{"gene":"IGF2BP1","run_date":"2026-06-10T01:55:22","timeline":{"discoveries":[{"year":2012,"finding":"IGF2BP1 promotes tumor cell migration velocity by inhibiting translation of MAPK4 mRNA, which prevents MK5 activation and HSP27 phosphorylation, thereby reducing G-actin sequestration and increasing F-actin polymerization. Simultaneously, IGF2BP1 stabilizes PTEN mRNA, enhancing PTEN expression and antagonizing PIP3 signaling to enforce RAC1-dependent cell polarization and directionality.","method":"RNA binding assays, knockdown/overexpression in tumor cell lines, cell migration assays, epistasis with MK5, RAC1, and HSP27","journal":"Genes & development","confidence":"High","confidence_rationale":"Tier 2 / Strong — multiple orthogonal methods (mRNA translation assays, protein phosphorylation, actin dynamics, directional migration) with defined pathway placement and mechanistic cascade","pmids":["22279049"],"is_preprint":false},{"year":2019,"finding":"IGF2BP1 promotes SRF expression by impairing miRNA-directed decay of SRF mRNA in an m6A-dependent manner. IGF2BP1 associates with target mRNAs in RISC-free complexes and its deletion enhances mRNA association with AGO2, indicating IGF2BP1 antagonizes miRNA-mediated mRNA degradation by competing with RISC.","method":"Gene expression analysis, AGO2-RIP, miRNA depletion experiments, m6A-dependent assays, knockdown/overexpression in cancer cell lines and nude mouse xenografts","journal":"Nucleic acids research","confidence":"High","confidence_rationale":"Tier 2 / Strong — multiple orthogonal methods (AGO2-RIP, miRNA depletion, m6A dependence, in vivo xenograft), replicated across multiple target mRNAs and cell lines","pmids":["30371874","29660014"],"is_preprint":false},{"year":2020,"finding":"The oncopeptide RBRP (encoded by LINC00266-1) directly binds IGF2BP1 and strengthens its m6A recognition on target RNAs such as c-Myc mRNA, increasing mRNA stability and c-Myc expression to promote tumorigenesis.","method":"Co-immunoprecipitation, RNA pulldown, m6A recognition assays, mRNA stability assays, overexpression/knockdown in cancer cells","journal":"Nature communications","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — reciprocal Co-IP and functional rescue experiments in single lab, mechanistically novel regulatory subunit concept","pmids":["32245947"],"is_preprint":false},{"year":2021,"finding":"IGF2BP1 recognizes m6A sites in the 3'UTR of PEG10 mRNA and recruits PABPC1 to enhance PEG10 mRNA stability, increasing PEG10 protein expression in endometrial cancer cells.","method":"RIP-seq, MeRIP-seq, RNA-seq, Co-immunoprecipitation and mass spectrometry to identify PABPC1 as interacting partner, mRNA stability assays","journal":"Theranostics","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — RIP-seq and MeRIP-seq combined with Co-IP/MS in single lab; identification of PABPC1 as recruitment partner is mechanistically novel","pmids":["33391523"],"is_preprint":false},{"year":2022,"finding":"A small molecule cucurbitacin B (CuB) directly targets IGF2BP1 at Cys253 in the KH1-2 domains, causing an allosteric effect that blocks IGF2BP1 recognition of m6A mRNA targets such as c-MYC.","method":"Chemical genetics, direct binding assays (Cys253 targeting), KH domain mutagenesis, m6A RNA binding assays, in vivo xenograft models","journal":"ACS central science","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — direct binding to defined residue with functional validation, single lab but multiple orthogonal methods","pmids":["36032766"],"is_preprint":false},{"year":2023,"finding":"PRMT3 methylates IGF2BP1 at R452, which is critical for IGF2BP1 function in stabilizing the mRNA of HEG1. PRMT3-mediated arginine methylation of IGF2BP1 drives oxaliplatin resistance in hepatocellular carcinoma.","method":"CRISPR/Cas9 activation library screen, transcriptomic profiling, site-specific mutagenesis at R452, mRNA stability assays, in vitro and in vivo functional validation","journal":"Nature communications","confidence":"High","confidence_rationale":"Tier 1 / Strong — site-specific mutagenesis of modification site combined with functional rescue and in vivo validation; rigorous multi-method approach in single study","pmids":["37024475"],"is_preprint":false},{"year":2021,"finding":"FBXO45 E3 ubiquitin ligase promotes IGF2BP1 ubiquitination at Lys190 and Lys450, leading to IGF2BP1 activation and subsequent upregulation of PLK1 expression, driving cell proliferation and liver tumorigenesis.","method":"Co-immunoprecipitation, ubiquitination assays, site-specific mutagenesis (Lys190/Lys450), IGF2BP1 knockdown rescue experiments, transgenic mouse models","journal":"eLife","confidence":"High","confidence_rationale":"Tier 1 / Strong — site-specific ubiquitination mutagenesis with functional validation in vitro and in transgenic mice; multiple orthogonal methods","pmids":["34779401"],"is_preprint":false},{"year":2023,"finding":"TRIM29 E3 ubiquitin ligase interacts with IGF2BP1 and induces K48-linked ubiquitination at Lys440 and Lys450, leading to IGF2BP1 protein degradation. IGF2BP1 promotes PD-L1 mRNA stability in a 3'UTR and m6A-dependent manner, and TRIM29-mediated degradation of IGF2BP1 reduces PD-L1 expression to enhance antitumor T-cell immunity.","method":"Proteomics, co-immunoprecipitation, site-specific ubiquitination assays (K48-linked), mRNA stability assays, in vivo tumor models","journal":"Cancer letters","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — reciprocal Co-IP with proteomics identification, site-specific ubiquitination characterization, single lab","pmids":["38029830"],"is_preprint":false},{"year":2023,"finding":"USP10 deubiquitinase directly binds, deubiquitinates, and stabilizes IGF2BP1 protein. IGF2BP1 in turn recognizes m6A sites on CPT1A mRNA to enhance its stability, mediating breast cancer metastasis.","method":"Co-immunoprecipitation, deubiquitination assays, MeRIP-seq, mRNA stability assays, in vitro and in vivo metastasis models","journal":"International journal of biological sciences","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — reciprocal Co-IP with functional deubiquitination assay and MeRIP-seq validation, single lab","pmids":["36632454"],"is_preprint":false},{"year":2021,"finding":"A small molecule inhibitor binds to a hydrophobic surface at the boundary of IGF2BP1 KH3 and KH4 domains and inhibits KRAS RNA binding, reducing KRAS mRNA and protein levels and downstream oncogenic signaling.","method":"Small molecule screening, direct binding assays to KH3/KH4 domain interface, RNA binding competition assays, wound healing and soft agar growth assays","journal":"RNA biology","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — direct binding to defined domain with functional RNA-binding competition assays, single lab","pmids":["34895045"],"is_preprint":false},{"year":2014,"finding":"IGF2BP1 drives translation of cIAP1 mRNA in rhabdomyosarcoma cells, protecting them from TNF-α-mediated apoptosis. IGF2BP1 knockdown reduces cIAP1 levels and sensitizes cells to cell death.","method":"IGF2BP1 knockdown, cIAP1 protein and mRNA quantification, TNF-α-mediated apoptosis assays, in vivo tumor growth experiments with IAP antagonists","journal":"Oncogene","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — knockdown with defined translational target and functional apoptosis readout, in vivo validation","pmids":["24704827"],"is_preprint":false},{"year":2017,"finding":"IGF2BP1 overexpression in human adult erythroblasts causes fetal-like hemoglobin expression by reprogramming at the transcriptional level; mechanistically, IGF2BP1 reduces BCL11A protein expression via posttranscriptional mechanisms (mRNA stability and polysome analysis) to increase fetal hemoglobin.","method":"Erythroid-specific IGF2BP1 overexpression, hemoglobin quantification by HPLC, mRNA stability and polysome sedimentation assays for BCL11A","journal":"Proceedings of the National Academy of Sciences of the United States of America","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — multiple orthogonal methods (polysome profiling, mRNA stability, HPLC hemoglobin quantification) in primary human cells, single lab","pmids":["28652347"],"is_preprint":false},{"year":2019,"finding":"IGF2BP1 controls the cargo of melanoma-derived extracellular vesicles (EVs) to promote metastasis. IGF2BP1 knockdown did not alter EV size, number, or protein/RNA concentration, but altered EV mRNA, protein, and miRNA cargo, blocking pre-metastatic niche formation by inhibiting fibronectin deposition and CD45+ cell accumulation in lungs.","method":"In vivo metastasis models (two models), EV isolation and characterization, RNA-sequencing and proteomics of EVs, IGF2BP1 knockdown/overexpression","journal":"Oncogene","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — two in vivo models with EV proteomics/transcriptomics, single lab","pmids":["30936459"],"is_preprint":false},{"year":2020,"finding":"IGF2BP1 maintains intestinal barrier function by directly binding occludin (Ocln) mRNA and stabilizing it, increasing occludin protein expression. Conditional knockout of IGF2BP1 in intestinal epithelial cells causes impaired tight junction function and colitis; ectopic occludin expression rescues barrier function in IGF2BP1-knockdown cells.","method":"Conditional knockout mouse (Villin CreERT2:Igf2bp1flox/flox), gut barrier assays, RIP demonstrating direct Ocln mRNA binding, mRNA stability assays, occludin rescue experiments","journal":"The Journal of biological chemistry","confidence":"High","confidence_rationale":"Tier 2 / Strong — in vivo conditional KO with specific phenotype, direct RIP, mRNA stability, and rescue experiment; multiple orthogonal methods","pmids":["32385106"],"is_preprint":false},{"year":2019,"finding":"IGF2BP1 directly binds and stabilizes ETV6/RUNX1 fusion mRNA in t(12;21)-positive acute lymphoblastic leukemia, as shown by RIP enrichment and the reduction of ETV6/RUNX1 mRNA upon IGF2BP1 knockdown.","method":"RNA immunoprecipitation (RIP), IGF2BP1 knockdown, quantification of ETV6/RUNX1 mRNA in cell lines and primary patient samples","journal":"Blood cells, molecules & diseases","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — RIP with functional knockdown validation in cell lines and primary samples, single lab","pmids":["26852652"],"is_preprint":false},{"year":2019,"finding":"IGF2BP1 maintains leukemia stem cell properties by stabilizing HOXB4, MYB, and ALDH1A1 mRNAs, as demonstrated by CLIP and PAR-CLIP techniques. Chemical or genetic inhibition of IGF2BP1 decreases tumorigenicity, promotes differentiation, and sensitizes leukemia cells to chemotherapy.","method":"CLIP, PAR-CLIP, gain- and loss-of-function systems, tumor-initiating potential assays","journal":"Leukemia","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — CLIP/PAR-CLIP with functional validation, single lab","pmids":["31768017"],"is_preprint":false},{"year":2020,"finding":"IGF2BP1 promotes SRC kinase activation through a protein-ligand-induced, RNA-independent mechanism, and separately enhances ERK2 expression in an RNA-binding-dependent manner, connecting SRC/MAPK signaling to promote invasive growth in ovarian cancer cells.","method":"Protein interaction studies, SRC kinase activation assays, RNA-binding-deficient mutants, 3D invasion cultures, intraperitoneal mouse models, SRC/MEK inhibitor rescue experiments","journal":"RNA biology","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — RNA-binding-deficient mutants distinguish RNA-independent SRC activation from RNA-dependent ERK2 regulation; in vivo validation, single lab","pmids":["32876513"],"is_preprint":false},{"year":2019,"finding":"IGF2BP1 binds Lnc-THOR RNA; disruption of Lnc-THOR–IGF2BP1 association (by triptonide or Lnc-THOR/IGF2BP1 CRISPR knockout) depletes IGF2BP1 mRNA targets (Myc, IGF2, Gli1) and inhibits NPC cell growth, establishing that Lnc-THOR stabilizes IGF2BP1-dependent target mRNAs.","method":"Small molecule disruption, CRISPR/Cas9 knockout of Lnc-THOR and IGF2BP1, target mRNA quantification, in vivo xenograft models","journal":"Cancer letters","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — genetic epistasis with dual CRISPR KO and functional rescue, single lab","pmids":["30503558"],"is_preprint":false},{"year":2021,"finding":"mTORC2 phosphorylates IGF2BP1 at Ser181; prevention of this phosphorylation enhances translation and destabilization of c-myc mRNA. Src kinase phosphorylates IGF2BP1 at Tyr396; prevention of Tyr396 phosphorylation causes accumulation of translationally silent IGF2BP1-sequestered mRNA in cytoplasmic granules.","method":"mTORC2 and Src kinase inhibition, phospho-site mutagenesis (Ser181, Tyr396), reporter assays with CRD sequence, polysome analysis, xenograft models","journal":"Cellular signalling","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — phospho-site mutagenesis with functional CRD reporter and xenograft validation, single lab","pmids":["33388443"],"is_preprint":false},{"year":2019,"finding":"IGF2BP1 directly binds MAP1LC3B, ATG3, and ATG5 transcripts (autophagy gene mRNAs), as demonstrated by in silico and biochemical analyses. Intestinal epithelial Imp1 deletion leads to upregulation of Atg5 and increased autophagy flux, and double knockout of Imp1 and Atg7 increases sensitivity to colonic injury, establishing a compensatory relationship between IMP1/IGF2BP1 and autophagy.","method":"Conditional knockout mice, RNA-IP, in silico binding analysis, DSS colitis models, autophagy flux assays, double-mutant epistasis","journal":"EMBO reports","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — direct RIP with genetic epistasis in double-mutant mice, single lab","pmids":["31061170"],"is_preprint":false},{"year":2022,"finding":"IGF2BP1 knockout mice display disorganized neocortical development with loss of cortical marginal cell density and fewer mitotically active cells. In IGF2BP1-null neurons, β-actin mRNA shows increased transcription rates and total protein content but decreased transport and anchoring, demonstrating IGF2BP1 is required for proper β-actin mRNA localization and transport in neurons.","method":"IGF2BP1 knockout mice, BrdU labeling, endogenously tagged β-actin-MS2 mRNA imaging, mRNA transport and anchoring measurements, transcription rate analysis","journal":"Proceedings of the National Academy of Sciences of the United States of America","confidence":"High","confidence_rationale":"Tier 2 / Strong — in vivo knockout with endogenous mRNA tagging and live imaging; multiple orthogonal methods for mRNA localization, transport, and protein quantification","pmids":["36067310"],"is_preprint":false},{"year":2015,"finding":"Igf2bp1 knockdown in zebrafish reduces retinal ganglion cell (RGC) axonal outgrowth and tectal coverage. RGC-specific expression of a phosphomimetic Igf2bp1 reduces axonal projection density without affecting RGC survival, demonstrating Igf2bp1 is required for axon outgrowth in vivo and that its phosphorylation state modulates this function.","method":"Morpholino knockdown and phosphomimetic rescue in zebrafish, timelapse imaging of RGC axon outgrowth, photoconvertible fluorescent protein reporter under β-actin 3'UTR","journal":"PloS one","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — in vivo knockdown with phosphomimetic rescue and live imaging, single lab","pmids":["26325373"],"is_preprint":false},{"year":2023,"finding":"RPS15 interacts with the KH domain of IGF2BP1, and this complex recognizes and directly binds the 3'UTR of MKK6 and MAPK14 mRNAs in an m6A-dependent manner to promote translation of core p38 MAPK pathway proteins and drive ESCC metastasis.","method":"CRISPR SAM library screen, Co-IP of RPS15-IGF2BP1, m6A-dependent RIP for MKK6/MAPK14 mRNAs, targeted drug screening, in vitro and in vivo functional assays","journal":"Signal transduction and targeted therapy","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — Co-IP with mechanistic m6A-RIP validation and in vivo studies, single lab","pmids":["37264021"],"is_preprint":false},{"year":2019,"finding":"IGF2BP1 promotes LPS-induced NFκB signaling in human macrophages and monocytes. Co-immunoprecipitation showed IGF2BP1 associates with the p65-p52 NFκB complex in nuclei of LPS-treated cells; IGF2BP1 knockdown/knockout inhibits p65-p52 nuclear translocation and NFκB transcriptional activation.","method":"Co-immunoprecipitation of IGF2BP1 with NFκB p65-p52, nuclear fractionation, shRNA knockdown and CRISPR/Cas9 KO, cytokine ELISA","journal":"Biochemical and biophysical research communications","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — Co-IP with nuclear complex and functional KO validation, single lab","pmids":["31000200"],"is_preprint":false},{"year":2022,"finding":"MNX1-AS1 lncRNA binds IGF2BP1 and drives its phase separation, which increases IGF2BP1 interaction with the 3'UTR of c-Myc and E2F1 mRNAs to promote their stability, creating a c-Myc/MNX1-AS1/IGF2BP1 positive feedback loop driving cell-cycle progression.","method":"RNA-protein binding assays, phase separation assays, 3'UTR interaction studies, cell cycle analysis, patient-derived xenograft model","journal":"Cancer research","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — phase separation and RNA-binding assays with functional rescue and PDX model, single lab","pmids":["36214649"],"is_preprint":false},{"year":2023,"finding":"MKRN3 interacts with IGF2BP1 (identified by proteomics), and IGF2BP1 in turn interacts with polyadenylate-binding protein family members, positioning IGF2BP1 as a target of MKRN3-mediated regulation of hypothalamic puberty-related gene expression.","method":"Proteomics interactome analysis, co-immunoprecipitation, Mkrn3 knockout mouse model","journal":"JCI insight","confidence":"Low","confidence_rationale":"Tier 3 / Weak — single Co-IP/proteomics identification without mechanistic follow-up for the IGF2BP1 interaction specifically","pmids":["37092553"],"is_preprint":false},{"year":2023,"finding":"IGF2BP1 directly binds and stabilizes INHBA mRNA; knockdown of IGF2BP1 reduces INHBA expression and attenuates Smad2/3 signaling to suppress ESCC cell invasion and migration. IGF2BP1 also interacts with G3BP1, and G3BP1 knockdown similarly downregulates INHBA-Smad2/3 signaling.","method":"RIP-seq, mass spectrometry for interacting proteins (identifying G3BP1), gene-specific m6A PCR, RNA stability assays, BTYNB inhibitor treatment","journal":"Experimental hematology & oncology","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — RIP-seq with MS-identified G3BP1 interaction and functional RNA stability validation, single lab","pmids":["37644505"],"is_preprint":false},{"year":2024,"finding":"ZDHHC1 palmitoylates IGF2BP1 at C337 (S-palmitoylation), which results in downregulated expression of LIPG mRNA via m6A modification, suppressing colorectal cancer cell growth.","method":"Palmitoylation assays, site-specific mutagenesis (C337), m6A modification analysis, mRNA stability assays, in vitro and in vivo functional studies","journal":"Cancer gene therapy","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — site-specific palmitoylation mutagenesis with functional m6A downstream readout, single lab","pmids":["39069526"],"is_preprint":false},{"year":2023,"finding":"IGF2BP1 directly binds and governs expression of SEMA3A and SHMT2 in neuroblastoma cells, modulating their protein levels in small extracellular vesicles (EVs) to regulate pro-metastatic microenvironment formation at potential metastatic organs.","method":"Unbiased proteomics of EVs, direct binding assays, knockdown/overexpression in immunocompetent mouse NB models, EV isolation and characterization","journal":"Oncogene","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — unbiased proteomics with functional validation in multiple immunocompetent models, single lab","pmids":["36973517"],"is_preprint":false},{"year":2017,"finding":"IGF2BP1 is identified as a novel binding partner of p38 MAPK by co-immunoprecipitation followed by mass spectrometry.","method":"Co-immunoprecipitation, mass spectrometry, in silico domain interaction analysis","journal":"Molecular and cellular biochemistry","confidence":"Low","confidence_rationale":"Tier 3 / Weak — single Co-IP/MS identification without functional follow-up on the interaction","pmids":["28497370"],"is_preprint":false},{"year":2023,"finding":"IGF2BP1 stabilizes c-MYC mRNA via m6A-dependent binding in gastric cancer cells, promoting aerobic glycolysis and cancer progression. However, a separate study in gastric cancer found IGF2BP1 promotes degradation and reduces translation efficiency of MYC mRNA in an m6A-dependent manner, suggesting a cell-context-dependent switch in IGF2BP1's regulation of MYC.","method":"RIP, MeRIP, mRNA stability assays, polysome profiling, gain/loss of function in gastric cancer cells","journal":"Experimental cell research / Cancer science","confidence":"Low","confidence_rationale":"Tier 3 / Weak — single-lab experiments with contradictory outcomes between two papers; mechanism direction uncertain","pmids":["35489385","38115228"],"is_preprint":false},{"year":2022,"finding":"IGF2BP1 stabilizes EZH2 mRNA in an m6A-dependent manner in neuroendocrine tumor cells, enhancing EZH2 protein levels which then trimethylates H3K27 to silence cell cycle arrest genes and drive proliferation.","method":"mRNA stability assays, m6A-dependent RIP, IGF2BP1 inhibitor (BTYNB), cell cycle analysis, H3K27me3 ChIP","journal":"Cancers","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — mRNA stability with m6A dependence, ChIP readout, and pharmacological inhibition, single lab","pmids":["35565249"],"is_preprint":false},{"year":2022,"finding":"Heat treatment promotes IGF2BP1 aggregation specifically in the presence of m6A-modified HPV E7 mRNA, forming heat-induced m6A E7 mRNA-IGF2BP1 granules that are resolved by the ubiquitin-proteasome system, downregulating E7 mRNA and protein.","method":"Heat treatment assays, m6A mutation experiments, granule imaging, proteasome inhibition assays, in vitro and in vivo HPV carcinogenesis models","journal":"Cell reports","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — m6A mutation and proteasome inhibition experiments with mechanistic granule imaging, single lab","pmids":["36288717"],"is_preprint":false},{"year":2024,"finding":"In zebrafish, Igf2bp1 acts as a reader of METTL16-mediated m6A modifications on mybl2b mRNA (cell-cycle transcription factor); Mettl16 deficiency destabilizes mybl2b mRNA due to lost Igf2bp1 binding, causing G1/S arrest in embryonic hematopoietic stem and progenitor cells. The METTL16-m6A-MYBL2-IGF2BP1 axis is conserved in humans.","method":"Single-cell RNA-seq cross-species, Mettl16-deficient zebrafish, methyltransferase-dead rescue, m6A-RIP for mybl2b, in vivo HSPC proliferation assays, human cell validation","journal":"The EMBO journal","confidence":"High","confidence_rationale":"Tier 2 / Strong — in vivo zebrafish model with methyltransferase-dead rescue, direct m6A-RIP, cross-species conservation validation; multiple orthogonal methods","pmids":["38605226"],"is_preprint":false},{"year":2023,"finding":"IGF2BP1 synergizes with ETV6-RUNX1 fusion protein in B-ALL by binding and stabilizing the ETV6::RUNX1 fusion transcript, creating a positive feedback loop that constitutively dysregulates TNFα/NFκB and PI3K-Akt oncogenic pathways; co-expression in mouse bone marrow causes pre-leukemic hypercellularity and splenomegaly.","method":"RIP-seq after IGF2BP1 pulldown, RNA-seq after IGF2BP1 KO, bone marrow transplant mouse model with retroviral co-expression, patient sample validation","journal":"Journal of experimental & clinical cancer research","confidence":"High","confidence_rationale":"Tier 2 / Strong — RIP-seq and RNA-seq integration, in vivo pre-leukemic model, patient sample correlation; multiple orthogonal methods","pmids":["37670323"],"is_preprint":false}],"current_model":"IGF2BP1 is an oncofetal RNA-binding protein that primarily stabilizes target mRNAs (including KRAS, c-MYC, PTEN, ACTB, cIAP1, PD-L1, and many others) in an m6A-dependent manner by competing with RISC/miRNA-mediated decay and recruiting co-factors such as PABPC1; its activity is regulated by post-translational modifications including PRMT3-mediated arginine methylation at R452, mTORC2-mediated Ser181 phosphorylation, Src-mediated Tyr396 phosphorylation, and ubiquitination at Lys190/Lys450/Lys440 by E3 ligases FBXO45 and TRIM29 (counteracted by USP10 deubiquitination), and palmitoylation at C337 by ZDHHC1; structurally, its KH3-4 domain interface mediates RNA binding and is the target of small molecule inhibitors; in neurons and developing tissues IGF2BP1 localizes mRNA (particularly β-actin mRNA) to regulate local translation and axon outgrowth, while in cancer cells it promotes migration, invasion, immune evasion, and stem cell properties through these post-transcriptional regulatory mechanisms."},"narrative":{"mechanistic_narrative":"IGF2BP1 is an oncofetal m6A-reader RNA-binding protein that post-transcriptionally controls the fate of target mRNAs to govern cell migration, proliferation, stemness, and tissue development [PMID:30371874, PMID:29660014, PMID:36067310]. Its dominant mechanism is m6A-dependent recognition of target transcripts, where binding stabilizes mRNAs by antagonizing miRNA/RISC-directed decay; IGF2BP1 associates with target mRNAs in RISC-free complexes, and its loss enhances AGO2 association and degradation of targets such as SRF [PMID:30371874, PMID:29660014]. Stabilization is reinforced by recruitment of co-factors including PABPC1 to m6A 3'UTR sites [PMID:33391523], and it acts on an extensive target set spanning oncogenic and barrier programs — PTEN and MAPK4 to enforce directional migration via actin dynamics [PMID:22279049], cIAP1 to suppress apoptosis [PMID:24704827], PD-L1 to drive immune evasion [PMID:38029830], EZH2 to silence cell-cycle genes [PMID:35565249], and occludin to maintain intestinal tight junctions [PMID:32385106]. In neurons IGF2BP1 localizes β-actin mRNA for transport and anchoring to support cortical development and axon outgrowth [PMID:36067310, PMID:26325373]. Its activity and abundance are tuned by a network of post-translational modifications: PRMT3-mediated arginine methylation at R452 [PMID:37024475], mTORC2 Ser181 and Src Tyr396 phosphorylation [PMID:33388443], ZDHHC1 palmitoylation at C337 [PMID:39069526], and competing ubiquitination by FBXO45 (K190/K450, activating) and TRIM29 (K48-linked K440/K450, degrading) opposed by USP10 deubiquitination [PMID:34779401, PMID:38029830, PMID:36632454]. The protein is functionally co-opted by regulatory lncRNAs and oncopeptides (RBRP, Lnc-THOR, MNX1-AS1) that enhance its m6A recognition or drive its phase separation [PMID:32245947, PMID:30503558, PMID:36214649], and its RNA-binding KH3-4 interface and KH1-2 Cys253 are targetable by small molecules that block recognition of KRAS and c-MYC mRNAs [PMID:36032766, PMID:34895045].","teleology":[{"year":2012,"claim":"Established that IGF2BP1 directs cell migration through dual post-transcriptional control of cytoskeletal signaling, defining a concrete mechanistic cascade rather than a generic RNA-binding role.","evidence":"RNA binding, knockdown/overexpression, migration assays, and epistasis with MK5/RAC1/HSP27 in tumor cell lines","pmids":["22279049"],"confidence":"High","gaps":["Did not address m6A dependence of these specific targets","Did not establish in vivo relevance"]},{"year":2014,"claim":"Showed IGF2BP1 enforces apoptosis resistance by driving cIAP1 translation, linking its activity to tumor cell survival under death-receptor stress.","evidence":"Knockdown, cIAP1 protein/mRNA quantification, TNF-α apoptosis assays, in vivo tumor growth with IAP antagonists","pmids":["24704827"],"confidence":"Medium","gaps":["Mechanism of translational enhancement not resolved","m6A involvement not tested"]},{"year":2017,"claim":"Demonstrated IGF2BP1 can reprogram differentiated cells toward a fetal state by post-transcriptionally repressing BCL11A, extending its oncofetal role to erythroid identity.","evidence":"Erythroid-specific overexpression, HPLC hemoglobin quantification, polysome and mRNA stability assays in primary human erythroblasts","pmids":["28652347"],"confidence":"Medium","gaps":["Direct binding to BCL11A mRNA not fully resolved","m6A dependence not addressed"]},{"year":2019,"claim":"Defined the core decay-protection mechanism: IGF2BP1 shields m6A-marked target mRNAs by sequestering them away from AGO2/RISC, resolving how stabilization is achieved.","evidence":"AGO2-RIP, miRNA depletion, m6A-dependent assays, xenografts across multiple targets","pmids":["30371874","29660014"],"confidence":"High","gaps":["Structural basis of RISC competition not defined","Generality across all targets not established"]},{"year":2019,"claim":"Expanded the target repertoire to stem cell, fusion-oncogene, autophagy, and inflammatory programs, showing IGF2BP1 sustains leukemia stemness, stabilizes ETV6/RUNX1 transcripts, buffers autophagy genes, and supports NF-κB signaling.","evidence":"CLIP/PAR-CLIP, RIP, conditional knockout mice, double-mutant epistasis, and Co-IP across leukemia, intestinal, and macrophage systems","pmids":["31768017","26852652","31061170","31000200"],"confidence":"Medium","gaps":["NF-κB association mechanism not resolved (RNA-dependent vs independent)","Autophagy gene binding mostly in silico/RIP without rescue for all targets"]},{"year":2020,"claim":"Revealed that an oncopeptide (RBRP) and a co-factor recruitment step (PABPC1) act as accessory modules strengthening IGF2BP1 m6A recognition and stabilization, and that IGF2BP1 has an RNA-independent function in activating SRC kinase.","evidence":"Co-IP, RNA pulldown, m6A recognition assays, RIP-seq/MeRIP-seq, RNA-binding-deficient mutants, in vivo models","pmids":["32245947","33391523","32876513"],"confidence":"Medium","gaps":["RNA-independent SRC activation mechanism not structurally defined","Stoichiometry and generality of PABPC1 recruitment unknown"]},{"year":2021,"claim":"Showed IGF2BP1 abundance and activity are governed by ubiquitination and phosphorylation, defining FBXO45-driven activating ubiquitination and mTORC2/Src phospho-control of its translational repression function.","evidence":"Site-specific ubiquitination/phospho mutagenesis (K190/K450, Ser181, Tyr396), polysome analysis, transgenic and xenograft models","pmids":["34779401","33388443"],"confidence":"High","gaps":["How non-degradative ubiquitination activates IGF2BP1 mechanistically unclear","Crosstalk between phospho- and ubiquitin marks not addressed"]},{"year":2021,"claim":"Established the RNA-binding KH domains as druggable: small molecules at the KH3-4 interface and KH1-2 Cys253 block target recognition, validating IGF2BP1 as a therapeutic target.","evidence":"Small molecule screening, direct binding to defined residues/domains, RNA-binding competition, in vivo xenografts (CuB reported 2022)","pmids":["34895045","36032766"],"confidence":"Medium","gaps":["No co-crystal structure of inhibitor-bound complex reported","Selectivity over paralogs not established"]},{"year":2022,"claim":"Demonstrated IGF2BP1 function is shaped by phase separation and granule dynamics, with lncRNAs driving condensate formation that enhances target binding and stress/heat promoting m6A-dependent aggregation routed to proteasomal clearance.","evidence":"Phase separation assays, RNA-binding, granule imaging, m6A mutation, proteasome inhibition, PDX and HPV carcinogenesis models","pmids":["36214649","36288717"],"confidence":"Medium","gaps":["Determinants of condensate composition not defined","Relationship between activating condensates and degradative granules unclear"]},{"year":2022,"claim":"Confirmed an in vivo developmental requirement: IGF2BP1 is needed for β-actin mRNA transport/anchoring and proper neocortical organization, anchoring its localization function in neurons genetically.","evidence":"IGF2BP1 knockout mice, endogenous β-actin-MS2 imaging, transport/anchoring and transcription-rate measurements","pmids":["36067310"],"confidence":"High","gaps":["Molecular machinery of mRNA transport not fully resolved","Link to specific neuronal m6A marks not addressed"]},{"year":2023,"claim":"Broadened the regulatory and partner landscape: PRMT3 methylation (R452), TRIM29/USP10 ubiquitin balance, and partners RPS15, G3BP1, and the ETV6-RUNX1 fusion couple IGF2BP1 to drug resistance, immune evasion, metastasis, and leukemogenesis.","evidence":"CRISPR activation screens, site-specific mutagenesis, Co-IP/MS, m6A-RIP, RIP-seq/RNA-seq, in vivo tumor and pre-leukemic models","pmids":["37024475","38029830","36632454","37264021","37644505","37670323"],"confidence":"High","gaps":["How distinct PTMs are integrated on a single IGF2BP1 molecule unknown","Whether RPS15/G3BP1 partnerships are constitutive or context-specific unresolved"]},{"year":2024,"claim":"Placed IGF2BP1 within a defined writer-reader axis and added palmitoylation as a control layer, showing it reads METTL16-deposited m6A on MYBL2 to drive HSPC cell-cycle progression and that ZDHHC1 palmitoylation tunes its output.","evidence":"Mettl16-deficient zebrafish with methyltransferase-dead rescue, cross-species m6A-RIP, palmitoylation site mutagenesis (C337), functional assays","pmids":["38605226","39069526"],"confidence":"High","gaps":["Whether other writers feed IGF2BP1 in different tissues unknown","How palmitoylation alters IGF2BP1 localization/RNA selectivity not resolved"]},{"year":null,"claim":"How IGF2BP1 selects between stabilizing versus destabilizing/translation-repressing fates for the same target (e.g. MYC) across cellular contexts remains unresolved.","evidence":"","pmids":[],"confidence":"Low","gaps":["Contradictory MYC outcomes reported in gastric cancer","No unifying rule linking PTM/condensate state to target fate","Context-dependent co-factor combinations not mapped"]}],"mechanism_profile":{"molecular_activity":[{"term_id":"GO:0003723","term_label":"RNA binding","supporting_discovery_ids":[0,1,3,9,13,15,20,26,33]},{"term_id":"GO:0140098","term_label":"catalytic activity, acting on RNA","supporting_discovery_ids":[1,3,33]},{"term_id":"GO:0140110","term_label":"transcription regulator activity","supporting_discovery_ids":[1,31]},{"term_id":"GO:0045182","term_label":"translation regulator activity","supporting_discovery_ids":[0,10,18,22]},{"term_id":"GO:0140313","term_label":"molecular sequestering activity","supporting_discovery_ids":[18,32]}],"localization":[{"term_id":"GO:0005829","term_label":"cytosol","supporting_discovery_ids":[18,20,32]},{"term_id":"GO:0005634","term_label":"nucleus","supporting_discovery_ids":[23]}],"pathway":[{"term_id":"R-HSA-8953854","term_label":"Metabolism of RNA","supporting_discovery_ids":[1,3,33]},{"term_id":"R-HSA-1643685","term_label":"Disease","supporting_discovery_ids":[5,7,34]},{"term_id":"R-HSA-162582","term_label":"Signal Transduction","supporting_discovery_ids":[0,16,22,26]},{"term_id":"R-HSA-168256","term_label":"Immune System","supporting_discovery_ids":[7,23]},{"term_id":"R-HSA-392499","term_label":"Metabolism of proteins","supporting_discovery_ids":[5,6,7,8,27]}],"complexes":[],"partners":["PABPC1","RPS15","G3BP1","FBXO45","TRIM29","USP10","PRMT3","ZDHHC1"],"other_free_text":[]}},"prefetch_data":{"uniprot":{"accession":"Q9NZI8","full_name":"Insulin-like growth factor 2 mRNA-binding protein 1","aliases":["Coding region determinant-binding protein","CRD-BP","IGF-II mRNA-binding protein 1","VICKZ family member 1","Zipcode-binding protein 1","ZBP-1"],"length_aa":577,"mass_kda":63.5,"function":"RNA-binding factor that recruits target transcripts to cytoplasmic protein-RNA complexes (mRNPs). This transcript 'caging' into mRNPs allows mRNA transport and transient storage. It also modulates the rate and location at which target transcripts encounter the translational apparatus and shields them from endonuclease attacks or microRNA-mediated degradation. Preferentially binds to N6-methyladenosine (m6A)-containing mRNAs and increases their stability (PubMed:29476152, PubMed:32245947). Plays a direct role in the transport and translation of transcripts required for axonal regeneration in adult sensory neurons (By similarity). Regulates localized beta-actin/ACTB mRNA translation, a crucial process for cell polarity, cell migration and neurite outgrowth. Co-transcriptionally associates with the ACTB mRNA in the nucleus. This binding involves a conserved 54-nucleotide element in the ACTB mRNA 3'-UTR, known as the 'zipcode'. The RNP thus formed is exported to the cytoplasm, binds to a motor protein and is transported along the cytoskeleton to the cell periphery. During transport, prevents ACTB mRNA from being translated into protein. When the RNP complex reaches its destination near the plasma membrane, IGF2BP1 is phosphorylated. This releases the mRNA, allowing ribosomal 40S and 60S subunits to assemble and initiate ACTB protein synthesis. Monomeric ACTB then assembles into the subcortical actin cytoskeleton (By similarity). During neuronal development, key regulator of neurite outgrowth, growth cone guidance and neuronal cell migration, presumably through the spatiotemporal fine tuning of protein synthesis, such as that of ACTB (By similarity). May regulate mRNA transport to activated synapses (By similarity). Binds to and stabilizes ABCB1/MDR-1 mRNA (By similarity). During interstinal wound repair, interacts with and stabilizes PTGS2 transcript. PTGS2 mRNA stabilization may be crucial for colonic mucosal wound healing (By similarity). Binds to the 3'-UTR of IGF2 mRNA by a mechanism of cooperative and sequential dimerization and regulates IGF2 mRNA subcellular localization and translation. Binds to MYC mRNA, in the coding region instability determinant (CRD) of the open reading frame (ORF), hence preventing MYC cleavage by endonucleases and possibly microRNA targeting to MYC-CRD (PubMed:29476152). Binding to MYC mRNA is enhanced by m6A-modification of the CRD (PubMed:29476152). Binds to the 3'-UTR of CD44 mRNA and stabilizes it, hence promotes cell adhesion and invadopodia formation in cancer cells. Binds to the oncofetal H19 transcript and to the neuron-specific TAU mRNA and regulates their localizations. Binds to and stabilizes BTRC/FBW1A mRNA. Binds to the adenine-rich autoregulatory sequence (ARS) located in PABPC1 mRNA and represses its translation. PABPC1 mRNA-binding is stimulated by PABPC1 protein. Prevents BTRC/FBW1A mRNA degradation by disrupting microRNA-dependent interaction with AGO2. Promotes the directed movement of tumor-derived cells by fine-tuning intracellular signaling networks. Binds to MAPK4 3'-UTR and inhibits its translation. Interacts with PTEN transcript open reading frame (ORF) and prevents mRNA decay. This combined action on MAPK4 (down-regulation) and PTEN (up-regulation) antagonizes HSPB1 phosphorylation, consequently it prevents G-actin sequestration by phosphorylated HSPB1, allowing F-actin polymerization. Hence enhances the velocity of cell migration and stimulates directed cell migration by PTEN-modulated polarization. Interacts with Hepatitis C virus (HCV) 5'-UTR and 3'-UTR and specifically enhances translation at the HCV IRES, but not 5'-cap-dependent translation, possibly by recruiting eIF3. Interacts with HIV-1 GAG protein and blocks the formation of infectious HIV-1 particles. Reduces HIV-1 assembly by inhibiting viral RNA packaging, as well as assembly and processing of GAG protein on cellular membranes. During cellular stress, such as oxidative stress or heat shock, stabilizes target mRNAs that are recruited to stress granules, including CD44, IGF2, MAPK4, MYC, PTEN, RAPGEF2 and RPS6KA5 transcripts","subcellular_location":"Nucleus; Cytoplasm; Cytoplasm, perinuclear region; Cytoplasm, P-body; Cytoplasm, Stress granule; Cell projection, lamellipodium; Cell projection, dendrite; Cell projection, dendritic spine; Cell projection, growth cone; Cell projection, filopodium; Cell projection, axon","url":"https://www.uniprot.org/uniprotkb/Q9NZI8/entry"},"depmap":{"release":"DepMap","has_data":true,"is_common_essential":false,"resolved_as":"","url":"https://depmap.org/portal/gene/IGF2BP1","classification":"Not 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NONCODING; SNHG11","url":"https://www.omim.org/entry/619494"},{"mim_id":"619296","title":"TESTIS-ASSOCIATED ONCOGENIC LONG NONCODING RNA; THORLNC","url":"https://www.omim.org/entry/619296"},{"mim_id":"611911","title":"IRON-SULFUR CLUSTER ASSEMBLY ENZYME; ISCU","url":"https://www.omim.org/entry/611911"},{"mim_id":"608289","title":"INSULIN-LIKE GROWTH FACTOR 2 mRNA-BINDING PROTEIN 2; IGF2BP2","url":"https://www.omim.org/entry/608289"}],"hpa":{"profiled":true,"resolved_as":"","reliability":"Supported","locations":[{"location":"Cytosol","reliability":"Supported"}],"tissue_specificity":"Group enriched","tissue_distribution":"Detected in some","driving_tissues":[{"tissue":"placenta","ntpm":5.1},{"tissue":"testis","ntpm":4.5}],"url":"https://www.proteinatlas.org/search/IGF2BP1"},"hgnc":{"alias_symbol":["IMP-1","IMP1"],"prev_symbol":[]},"alphafold":{"accession":"Q9NZI8","domains":[{"cath_id":"3.30.70.330","chopping":"2-71","consensus_level":"medium","plddt":83.5149,"start":2,"end":71},{"cath_id":"3.30.70.330","chopping":"81-152","consensus_level":"medium","plddt":81.2801,"start":81,"end":152},{"cath_id":"3.30.310.210","chopping":"197-354","consensus_level":"medium","plddt":86.9963,"start":197,"end":354},{"cath_id":"3.30.310.210","chopping":"405-563","consensus_level":"medium","plddt":87.2595,"start":405,"end":563}],"viewer_url":"https://alphafold.ebi.ac.uk/entry/Q9NZI8","model_url":"https://alphafold.ebi.ac.uk/files/AF-Q9NZI8-F1-model_v6.cif","pae_url":"https://alphafold.ebi.ac.uk/files/AF-Q9NZI8-F1-predicted_aligned_error_v6.png","plddt_mean":77.38},"mouse_models":{"mgi_url":"https://www.informatics.jax.org/marker/summary?nomen=IGF2BP1","jax_strain_url":"https://www.jax.org/strain/search?query=IGF2BP1"},"sequence":{"accession":"Q9NZI8","fasta_url":"https://rest.uniprot.org/uniprotkb/Q9NZI8.fasta","uniprot_url":"https://www.uniprot.org/uniprotkb/Q9NZI8/entry","alphafold_viewer_url":"https://alphafold.ebi.ac.uk/entry/Q9NZI8"}},"corpus_meta":[{"pmid":"30371874","id":"PMC_30371874","title":"IGF2BP1 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Simultaneously, IGF2BP1 stabilizes PTEN mRNA, enhancing PTEN expression and antagonizing PIP3 signaling to enforce RAC1-dependent cell polarization and directionality.\",\n      \"method\": \"RNA binding assays, knockdown/overexpression in tumor cell lines, cell migration assays, epistasis with MK5, RAC1, and HSP27\",\n      \"journal\": \"Genes & development\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 / Strong — multiple orthogonal methods (mRNA translation assays, protein phosphorylation, actin dynamics, directional migration) with defined pathway placement and mechanistic cascade\",\n      \"pmids\": [\"22279049\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2019,\n      \"finding\": \"IGF2BP1 promotes SRF expression by impairing miRNA-directed decay of SRF mRNA in an m6A-dependent manner. IGF2BP1 associates with target mRNAs in RISC-free complexes and its deletion enhances mRNA association with AGO2, indicating IGF2BP1 antagonizes miRNA-mediated mRNA degradation by competing with RISC.\",\n      \"method\": \"Gene expression analysis, AGO2-RIP, miRNA depletion experiments, m6A-dependent assays, knockdown/overexpression in cancer cell lines and nude mouse xenografts\",\n      \"journal\": \"Nucleic acids research\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 / Strong — multiple orthogonal methods (AGO2-RIP, miRNA depletion, m6A dependence, in vivo xenograft), replicated across multiple target mRNAs and cell lines\",\n      \"pmids\": [\"30371874\", \"29660014\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2020,\n      \"finding\": \"The oncopeptide RBRP (encoded by LINC00266-1) directly binds IGF2BP1 and strengthens its m6A recognition on target RNAs such as c-Myc mRNA, increasing mRNA stability and c-Myc expression to promote tumorigenesis.\",\n      \"method\": \"Co-immunoprecipitation, RNA pulldown, m6A recognition assays, mRNA stability assays, overexpression/knockdown in cancer cells\",\n      \"journal\": \"Nature communications\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — reciprocal Co-IP and functional rescue experiments in single lab, mechanistically novel regulatory subunit concept\",\n      \"pmids\": [\"32245947\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2021,\n      \"finding\": \"IGF2BP1 recognizes m6A sites in the 3'UTR of PEG10 mRNA and recruits PABPC1 to enhance PEG10 mRNA stability, increasing PEG10 protein expression in endometrial cancer cells.\",\n      \"method\": \"RIP-seq, MeRIP-seq, RNA-seq, Co-immunoprecipitation and mass spectrometry to identify PABPC1 as interacting partner, mRNA stability assays\",\n      \"journal\": \"Theranostics\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — RIP-seq and MeRIP-seq combined with Co-IP/MS in single lab; identification of PABPC1 as recruitment partner is mechanistically novel\",\n      \"pmids\": [\"33391523\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2022,\n      \"finding\": \"A small molecule cucurbitacin B (CuB) directly targets IGF2BP1 at Cys253 in the KH1-2 domains, causing an allosteric effect that blocks IGF2BP1 recognition of m6A mRNA targets such as c-MYC.\",\n      \"method\": \"Chemical genetics, direct binding assays (Cys253 targeting), KH domain mutagenesis, m6A RNA binding assays, in vivo xenograft models\",\n      \"journal\": \"ACS central science\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — direct binding to defined residue with functional validation, single lab but multiple orthogonal methods\",\n      \"pmids\": [\"36032766\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2023,\n      \"finding\": \"PRMT3 methylates IGF2BP1 at R452, which is critical for IGF2BP1 function in stabilizing the mRNA of HEG1. PRMT3-mediated arginine methylation of IGF2BP1 drives oxaliplatin resistance in hepatocellular carcinoma.\",\n      \"method\": \"CRISPR/Cas9 activation library screen, transcriptomic profiling, site-specific mutagenesis at R452, mRNA stability assays, in vitro and in vivo functional validation\",\n      \"journal\": \"Nature communications\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 1 / Strong — site-specific mutagenesis of modification site combined with functional rescue and in vivo validation; rigorous multi-method approach in single study\",\n      \"pmids\": [\"37024475\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2021,\n      \"finding\": \"FBXO45 E3 ubiquitin ligase promotes IGF2BP1 ubiquitination at Lys190 and Lys450, leading to IGF2BP1 activation and subsequent upregulation of PLK1 expression, driving cell proliferation and liver tumorigenesis.\",\n      \"method\": \"Co-immunoprecipitation, ubiquitination assays, site-specific mutagenesis (Lys190/Lys450), IGF2BP1 knockdown rescue experiments, transgenic mouse models\",\n      \"journal\": \"eLife\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 1 / Strong — site-specific ubiquitination mutagenesis with functional validation in vitro and in transgenic mice; multiple orthogonal methods\",\n      \"pmids\": [\"34779401\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2023,\n      \"finding\": \"TRIM29 E3 ubiquitin ligase interacts with IGF2BP1 and induces K48-linked ubiquitination at Lys440 and Lys450, leading to IGF2BP1 protein degradation. IGF2BP1 promotes PD-L1 mRNA stability in a 3'UTR and m6A-dependent manner, and TRIM29-mediated degradation of IGF2BP1 reduces PD-L1 expression to enhance antitumor T-cell immunity.\",\n      \"method\": \"Proteomics, co-immunoprecipitation, site-specific ubiquitination assays (K48-linked), mRNA stability assays, in vivo tumor models\",\n      \"journal\": \"Cancer letters\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — reciprocal Co-IP with proteomics identification, site-specific ubiquitination characterization, single lab\",\n      \"pmids\": [\"38029830\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2023,\n      \"finding\": \"USP10 deubiquitinase directly binds, deubiquitinates, and stabilizes IGF2BP1 protein. IGF2BP1 in turn recognizes m6A sites on CPT1A mRNA to enhance its stability, mediating breast cancer metastasis.\",\n      \"method\": \"Co-immunoprecipitation, deubiquitination assays, MeRIP-seq, mRNA stability assays, in vitro and in vivo metastasis models\",\n      \"journal\": \"International journal of biological sciences\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — reciprocal Co-IP with functional deubiquitination assay and MeRIP-seq validation, single lab\",\n      \"pmids\": [\"36632454\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2021,\n      \"finding\": \"A small molecule inhibitor binds to a hydrophobic surface at the boundary of IGF2BP1 KH3 and KH4 domains and inhibits KRAS RNA binding, reducing KRAS mRNA and protein levels and downstream oncogenic signaling.\",\n      \"method\": \"Small molecule screening, direct binding assays to KH3/KH4 domain interface, RNA binding competition assays, wound healing and soft agar growth assays\",\n      \"journal\": \"RNA biology\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — direct binding to defined domain with functional RNA-binding competition assays, single lab\",\n      \"pmids\": [\"34895045\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2014,\n      \"finding\": \"IGF2BP1 drives translation of cIAP1 mRNA in rhabdomyosarcoma cells, protecting them from TNF-α-mediated apoptosis. IGF2BP1 knockdown reduces cIAP1 levels and sensitizes cells to cell death.\",\n      \"method\": \"IGF2BP1 knockdown, cIAP1 protein and mRNA quantification, TNF-α-mediated apoptosis assays, in vivo tumor growth experiments with IAP antagonists\",\n      \"journal\": \"Oncogene\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — knockdown with defined translational target and functional apoptosis readout, in vivo validation\",\n      \"pmids\": [\"24704827\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2017,\n      \"finding\": \"IGF2BP1 overexpression in human adult erythroblasts causes fetal-like hemoglobin expression by reprogramming at the transcriptional level; mechanistically, IGF2BP1 reduces BCL11A protein expression via posttranscriptional mechanisms (mRNA stability and polysome analysis) to increase fetal hemoglobin.\",\n      \"method\": \"Erythroid-specific IGF2BP1 overexpression, hemoglobin quantification by HPLC, mRNA stability and polysome sedimentation assays for BCL11A\",\n      \"journal\": \"Proceedings of the National Academy of Sciences of the United States of America\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — multiple orthogonal methods (polysome profiling, mRNA stability, HPLC hemoglobin quantification) in primary human cells, single lab\",\n      \"pmids\": [\"28652347\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2019,\n      \"finding\": \"IGF2BP1 controls the cargo of melanoma-derived extracellular vesicles (EVs) to promote metastasis. IGF2BP1 knockdown did not alter EV size, number, or protein/RNA concentration, but altered EV mRNA, protein, and miRNA cargo, blocking pre-metastatic niche formation by inhibiting fibronectin deposition and CD45+ cell accumulation in lungs.\",\n      \"method\": \"In vivo metastasis models (two models), EV isolation and characterization, RNA-sequencing and proteomics of EVs, IGF2BP1 knockdown/overexpression\",\n      \"journal\": \"Oncogene\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — two in vivo models with EV proteomics/transcriptomics, single lab\",\n      \"pmids\": [\"30936459\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2020,\n      \"finding\": \"IGF2BP1 maintains intestinal barrier function by directly binding occludin (Ocln) mRNA and stabilizing it, increasing occludin protein expression. Conditional knockout of IGF2BP1 in intestinal epithelial cells causes impaired tight junction function and colitis; ectopic occludin expression rescues barrier function in IGF2BP1-knockdown cells.\",\n      \"method\": \"Conditional knockout mouse (Villin CreERT2:Igf2bp1flox/flox), gut barrier assays, RIP demonstrating direct Ocln mRNA binding, mRNA stability assays, occludin rescue experiments\",\n      \"journal\": \"The Journal of biological chemistry\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 / Strong — in vivo conditional KO with specific phenotype, direct RIP, mRNA stability, and rescue experiment; multiple orthogonal methods\",\n      \"pmids\": [\"32385106\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2019,\n      \"finding\": \"IGF2BP1 directly binds and stabilizes ETV6/RUNX1 fusion mRNA in t(12;21)-positive acute lymphoblastic leukemia, as shown by RIP enrichment and the reduction of ETV6/RUNX1 mRNA upon IGF2BP1 knockdown.\",\n      \"method\": \"RNA immunoprecipitation (RIP), IGF2BP1 knockdown, quantification of ETV6/RUNX1 mRNA in cell lines and primary patient samples\",\n      \"journal\": \"Blood cells, molecules & diseases\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — RIP with functional knockdown validation in cell lines and primary samples, single lab\",\n      \"pmids\": [\"26852652\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2019,\n      \"finding\": \"IGF2BP1 maintains leukemia stem cell properties by stabilizing HOXB4, MYB, and ALDH1A1 mRNAs, as demonstrated by CLIP and PAR-CLIP techniques. Chemical or genetic inhibition of IGF2BP1 decreases tumorigenicity, promotes differentiation, and sensitizes leukemia cells to chemotherapy.\",\n      \"method\": \"CLIP, PAR-CLIP, gain- and loss-of-function systems, tumor-initiating potential assays\",\n      \"journal\": \"Leukemia\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — CLIP/PAR-CLIP with functional validation, single lab\",\n      \"pmids\": [\"31768017\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2020,\n      \"finding\": \"IGF2BP1 promotes SRC kinase activation through a protein-ligand-induced, RNA-independent mechanism, and separately enhances ERK2 expression in an RNA-binding-dependent manner, connecting SRC/MAPK signaling to promote invasive growth in ovarian cancer cells.\",\n      \"method\": \"Protein interaction studies, SRC kinase activation assays, RNA-binding-deficient mutants, 3D invasion cultures, intraperitoneal mouse models, SRC/MEK inhibitor rescue experiments\",\n      \"journal\": \"RNA biology\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — RNA-binding-deficient mutants distinguish RNA-independent SRC activation from RNA-dependent ERK2 regulation; in vivo validation, single lab\",\n      \"pmids\": [\"32876513\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2019,\n      \"finding\": \"IGF2BP1 binds Lnc-THOR RNA; disruption of Lnc-THOR–IGF2BP1 association (by triptonide or Lnc-THOR/IGF2BP1 CRISPR knockout) depletes IGF2BP1 mRNA targets (Myc, IGF2, Gli1) and inhibits NPC cell growth, establishing that Lnc-THOR stabilizes IGF2BP1-dependent target mRNAs.\",\n      \"method\": \"Small molecule disruption, CRISPR/Cas9 knockout of Lnc-THOR and IGF2BP1, target mRNA quantification, in vivo xenograft models\",\n      \"journal\": \"Cancer letters\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — genetic epistasis with dual CRISPR KO and functional rescue, single lab\",\n      \"pmids\": [\"30503558\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2021,\n      \"finding\": \"mTORC2 phosphorylates IGF2BP1 at Ser181; prevention of this phosphorylation enhances translation and destabilization of c-myc mRNA. Src kinase phosphorylates IGF2BP1 at Tyr396; prevention of Tyr396 phosphorylation causes accumulation of translationally silent IGF2BP1-sequestered mRNA in cytoplasmic granules.\",\n      \"method\": \"mTORC2 and Src kinase inhibition, phospho-site mutagenesis (Ser181, Tyr396), reporter assays with CRD sequence, polysome analysis, xenograft models\",\n      \"journal\": \"Cellular signalling\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — phospho-site mutagenesis with functional CRD reporter and xenograft validation, single lab\",\n      \"pmids\": [\"33388443\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2019,\n      \"finding\": \"IGF2BP1 directly binds MAP1LC3B, ATG3, and ATG5 transcripts (autophagy gene mRNAs), as demonstrated by in silico and biochemical analyses. Intestinal epithelial Imp1 deletion leads to upregulation of Atg5 and increased autophagy flux, and double knockout of Imp1 and Atg7 increases sensitivity to colonic injury, establishing a compensatory relationship between IMP1/IGF2BP1 and autophagy.\",\n      \"method\": \"Conditional knockout mice, RNA-IP, in silico binding analysis, DSS colitis models, autophagy flux assays, double-mutant epistasis\",\n      \"journal\": \"EMBO reports\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — direct RIP with genetic epistasis in double-mutant mice, single lab\",\n      \"pmids\": [\"31061170\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2022,\n      \"finding\": \"IGF2BP1 knockout mice display disorganized neocortical development with loss of cortical marginal cell density and fewer mitotically active cells. In IGF2BP1-null neurons, β-actin mRNA shows increased transcription rates and total protein content but decreased transport and anchoring, demonstrating IGF2BP1 is required for proper β-actin mRNA localization and transport in neurons.\",\n      \"method\": \"IGF2BP1 knockout mice, BrdU labeling, endogenously tagged β-actin-MS2 mRNA imaging, mRNA transport and anchoring measurements, transcription rate analysis\",\n      \"journal\": \"Proceedings of the National Academy of Sciences of the United States of America\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 / Strong — in vivo knockout with endogenous mRNA tagging and live imaging; multiple orthogonal methods for mRNA localization, transport, and protein quantification\",\n      \"pmids\": [\"36067310\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2015,\n      \"finding\": \"Igf2bp1 knockdown in zebrafish reduces retinal ganglion cell (RGC) axonal outgrowth and tectal coverage. RGC-specific expression of a phosphomimetic Igf2bp1 reduces axonal projection density without affecting RGC survival, demonstrating Igf2bp1 is required for axon outgrowth in vivo and that its phosphorylation state modulates this function.\",\n      \"method\": \"Morpholino knockdown and phosphomimetic rescue in zebrafish, timelapse imaging of RGC axon outgrowth, photoconvertible fluorescent protein reporter under β-actin 3'UTR\",\n      \"journal\": \"PloS one\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — in vivo knockdown with phosphomimetic rescue and live imaging, single lab\",\n      \"pmids\": [\"26325373\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2023,\n      \"finding\": \"RPS15 interacts with the KH domain of IGF2BP1, and this complex recognizes and directly binds the 3'UTR of MKK6 and MAPK14 mRNAs in an m6A-dependent manner to promote translation of core p38 MAPK pathway proteins and drive ESCC metastasis.\",\n      \"method\": \"CRISPR SAM library screen, Co-IP of RPS15-IGF2BP1, m6A-dependent RIP for MKK6/MAPK14 mRNAs, targeted drug screening, in vitro and in vivo functional assays\",\n      \"journal\": \"Signal transduction and targeted therapy\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — Co-IP with mechanistic m6A-RIP validation and in vivo studies, single lab\",\n      \"pmids\": [\"37264021\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2019,\n      \"finding\": \"IGF2BP1 promotes LPS-induced NFκB signaling in human macrophages and monocytes. Co-immunoprecipitation showed IGF2BP1 associates with the p65-p52 NFκB complex in nuclei of LPS-treated cells; IGF2BP1 knockdown/knockout inhibits p65-p52 nuclear translocation and NFκB transcriptional activation.\",\n      \"method\": \"Co-immunoprecipitation of IGF2BP1 with NFκB p65-p52, nuclear fractionation, shRNA knockdown and CRISPR/Cas9 KO, cytokine ELISA\",\n      \"journal\": \"Biochemical and biophysical research communications\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — Co-IP with nuclear complex and functional KO validation, single lab\",\n      \"pmids\": [\"31000200\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2022,\n      \"finding\": \"MNX1-AS1 lncRNA binds IGF2BP1 and drives its phase separation, which increases IGF2BP1 interaction with the 3'UTR of c-Myc and E2F1 mRNAs to promote their stability, creating a c-Myc/MNX1-AS1/IGF2BP1 positive feedback loop driving cell-cycle progression.\",\n      \"method\": \"RNA-protein binding assays, phase separation assays, 3'UTR interaction studies, cell cycle analysis, patient-derived xenograft model\",\n      \"journal\": \"Cancer research\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — phase separation and RNA-binding assays with functional rescue and PDX model, single lab\",\n      \"pmids\": [\"36214649\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2023,\n      \"finding\": \"MKRN3 interacts with IGF2BP1 (identified by proteomics), and IGF2BP1 in turn interacts with polyadenylate-binding protein family members, positioning IGF2BP1 as a target of MKRN3-mediated regulation of hypothalamic puberty-related gene expression.\",\n      \"method\": \"Proteomics interactome analysis, co-immunoprecipitation, Mkrn3 knockout mouse model\",\n      \"journal\": \"JCI insight\",\n      \"confidence\": \"Low\",\n      \"confidence_rationale\": \"Tier 3 / Weak — single Co-IP/proteomics identification without mechanistic follow-up for the IGF2BP1 interaction specifically\",\n      \"pmids\": [\"37092553\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2023,\n      \"finding\": \"IGF2BP1 directly binds and stabilizes INHBA mRNA; knockdown of IGF2BP1 reduces INHBA expression and attenuates Smad2/3 signaling to suppress ESCC cell invasion and migration. IGF2BP1 also interacts with G3BP1, and G3BP1 knockdown similarly downregulates INHBA-Smad2/3 signaling.\",\n      \"method\": \"RIP-seq, mass spectrometry for interacting proteins (identifying G3BP1), gene-specific m6A PCR, RNA stability assays, BTYNB inhibitor treatment\",\n      \"journal\": \"Experimental hematology & oncology\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — RIP-seq with MS-identified G3BP1 interaction and functional RNA stability validation, single lab\",\n      \"pmids\": [\"37644505\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2024,\n      \"finding\": \"ZDHHC1 palmitoylates IGF2BP1 at C337 (S-palmitoylation), which results in downregulated expression of LIPG mRNA via m6A modification, suppressing colorectal cancer cell growth.\",\n      \"method\": \"Palmitoylation assays, site-specific mutagenesis (C337), m6A modification analysis, mRNA stability assays, in vitro and in vivo functional studies\",\n      \"journal\": \"Cancer gene therapy\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — site-specific palmitoylation mutagenesis with functional m6A downstream readout, single lab\",\n      \"pmids\": [\"39069526\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2023,\n      \"finding\": \"IGF2BP1 directly binds and governs expression of SEMA3A and SHMT2 in neuroblastoma cells, modulating their protein levels in small extracellular vesicles (EVs) to regulate pro-metastatic microenvironment formation at potential metastatic organs.\",\n      \"method\": \"Unbiased proteomics of EVs, direct binding assays, knockdown/overexpression in immunocompetent mouse NB models, EV isolation and characterization\",\n      \"journal\": \"Oncogene\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — unbiased proteomics with functional validation in multiple immunocompetent models, single lab\",\n      \"pmids\": [\"36973517\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2017,\n      \"finding\": \"IGF2BP1 is identified as a novel binding partner of p38 MAPK by co-immunoprecipitation followed by mass spectrometry.\",\n      \"method\": \"Co-immunoprecipitation, mass spectrometry, in silico domain interaction analysis\",\n      \"journal\": \"Molecular and cellular biochemistry\",\n      \"confidence\": \"Low\",\n      \"confidence_rationale\": \"Tier 3 / Weak — single Co-IP/MS identification without functional follow-up on the interaction\",\n      \"pmids\": [\"28497370\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2023,\n      \"finding\": \"IGF2BP1 stabilizes c-MYC mRNA via m6A-dependent binding in gastric cancer cells, promoting aerobic glycolysis and cancer progression. However, a separate study in gastric cancer found IGF2BP1 promotes degradation and reduces translation efficiency of MYC mRNA in an m6A-dependent manner, suggesting a cell-context-dependent switch in IGF2BP1's regulation of MYC.\",\n      \"method\": \"RIP, MeRIP, mRNA stability assays, polysome profiling, gain/loss of function in gastric cancer cells\",\n      \"journal\": \"Experimental cell research / Cancer science\",\n      \"confidence\": \"Low\",\n      \"confidence_rationale\": \"Tier 3 / Weak — single-lab experiments with contradictory outcomes between two papers; mechanism direction uncertain\",\n      \"pmids\": [\"35489385\", \"38115228\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2022,\n      \"finding\": \"IGF2BP1 stabilizes EZH2 mRNA in an m6A-dependent manner in neuroendocrine tumor cells, enhancing EZH2 protein levels which then trimethylates H3K27 to silence cell cycle arrest genes and drive proliferation.\",\n      \"method\": \"mRNA stability assays, m6A-dependent RIP, IGF2BP1 inhibitor (BTYNB), cell cycle analysis, H3K27me3 ChIP\",\n      \"journal\": \"Cancers\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — mRNA stability with m6A dependence, ChIP readout, and pharmacological inhibition, single lab\",\n      \"pmids\": [\"35565249\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2022,\n      \"finding\": \"Heat treatment promotes IGF2BP1 aggregation specifically in the presence of m6A-modified HPV E7 mRNA, forming heat-induced m6A E7 mRNA-IGF2BP1 granules that are resolved by the ubiquitin-proteasome system, downregulating E7 mRNA and protein.\",\n      \"method\": \"Heat treatment assays, m6A mutation experiments, granule imaging, proteasome inhibition assays, in vitro and in vivo HPV carcinogenesis models\",\n      \"journal\": \"Cell reports\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — m6A mutation and proteasome inhibition experiments with mechanistic granule imaging, single lab\",\n      \"pmids\": [\"36288717\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2024,\n      \"finding\": \"In zebrafish, Igf2bp1 acts as a reader of METTL16-mediated m6A modifications on mybl2b mRNA (cell-cycle transcription factor); Mettl16 deficiency destabilizes mybl2b mRNA due to lost Igf2bp1 binding, causing G1/S arrest in embryonic hematopoietic stem and progenitor cells. The METTL16-m6A-MYBL2-IGF2BP1 axis is conserved in humans.\",\n      \"method\": \"Single-cell RNA-seq cross-species, Mettl16-deficient zebrafish, methyltransferase-dead rescue, m6A-RIP for mybl2b, in vivo HSPC proliferation assays, human cell validation\",\n      \"journal\": \"The EMBO journal\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 / Strong — in vivo zebrafish model with methyltransferase-dead rescue, direct m6A-RIP, cross-species conservation validation; multiple orthogonal methods\",\n      \"pmids\": [\"38605226\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2023,\n      \"finding\": \"IGF2BP1 synergizes with ETV6-RUNX1 fusion protein in B-ALL by binding and stabilizing the ETV6::RUNX1 fusion transcript, creating a positive feedback loop that constitutively dysregulates TNFα/NFκB and PI3K-Akt oncogenic pathways; co-expression in mouse bone marrow causes pre-leukemic hypercellularity and splenomegaly.\",\n      \"method\": \"RIP-seq after IGF2BP1 pulldown, RNA-seq after IGF2BP1 KO, bone marrow transplant mouse model with retroviral co-expression, patient sample validation\",\n      \"journal\": \"Journal of experimental & clinical cancer research\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 / Strong — RIP-seq and RNA-seq integration, in vivo pre-leukemic model, patient sample correlation; multiple orthogonal methods\",\n      \"pmids\": [\"37670323\"],\n      \"is_preprint\": false\n    }\n  ],\n  \"current_model\": \"IGF2BP1 is an oncofetal RNA-binding protein that primarily stabilizes target mRNAs (including KRAS, c-MYC, PTEN, ACTB, cIAP1, PD-L1, and many others) in an m6A-dependent manner by competing with RISC/miRNA-mediated decay and recruiting co-factors such as PABPC1; its activity is regulated by post-translational modifications including PRMT3-mediated arginine methylation at R452, mTORC2-mediated Ser181 phosphorylation, Src-mediated Tyr396 phosphorylation, and ubiquitination at Lys190/Lys450/Lys440 by E3 ligases FBXO45 and TRIM29 (counteracted by USP10 deubiquitination), and palmitoylation at C337 by ZDHHC1; structurally, its KH3-4 domain interface mediates RNA binding and is the target of small molecule inhibitors; in neurons and developing tissues IGF2BP1 localizes mRNA (particularly β-actin mRNA) to regulate local translation and axon outgrowth, while in cancer cells it promotes migration, invasion, immune evasion, and stem cell properties through these post-transcriptional regulatory mechanisms.\"\n}\n```","stage2_raw":"```json\n{\n  \"mechanistic_narrative\": \"IGF2BP1 is an oncofetal m6A-reader RNA-binding protein that post-transcriptionally controls the fate of target mRNAs to govern cell migration, proliferation, stemness, and tissue development [#1, #20]. Its dominant mechanism is m6A-dependent recognition of target transcripts, where binding stabilizes mRNAs by antagonizing miRNA/RISC-directed decay; IGF2BP1 associates with target mRNAs in RISC-free complexes, and its loss enhances AGO2 association and degradation of targets such as SRF [#1]. Stabilization is reinforced by recruitment of co-factors including PABPC1 to m6A 3'UTR sites [#3], and it acts on an extensive target set spanning oncogenic and barrier programs — PTEN and MAPK4 to enforce directional migration via actin dynamics [#0], cIAP1 to suppress apoptosis [#10], PD-L1 to drive immune evasion [#7], EZH2 to silence cell-cycle genes [#31], and occludin to maintain intestinal tight junctions [#13]. In neurons IGF2BP1 localizes β-actin mRNA for transport and anchoring to support cortical development and axon outgrowth [#20, #21]. Its activity and abundance are tuned by a network of post-translational modifications: PRMT3-mediated arginine methylation at R452 [#5], mTORC2 Ser181 and Src Tyr396 phosphorylation [#18], ZDHHC1 palmitoylation at C337 [#27], and competing ubiquitination by FBXO45 (K190/K450, activating) and TRIM29 (K48-linked K440/K450, degrading) opposed by USP10 deubiquitination [#6, #7, #8]. The protein is functionally co-opted by regulatory lncRNAs and oncopeptides (RBRP, Lnc-THOR, MNX1-AS1) that enhance its m6A recognition or drive its phase separation [#2, #17, #24], and its RNA-binding KH3-4 interface and KH1-2 Cys253 are targetable by small molecules that block recognition of KRAS and c-MYC mRNAs [#4, #9].\",\n  \"teleology\": [\n    {\n      \"year\": 2012,\n      \"claim\": \"Established that IGF2BP1 directs cell migration through dual post-transcriptional control of cytoskeletal signaling, defining a concrete mechanistic cascade rather than a generic RNA-binding role.\",\n      \"evidence\": \"RNA binding, knockdown/overexpression, migration assays, and epistasis with MK5/RAC1/HSP27 in tumor cell lines\",\n      \"pmids\": [\"22279049\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Did not address m6A dependence of these specific targets\", \"Did not establish in vivo relevance\"]\n    },\n    {\n      \"year\": 2014,\n      \"claim\": \"Showed IGF2BP1 enforces apoptosis resistance by driving cIAP1 translation, linking its activity to tumor cell survival under death-receptor stress.\",\n      \"evidence\": \"Knockdown, cIAP1 protein/mRNA quantification, TNF-α apoptosis assays, in vivo tumor growth with IAP antagonists\",\n      \"pmids\": [\"24704827\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Mechanism of translational enhancement not resolved\", \"m6A involvement not tested\"]\n    },\n    {\n      \"year\": 2017,\n      \"claim\": \"Demonstrated IGF2BP1 can reprogram differentiated cells toward a fetal state by post-transcriptionally repressing BCL11A, extending its oncofetal role to erythroid identity.\",\n      \"evidence\": \"Erythroid-specific overexpression, HPLC hemoglobin quantification, polysome and mRNA stability assays in primary human erythroblasts\",\n      \"pmids\": [\"28652347\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Direct binding to BCL11A mRNA not fully resolved\", \"m6A dependence not addressed\"]\n    },\n    {\n      \"year\": 2019,\n      \"claim\": \"Defined the core decay-protection mechanism: IGF2BP1 shields m6A-marked target mRNAs by sequestering them away from AGO2/RISC, resolving how stabilization is achieved.\",\n      \"evidence\": \"AGO2-RIP, miRNA depletion, m6A-dependent assays, xenografts across multiple targets\",\n      \"pmids\": [\"30371874\", \"29660014\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Structural basis of RISC competition not defined\", \"Generality across all targets not established\"]\n    },\n    {\n      \"year\": 2019,\n      \"claim\": \"Expanded the target repertoire to stem cell, fusion-oncogene, autophagy, and inflammatory programs, showing IGF2BP1 sustains leukemia stemness, stabilizes ETV6/RUNX1 transcripts, buffers autophagy genes, and supports NF-κB signaling.\",\n      \"evidence\": \"CLIP/PAR-CLIP, RIP, conditional knockout mice, double-mutant epistasis, and Co-IP across leukemia, intestinal, and macrophage systems\",\n      \"pmids\": [\"31768017\", \"26852652\", \"31061170\", \"31000200\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"NF-κB association mechanism not resolved (RNA-dependent vs independent)\", \"Autophagy gene binding mostly in silico/RIP without rescue for all targets\"]\n    },\n    {\n      \"year\": 2020,\n      \"claim\": \"Revealed that an oncopeptide (RBRP) and a co-factor recruitment step (PABPC1) act as accessory modules strengthening IGF2BP1 m6A recognition and stabilization, and that IGF2BP1 has an RNA-independent function in activating SRC kinase.\",\n      \"evidence\": \"Co-IP, RNA pulldown, m6A recognition assays, RIP-seq/MeRIP-seq, RNA-binding-deficient mutants, in vivo models\",\n      \"pmids\": [\"32245947\", \"33391523\", \"32876513\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"RNA-independent SRC activation mechanism not structurally defined\", \"Stoichiometry and generality of PABPC1 recruitment unknown\"]\n    },\n    {\n      \"year\": 2021,\n      \"claim\": \"Showed IGF2BP1 abundance and activity are governed by ubiquitination and phosphorylation, defining FBXO45-driven activating ubiquitination and mTORC2/Src phospho-control of its translational repression function.\",\n      \"evidence\": \"Site-specific ubiquitination/phospho mutagenesis (K190/K450, Ser181, Tyr396), polysome analysis, transgenic and xenograft models\",\n      \"pmids\": [\"34779401\", \"33388443\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"How non-degradative ubiquitination activates IGF2BP1 mechanistically unclear\", \"Crosstalk between phospho- and ubiquitin marks not addressed\"]\n    },\n    {\n      \"year\": 2021,\n      \"claim\": \"Established the RNA-binding KH domains as druggable: small molecules at the KH3-4 interface and KH1-2 Cys253 block target recognition, validating IGF2BP1 as a therapeutic target.\",\n      \"evidence\": \"Small molecule screening, direct binding to defined residues/domains, RNA-binding competition, in vivo xenografts (CuB reported 2022)\",\n      \"pmids\": [\"34895045\", \"36032766\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"No co-crystal structure of inhibitor-bound complex reported\", \"Selectivity over paralogs not established\"]\n    },\n    {\n      \"year\": 2022,\n      \"claim\": \"Demonstrated IGF2BP1 function is shaped by phase separation and granule dynamics, with lncRNAs driving condensate formation that enhances target binding and stress/heat promoting m6A-dependent aggregation routed to proteasomal clearance.\",\n      \"evidence\": \"Phase separation assays, RNA-binding, granule imaging, m6A mutation, proteasome inhibition, PDX and HPV carcinogenesis models\",\n      \"pmids\": [\"36214649\", \"36288717\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Determinants of condensate composition not defined\", \"Relationship between activating condensates and degradative granules unclear\"]\n    },\n    {\n      \"year\": 2022,\n      \"claim\": \"Confirmed an in vivo developmental requirement: IGF2BP1 is needed for β-actin mRNA transport/anchoring and proper neocortical organization, anchoring its localization function in neurons genetically.\",\n      \"evidence\": \"IGF2BP1 knockout mice, endogenous β-actin-MS2 imaging, transport/anchoring and transcription-rate measurements\",\n      \"pmids\": [\"36067310\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Molecular machinery of mRNA transport not fully resolved\", \"Link to specific neuronal m6A marks not addressed\"]\n    },\n    {\n      \"year\": 2023,\n      \"claim\": \"Broadened the regulatory and partner landscape: PRMT3 methylation (R452), TRIM29/USP10 ubiquitin balance, and partners RPS15, G3BP1, and the ETV6-RUNX1 fusion couple IGF2BP1 to drug resistance, immune evasion, metastasis, and leukemogenesis.\",\n      \"evidence\": \"CRISPR activation screens, site-specific mutagenesis, Co-IP/MS, m6A-RIP, RIP-seq/RNA-seq, in vivo tumor and pre-leukemic models\",\n      \"pmids\": [\"37024475\", \"38029830\", \"36632454\", \"37264021\", \"37644505\", \"37670323\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"How distinct PTMs are integrated on a single IGF2BP1 molecule unknown\", \"Whether RPS15/G3BP1 partnerships are constitutive or context-specific unresolved\"]\n    },\n    {\n      \"year\": 2024,\n      \"claim\": \"Placed IGF2BP1 within a defined writer-reader axis and added palmitoylation as a control layer, showing it reads METTL16-deposited m6A on MYBL2 to drive HSPC cell-cycle progression and that ZDHHC1 palmitoylation tunes its output.\",\n      \"evidence\": \"Mettl16-deficient zebrafish with methyltransferase-dead rescue, cross-species m6A-RIP, palmitoylation site mutagenesis (C337), functional assays\",\n      \"pmids\": [\"38605226\", \"39069526\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Whether other writers feed IGF2BP1 in different tissues unknown\", \"How palmitoylation alters IGF2BP1 localization/RNA selectivity not resolved\"]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"How IGF2BP1 selects between stabilizing versus destabilizing/translation-repressing fates for the same target (e.g. MYC) across cellular contexts remains unresolved.\",\n      \"evidence\": \"\",\n      \"pmids\": [],\n      \"confidence\": \"Low\",\n      \"gaps\": [\"Contradictory MYC outcomes reported in gastric cancer\", \"No unifying rule linking PTM/condensate state to target fate\", \"Context-dependent co-factor combinations not mapped\"]\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [\n      {\"term_id\": \"GO:0003723\", \"supporting_discovery_ids\": [0, 1, 3, 9, 13, 15, 20, 26, 33]},\n      {\"term_id\": \"GO:0140098\", \"supporting_discovery_ids\": [1, 3, 33]},\n      {\"term_id\": \"GO:0140110\", \"supporting_discovery_ids\": [1, 31]},\n      {\"term_id\": \"GO:0045182\", \"supporting_discovery_ids\": [0, 10, 18, 22]},\n      {\"term_id\": \"GO:0140313\", \"supporting_discovery_ids\": [18, 32]}\n    ],\n    \"localization\": [\n      {\"term_id\": \"GO:0005829\", \"supporting_discovery_ids\": [18, 20, 32]},\n      {\"term_id\": \"GO:0005634\", \"supporting_discovery_ids\": [23]}\n    ],\n    \"pathway\": [\n      {\"term_id\": \"R-HSA-8953854\", \"supporting_discovery_ids\": [1, 3, 33]},\n      {\"term_id\": \"R-HSA-1643685\", \"supporting_discovery_ids\": [5, 7, 34]},\n      {\"term_id\": \"R-HSA-162582\", \"supporting_discovery_ids\": [0, 16, 22, 26]},\n      {\"term_id\": \"R-HSA-168256\", \"supporting_discovery_ids\": [7, 23]},\n      {\"term_id\": \"R-HSA-392499\", \"supporting_discovery_ids\": [5, 6, 7, 8, 27]}\n    ],\n    \"complexes\": [],\n    \"partners\": [\"PABPC1\", \"RPS15\", \"G3BP1\", \"FBXO45\", \"TRIM29\", \"USP10\", \"PRMT3\", \"ZDHHC1\"],\n    \"other_free_text\": []\n  }\n}\n```","audit_flag":null,"evaluation":{"pairwise":"win","faith_supported":6,"faith_total":6,"faith_pct":100.0}}