ArticleThe Journal of biological chemistry2015
An RNA-binding Protein, Lin28, Recognizes and Remodels G-quartets in the MicroRNAs (miRNAs) and mRNAs It Regulates.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 42 citations in OpenAlex.
- MoRNiNG: A Database of RNA Modification Sites Associated with RNA Secondary Structure Dynamics.Genomics, proteomics & bioinformatics · 2026Article
- LIN28-mediated gene regulatory loops synchronize transitions throughout organogenesis.Biochemistry and biophysics reports · 2025Article
- An Anticancer Bioactive Peptide Combined with Oxaliplatin Inhibited Gastric Cancer CellsCurrent protein & peptide science · 2025Article
- Apurinic/Apyrimidinic Endodeoxyribonuclease 1 modulates RNA G-quadruplex folding of miR-92b and controls its expression in cancer cells.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- G-quadruplexes from non-coding RNAs.Journal of molecular medicine (Berlin, Germany) · 2023Review
- G-Quadruplexes Regulate miRNA Biogenesis in Live Zebrafish Embryos.International journal of molecular sciences · 2023Article
- Action and function of helicases on RNA G-quadruplexes.Methods (San Diego, Calif.) · 2022Review
- LIN28B inhibition sensitizes cells to p53-restoring PPI therapy through unleashed translational suppression.Oncogenesis · 2022Article
- DNA G-quadruplexes are uniquely stable in the presence of denaturants and monovalent cations.Biochemistry and biophysics reports · 2022Article
- Switchable DNA-Based Peroxidases Controlled by a Chaotropic Ion.Chembiochem : a European journal of chemical biology · 2022Article
- Interaction between non-coding RNAs, mRNAs and G-quadruplexes.Cancer cell international · 2022Review
- Can G-quadruplex become a promising target in HBV therapy?Frontiers in immunology · 2022Review
- MicroRNAs and Stem-like Properties: The Complex Regulation Underlying Stemness Maintenance and Cancer Development.Biomolecules · 2021Review
- RNA G-quadruplexes (rG4s): genomics and biological functions.Nucleic acids research · 2021Review
- Properties and biological impact of RNA G-quadruplexes: from order to turmoil and back.Nucleic acids research · 2020Article
- Inhibition of RNA-binding proteins with small molecules.Nature reviews. Chemistry · 2020Review
- Molecular entrapment by RNA: an emerging tool for disrupting protein-RNA interactionsRNA biology · 2020Article
- Article
- HMGA1 expression levels are elevated in pancreatic intraepithelial neoplasia cells in the Ptf1a-Cre; LSL-KrasG12D transgenic mouse model of pancreatic cancer.British journal of cancer · 2017Article
- RNA G-Quadruplexes in Biology: Principles and Molecular Mechanisms.Journal of molecular biology · 2017Review
Corrections and comments
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Authors and funding
9 authors at 2 institutions in 1 country.
Funding
Abstract
Lin28 is an evolutionarily conserved RNA-binding protein that inhibits processing of pre-let-7 microRNAs (miRNAs) and regulates translation of mRNAs that control developmental timing, pluripotency, metabolism, and tumorigenesis. The RNA features that mediate Lin28 binding to the terminal loops of let-7 pre-miRNAs and to Lin28-responsive elements (LREs) in mRNAs are not well defined. Here we show that Lin28 target datasets are enriched for RNA sequences predicted to contain stable planar structures of 4 guanines known as G-quartets (G4s). The imino NMR spectra of pre-let-7 loops and LREs contain resonances characteristic of G4 hydrogen bonds. These sequences bind to a G4-binding fluorescent dye, N-methyl-mesoporphyrin IX (NMM). Mutations and truncations in the RNA sequence that prevent G4 formation also prevent Lin28 binding. The addition of Lin28 to a pre-let-7 loop or an LRE reduces G4 resonance intensity and NMM binding, suggesting that Lin28 may function to remodel G4s. Further, we show that NMM inhibits Lin28 binding. Incubation of a human embryonal carcinoma cell line with NMM reduces its stem cell traits. In particular it increases mature let-7 levels, decreases OCT4, HMGA1, CCNB1, CDK4, and Lin28A protein, decreases sphere formation, and inhibits colony formation. Our results suggest a previously unknown structural feature of Lin28 targets and a new strategy for manipulating Lin28 function.
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