ArticleNature structural & molecular biology2011
Structural basis of pre-let-7 miRNA recognition by the zinc knuckles of pluripotency factor Lin28.
Article in Nature structural & molecular biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 78 papers.
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Who cites it
78 citing papers in PubMed, 129 citations in OpenAlex.
- let-7 miRNA and lin-46 mRNA are essential targets of the LIN28 RNA-binding protein in Caenorhabditis elegans developmental timing regulation.PLoS biology · 2026Article
- Mechanistic insights into Lin28-dependent oligo-uridylylation of pre-let-7 by TUT4.Nucleic acids research · 2026Article
- Sulindac sulfide suppresses oncogenic transformation through let-7b-mediated repression of K-Ras signaling.Cell death discovery · 2025Article
- Development of miRNA-based PROTACs targeting Lin28 for breast cancer therapy.Science advances · 2024Article
- Structural basis for activity switching in polymerases determining the fate of let-7 pre-miRNAs.Nature structural & molecular biology · 2024Article
- Short 2'-O-methyl/LNA oligomers as highly-selective inhibitors of miRNA production in vitro and in vivo.Nucleic acids research · 2024Article
- The microRNA Let-7 and its exosomal form: Epigenetic regulators of gynecological cancers.Cell biology and toxicology · 2024Review
- EGCG Disrupts the LIN28B/Let-7 Interaction and Reduces Neuroblastoma Aggressiveness.International journal of molecular sciences · 2024Article
- Regulating Protein-RNA Interactions: Advances in Targeting the LIN28/Let-7 Pathway.International journal of molecular sciences · 2024Review
- Growth-suppressor microRNAs mediate synaptic overgrowth and behavioral deficits in Fragile X mental retardation protein deficiency.iScience · 2024Article
- Two cold shock domain containing proteins trigger the development of infectious Trypanosoma brucei.PLoS pathogens · 2023Article
- LIN28 Family in Testis: Control of Cell Renewal, Maturation, Fertility and Aging.International journal of molecular sciences · 2022Review
- The function and regulatory mechanism of RNA-binding proteins in breast cancer and their future clinical treatment prospects.Frontiers in oncology · 2022Review
- The distinct RNA-interaction modes of a small ZnF domain underlay TUT4(7) diverse action in miRNA regulation.RNA biology · 2021Article
- Non-microRNA binding competitively inhibits LIN28 regulation.Cell reports · 2021Article
- Trisubstituted Pyrrolinones as Small-Molecule Inhibitors Disrupting the Protein-RNA Interaction of LIN28 andACS medicinal chemistry letters · 2021Article
- Therapeutic targeting of RNA-binding protein by RNA-PROTAC.Molecular therapy : the journal of the American Society of Gene Therapy · 2021Article
- Identification of novel targets of miR-622 in hepatocellular carcinoma reveals common regulation of cooperating genes and outlines the oncogenic role of zinc finger CCHC-type containing 11.Neoplasia (New York, N.Y.) · 2021Article
- Lin28, a major translation reprogramming factor, gains access to YB-1-packaged mRNA through its cold-shock domain.Communications biology · 2021Article
- RNA-PROTACs: Degraders of RNA-Binding Proteins.Angewandte Chemie (International ed. in English) · 2021Article
18 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Lin28 inhibits the biogenesis of let-7 miRNAs through a direct interaction with the terminal loop of pre-let-7. This interaction requires the zinc-knuckle domains of Lin28. We show that the zinc knuckle domains of Lin28 are sufficient to provide binding selectivity for pre-let-7 miRNAs and present the NMR structure of human Lin28 zinc knuckles bound to the short sequence 5'-AGGAGAU-3'. The structure reveals that each zinc knuckle recognizes an AG dinucleotide separated by a single nucleotide spacer. This defines a new 5'-NGNNG-3' consensus motif that explains how Lin28 selectively recognizes pre-let-7 family members. Binding assays in cell lysates and functional assays in cultured cells demonstrate that the interactions observed in the solution structure also occur between the full-length protein and members of the pre-let-7 family. The consensus sequence explains several seemingly disparate previously published observations on the binding properties of Lin28.
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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.