Ask about this productRelated genes to: IGF2BP1 antibody
- Gene:
- IGF2BP1 NIH gene
- Name:
- insulin like growth factor 2 mRNA binding protein 1
- Previous symbol:
- -
- Synonyms:
- IMP-1
- Chromosome:
- 17q21.32
- Locus Type:
- gene with protein product
- Date approved:
- 2006-02-09
- Date modifiied:
- 2015-11-23
Related products to: IGF2BP1 antibody
Related articles to: IGF2BP1 antibody
- IGF2BP1 stabilizes oncogenic mRNAs via m6A binding to drive lung adenocarcinoma (LUAD) progression, yet how this modification orchestrates immune evasion remains unclear. - Source: PubMed
Publication date: 2026/05/10
Xu YufenTan XiaoliLv XiaodongYang QiKe XingxingChen Wenyu - N6-methyladenosine (m6A) RNA-binding protein IGF2BP1 has been shown to play a significant role in cancer cell proliferation, cellular stress response, metastasis, and immune modulation. However, its specific function and regulatory mechanism in laryngeal squamous cell carcinoma (LSCC) have not been fully elucidated. Clinically, IGF2BP1 expression was markedly upregulated in 30 cases of LSCC tissue samples and was correlated with poor patient prognosis. Functionally, loss- and gain-of-function studies demonstrated that IGF2BP1 promoted the proliferation, invasion, and migration of LSCC cells in vitro, while knockdown of IGF2BP1 inhibited tumor growth in vivo. Mechanistically, MeRIP-qPCR, RIP-qPCR, dual-luciferase reporter assay, and actinomycin D treatment revealed that IGF2BP1 targeted the 3'UTR of the C-MYC transcript for m6A modification and enhanced its stability. Furthermore, IGF2BP1 induced epithelial-mesenchymal transition (EMT) through the overexpression of C-MYC. In conclusion, these findings suggest that IGF2BP1-mediated m6A modification of C-MYC promotes LSCC progression via the EMT pathway, providing potential biomarkers and therapeutic targets for LSCC. - Source: PubMed
Publication date: 2026/05/07
Yang MingZhao XinWang MaomengZhang ZileSui JiaxinQin HanbinLiu XuexiaZhang Hua - RNF43 is frequently inactivated by mutations in pancreatic ductal adenocarcinoma (PDAC), but the molecular mechanisms and therapeutic vulnerabilities associated with RNF43 loss remain poorly defined. Here, we demonstrate that RNF43 functions as an E3 ubiquitin ligase targeting YBX1 for degradation, thereby suppressing mitochondrial oxidative phosphorylation (OXPHOS). In RNF43-deficient PDAC models, stabilized YBX1 activates MYC through dual mechanisms-enhancing MYC mRNA stability via IGF2BP1 and physically interacting with c-Myc protein-leading to transcriptional upregulation of IDH2 and IDH3A and subsequent OXPHOS activation. Importantly, RNF43 loss conferred sensitivity to OXPHOS inhibition both in vitro and in vivo. Treatment with the OXPHOS inhibitor IACS-010759 suppressed the proliferation, migration, invasion, and metastasis of RNF43-mutant tumors. Our findings identify a RNF43-YBX1-MYC signaling axis associated with metabolic reprogramming in pancreatic cancer and suggest that OXPHOS inhibition may represent a potential therapeutic vulnerability in tumors with RNF43-inactivating mutations. - Source: PubMed
Publication date: 2026/05/05
Qin GengduPan PenglinQin YangWei RuozhengZhao YuhanFu QixunYu HaixinLiu JiayingWu HeshuiLiu ZhiqiangZhou Yingke - Prostate cancer (PC) is one of the most common malignancies in men, and the emergence of androgen receptor-low/negative castration-resistant PC (ARL/- CRPC) following androgen receptor signaling inhibitor (ARSI) therapy remains a critical clinical challenge. The RNA-binding protein DEAD-box helicase 3 X-linked (DDX3X) has been implicated in the translational regulation of androgen receptor (AR) mRNA; however, the underlying binding mechanisms are not well defined. Here, we show that DDX3X colocalizes with AR mRNA in ARL/- CRPC cells and selectively recognizes non-canonical RNA G-quadruplex (rG4) motifs within the sequence of AR mRNA. RNA immunoprecipitation sequencing (RIP-seq) revealed enrichment of DDX3X-AR mRNA interactions in ARL/- CRPC cells. Fluorescence imaging confirmed the colocalization of DDX3X and AR mRNA within cytoplasmic granules, and biochemical assays confirmed the ability of selected AR mRNA fragments to form rG4 structures bound by DDX3X. Proteomic profiling of DDX3X-Ras GTPase-activating protein-binding protein 1 (G3BP1) complexes identified several RNA-binding proteins, including IGF2BP1, PUM2, and UBAP2, which may act as candidate cofactors. Together, these findings shed light on the interaction between AR mRNA and DDX3X and identify putative protein partners, offering insights into future therapeutic strategies. - Source: PubMed
Publication date: 2026/05/04
Zhang HanLiu Teresa TWu FeixuanColah Avan NRicke Emily ALi LingjunPutnam Andrea ARicke William A - RNA-binding proteins (RBPs) are critical regulators of mRNAs controlling all processes such as RNA transcription, transport, localization, translation, mRNA:ncRNA interactions, and decay. Cellular differentiation is driven by temporally and spatially regulated expression of proteins needed for the optimal function of individual cells, tissues and organs. Lens fiber cell differentiation is marked by high levels of expression of crystallin genes encoding critical proteins for lens transparency and light refraction. Herein we performed proteomic and transcriptomic analyses of RBPs in differentiating mouse lenses to identify the most abundant RBPs and establish dynamic changes of their expression in differentiating lenses. Expression analyses showed highly abundant RBPs, including Carhsp1, Igf2bp1/ZBP1, Ybx1, Pabpc1, Ddx39, and Rbm38. Binding sites of Carhsp1, the most abundant lens RBP, were predicted in various crystallin and β-actin mRNAs. Immunoprecipitations using Carhsp1-specific antibodies confirmed interactions of Carhsp1 with crystallin mRNAs in newborn lens. A combination of single molecule RNA FISH (smFISH) and immunofluorescence was used to probe in vivo interactions of Carhsp1 with αA-, αB-crystallin, and β-actin mRNAs in cytoplasm and nucleoplasm of cultured mouse lens epithelial cells. These experiments favor a working model of direct association of Carhsp1 mediated by multiple candidate binding sites within both αA-, αB-crystallin mRNAs. Together, these results open new avenues to perform comprehensive genetic, cell, and molecular biology studies of individual RBPs in the lens. - Source: PubMed
Publication date: 2026/04/28
Rayêe DanielleHwang Dong-WooChang William KKarp Ilana NCoomson Sarah YZhao YilinBowman TeresaLachke Salil ASinger Robert HEliscovich CarolinaCvekl Ales