Ask about this productRelated genes to: IGF2BP1 Blocking Peptide
- 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 Blocking Peptide
Related articles to: IGF2BP1 Blocking Peptide
- Protein arginine methyltransferase 3 (PRMT3) is a type I arginine methyltransferase that catalyzes asymmetric dimethylation of arginine residues on diverse substrate proteins. Initially characterized as a regulator of ribosomal protein methylation, PRMT3 has more recently been implicated in several cancer-related processes. Accumulating evidence suggests that PRMT3 is dysregulated in a variety of malignancies, including hepatocellular carcinoma, colorectal cancer, glioblastoma, breast cancer, pancreatic cancer, and non-small cell lung cancer. Through arginine methylation of selected regulatory proteins, PRMT3 has been linked to signaling pathways associated with tumor progression, metabolic adaptation, immune modulation, and therapeutic resistance. Mechanistically, available studies indicate that PRMT3 can regulate RNA-associated networks by methylating RNA-binding proteins and epitranscriptomic regulators such as IGF2BP1 and METTL14, thereby influencing mRNA stability and gene expression programs. In addition, PRMT3 has been reported to contribute to tumor metabolic reprogramming by promoting glycolytic activity and modulating amino acid metabolism through factors including HIF1A, PDHK1, and IDO1. These alterations may support tumor growth and, in some contexts, influence the tumor immune microenvironment. PRMT3 has also been associated with immune evasion, for example through effects on PD-L1 expression and innate immune signaling pathways such as cGAS-STING. Moreover, emerging evidence links PRMT3 to therapeutic resistance through mechanisms involving oncogenic transcript stabilization, immunometabolic remodeling, and drug efflux regulation. In this review, we summarize the current understanding of PRMT3 structure, catalytic mechanisms, and biological functions in cancer. We further discuss its emerging roles in metabolic regulation, immune suppression, and therapy resistance, while distinguishing mechanisms directly supported within specific cancer contexts from broader conceptual models inferred across studies. Overall, current evidence supports PRMT3 as an emerging and context-dependent regulator of tumor biology and a potential target for anticancer therapy. - Source: PubMed
Publication date: 2026/05/01
Jin HuiHuang HuaPan Xin - The insulin-like growth factor 2 mRNA-binding proteins (IGF2BP1-3) are oncofetal RNA regulators that control translation, stability, and localization of several transcripts, yet display paralog-specific functions despite high structural similarity. Each paralog contains six RNA-binding domains (two RRMs and four KH domains) linked by intrinsically disordered segments. mTORC2 phosphorylates IGF2BP1 and IGF2BP3 at a single conserved serine within the disordered linker between the RRM2 and KH1 domains, a modification required for proper regulation of mRNA translational fate. Pairing site-specific phosphoserine incorporation with structural and biophysical interrogations, we show that this phosphorylation acts as a configurational switch that reorganizes long-range arrangements of RNA-binding domains and linkers without altering the secondary structure, and with only modest effects on RNA-binding affinity. Critically, pSer-driven rearrangements occur both in the RNA-free state and upon RNA engagement, and the resulting architectures differ markedly between IGF2BP1 and IGF2BP3 despite >70% sequence identity. These paralog-specific, phosphorylation-dependent configurational landscapes likely underlie differences in mRNA recognition modes and functional outcomes. Our work identifies a post-translational mechanism that tunes IGF2BP paralog dynamics across free and RNA-bound states to program target mRNA selection, processing, and translational fate. - Source: PubMed
Publication date: 2026/05/08
Kaushik VikasSanjayan VaishnaviMattice JennaTokmina-Lukaszewska MonikaTörner RicardaChadda RahulKashyap RajnandaniVayyeti AbhinavRoy PralambikaMehl Ryan ACooley Richard BSigurdsson Snorri ThDastvan RezaArthanari HaribabuBothner Brian BOriganti SofiaAntony Edwin - Cardiac ischemia-reperfusion (I/R) injury is a major contributor to morbidity following myocardial infarction. While PDE4D has been implicated in cerebral I/R injury, its role and regulatory mechanisms in the cardiac context remain unclear. - Source: PubMed
Publication date: 2026/04/06
Li BeibeiLiu Hui - Irritable bowel syndrome (IBS) increases the risk of depression and damages the body, but there is no ideal treatment. However, aberrant expression of miRNAs in gastrointestinal diseases holds promise for the treatment of IBS. The aim of this study was to investigate how miR-149-5p regulates IBS by affecting the function of colonic mucosal epithelial cells. - Source: PubMed
He XiaotongChen GuoyuFeng LingmeiJi Jieru - 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