Fig. 1

The KH domains of IGF2BP1 recognize and bind m⁶A-mRNAs, as well as the potential fate selection of IGF2BP1-targeted mRNAs. a Domain structure of human IGF2BP1. RNA-binding domains include two RNA recognition motifs (RRMs, blue) and four hnRNP-K homology domains (KH, red) [5]. b Schematic structures showing that mRNAs are methylated at the 3′-UTR by methyltransferase complex then recognized by IGF2BP1 under the co-effects of stabilizers such as ELAVL1, which finally inhibits the decay of m⁶A-RNAs [10]. c YT521-B homology (YTH) domain-containing proteins (YTHDFs) compete for the same m⁶A sites with IGF2BP1 and promote decay of m⁶A-RNAs. d The β-catenin physically binds to the element (CTTTG-TC) located in the promoter of IGF2BP1, which contributes to IGF2BP1 transcription activity (left) [12,13,14,15]. The hypermethylation of element (CTTTG-TC) blocks β-catenin binding to the region and thus suppresses IGF2BP1 transcription activity (right), leading to increased proliferation and migration of metastatic breast cancer cells [54, 103]