGFBP5 deficiency in vitro. In vivo, endothelial knockdown of METTL14 abolished the improved hind-limb ischemia recovery in Igfbp5 mice. Methylated RNA immunoprecipitation sequencing revealed that IGFBP5 depletion in endothelial cells increases both mA modification and mRNA abundance of FGF16. Notably, METTL14 or METTL3 silencing suppressed IGFBP5-dependent FGF16 upregulation. Enhanced translational efficiency of FGF16 in IGFBP5-deficient cells was reversed by METTL14 knockdown, indicating that IGFBP5 regulates FGF16 translation via mA modification. Mechanistically, IGFBP5 modulates FGF16 mA modification via interaction with the mA reader protein IGF2BP2, targeting the mA site at position 255 of FGF16 mRNA. In summary, our study establishes METTL14-mediated mA modification of FGF16 as a key mechanism underlying IGFBP5-driven angiogenesis. Targeting the IGFBP5-METTL14-mA-FGF16 axis may offer novel therapeutic strategies for ischemic disease. - Source: PubMed
Publication date: 2026/08/04
Song FeiHu YuHong Yi-XiangZhao Shan-ShanHuang Hui-ZhuWang YutianZhang LeWu Wei-YinWang YanLi Gang - Lactate, a metabolic byproduct of glycolysis, accumulates during myocardial infarction and ischemia/reperfusion (I/R) injury, acting as both a metabolic stress marker and a signaling molecule that influences inflammation and cell fate. Lactate can induce histone lysine lactylation (Kla), a novel post-translational modification that regulates gene transcription and immune responses. Despite this discovery, its role in I/R injury remains unclear. To investigate the effects of lactate and histone lactylation, both in vivo myocardial I/R injury and in vitro hypoxia/reoxygenation (H/R) injury models using cardiomyocytes were established. Lipid peroxidation, LDH, MDA, SOD, and iron levels were quantified using specialized fluorescent probes and commercial kits. MeRIP and RIP assays were performed to investigate WTAP, YTHDF1, and ALOX15 interactions. TEM was utilized to examine mitochondrial ultrastructure and morphology. Lactate levels were elevated in I/R rats, and reducing lactate levels effectively mitigated ferroptosis and myocardial injury. Furthermore, lactate promoted Kla of WTAP, resulting in upregulation of WTAP protein expression compared to the I/R group. Global mA RNA methylation levels increased by lactate treatment. Elevated WTAP levels, or overexpression of YTHDF1, facilitated m6A modification of ALOX15 mRNA, leading to upregulation of ALOX15 expression and enhanced ferroptosis during I/R injury. Notably, overexpression of ALOX15 reversed the protective effects of WTAP knockdown. Finally, we validated the involvement of the WTAP-YTHDF1-ALOX15 regulatory axis in vivo. Lactate-induced Kla of WTAP led to its upregulation, which, together with YTHDF1, facilitated the m6A modification of ALOX15 mRNA. This modification increased ALOX15 expression, triggering cardiomyocyte ferroptosis and worsening myocardial I/R injury. These findings highlight the potential of targeting lactate-induced Kla and its downstream effectors, including WTAP, YTHDF1, and ALOX15, as therapeutic strategies. - Source: PubMed
Liu WeiWang YuqinWu JiayuanHe CaihongZhou Zhengwei