IGF2BP1 is an RNA-binding protein that functions as an m6A reader, recognizing N6-methyladenosine-modified transcripts through a conserved GG(m6A)C consensus sequence 1. Unlike YTH domain proteins that promote mRNA decay, IGF2BP1 enhances mRNA stability and translation of target transcripts including MYC, IGF2, CD44, and PTEN 1. It recruits target mRNAs into cytoplasmic ribonucleoprotein complexes that facilitate mRNA transport, localized translation, and protection from endonuclease and microRNA-mediated degradation. During cellular stress, IGF2BP1 stabilizes stress granule-localized mRNAs, supporting cell survival and metabolism. Mechanistically, IGF2BP1 recognizes m6A modifications via its K homology domains and recruits PABPC1 to prevent mRNA deadenylation 2. IGF2BP1 overexpression correlates strongly with cancer progression and metastasis. In breast cancer, USP10-mediated stabilization of IGF2BP1 promotes metastasis through CPT1A mRNA recognition and stabilization 3. In colorectal cancer, METTL16-deposited m6A on SOGA1 mRNA enables IGF2BP1 recognition, enhancing glycolytic reprogramming 4. In hepatocellular carcinoma, PRMT3-mediated arginine methylation of IGF2BP1 promotes oxaliplatin resistance via HEG1 stabilization 5. These findings position IGF2BP1 as a critical m6A reader driving cancer progression and a potential therapeutic target.