ArticleNucleic acids research2019
IMP1 KH1 and KH2 domains create a structural platform with unique RNA recognition and re-modelling properties.
Article in Nucleic acids research, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 17 citations in OpenAlex.
- A Phosphorylation Switch Modulates Configurational Codes in the Oncofetal IGF2BP RNA Binding Paralogs.bioRxiv : the preprint server for biology · 2026Article
- Structural insights into IMP2 dimerization and RNA binding.Journal of structural biology · 2025Article
- Novel insights into the interaction between IGF2BPs and ncRNAs in cancers.Cancer cell international · 2024Review
- The Emerging Role of IGF2BP2 in Cancer Therapy Resistance: From Molecular Mechanism to Future Potential.International journal of molecular sciences · 2024Review
- Insulin-like growth factor 2 mRNA-binding protein 1 (IGF2BP1) in hematological diseases.Molecular medicine (Cambridge, Mass.) · 2024Review
- m6a methylation orchestrates IMP1 regulation of microtubules during human neuronal differentiation.Nature communications · 2024Article
- IGF2BPs as novel mGenes & diseases · 2024Review
- Cooperativity boosts affinity and specificity of proteins with multiple RNA-binding domains.NAR genomics and bioinformatics · 2023Article
- Allosteric Regulation of IGF2BP1 as a Novel Strategy for the Activation of Tumor Immune Microenvironment.ACS central science · 2022Article
- HDLBP binds ER-targeted mRNAs by multivalent interactions to promote protein synthesis of transmembrane and secreted proteins.Nature communications · 2022Article
- Small molecule inhibitor of Igf2bp1 represses Kras and a pro-oncogenic phenotype in cancer cells.RNA biology · 2022Article
- KH domain proteins: Another family of bacterial RNA matchmakers?Molecular microbiology · 2022Review
- The distinct RNA-interaction modes of a small ZnF domain underlay TUT4(7) diverse action in miRNA regulation.RNA biology · 2021Article
- Oncogenic Potential of the Dual-Function Protein MEX3A.Biology · 2021Review
- Article
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Authors and funding
9 authors at 2 institutions in 1 country.
Funding
Abstract
IGF2 mRNA-binding protein 1 (IMP1) is a key regulator of messenger RNA (mRNA) metabolism and transport in organismal development and, in cancer, its mis-regulation is an important component of tumour metastasis. IMP1 function relies on the recognition of a diverse set of mRNA targets that is mediated by the combinatorial action of multiple RNA-binding domains. Here, we dissect the structure and RNA-binding properties of two key RNA-binding domains of IMP1, KH1 and KH2, and we build a kinetic model for the recognition of RNA targets. Our data and model explain how the two domains are organized as an intermolecular pseudo-dimer and that the important role they play in mRNA target recognition is underpinned by the high RNA-binding affinity and fast kinetics of this KH1KH2-RNA recognition unit. Importantly, the high-affinity RNA-binding by KH1KH2 is achieved by an inter-domain coupling 50-fold stronger than that existing in a second pseudo-dimer in the protein, KH3KH4. The presence of this strong coupling supports a role of RNA re-modelling in IMP1 recognition of known cancer targets.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.