ArticleJournal of molecular biology2020
RNA-Binding Specificity of the Human Fragile X Mental Retardation Protein.
Article in Journal of molecular biology, 2020. 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, 34 citations in OpenAlex.
- Massively parallel characterization of RNA G-quadruplex stability and molecular recognition.Nucleic acids research · 2026Article
- Article
- A missense variant in the KH0-domain of FMRP downregulates the protein in a patient with the clinical hallmarks of fragile X syndrome.European journal of human genetics : EJHG · 2025Article
- Computational investigation of the sequence context of arginine/glycine-rich motifs in the human proteome.BMC genomics · 2025Article
- FMRP drives mRNP targets into translationally silenced complexes.Molecular cell · 2025Article
- The role of RNA binding proteins in cancer biology: A focus on FMRP.Genes & diseases · 2025Review
- RNA guanine content and G-quadruplex structure tune the phase behavior and material properties of biomolecular condensates.Scientific reports · 2025Article
- Novel p.Arg534del Mutation and MTHFR C667T Polymorphism in Fragile X Syndrome (FXS) With Autism Spectrum Phenotype: A Case Report.Case reports in genetics · 2025Article
- Nucleic acid-binding KH domain proteins influence a spectrum of biological pathways including as part of membrane-localized complexes.Journal of structural biology: X · 2024Article
- [DDX5-Targeting Fragile X Mental Retardation Protein Regulates the Wnt/β-catenin Signaling Pathway to Promote Epithelial Mesenchymal Transition in Breast Cancer].Sichuan da xue xue bao. Yi xue ban = Journal of Sichuan University. Medical science edition · 2024Article
- Article
- The FXR1 network acts as signaling scaffold for actomyosin remodeling.bioRxiv : the preprint server for biology · 2024Article
- Methylation across the central dogma in health and diseases: new therapeutic strategies.Signal transduction and targeted therapy · 2023Review
- Interaction of the Influenza A Virus NS1 Protein with the 5'-m7G-mRNA·eIF4E·eIF4G1 Complex.Biochemistry · 2022Article
- The Fragile X Protein Disordered Regions Bind a Novel RNA Target.Biochemistry · 2022Article
- FXS causing missense mutations disrupt FMRP granule formation, dynamics, and function.PLoS genetics · 2022Article
- The Fragile X Proteins Differentially Regulate Translation of Reporter mRNAs with G-quadruplex Structures.Journal of molecular biology · 2022Article
- Genome-Wide Characterization and Expression Analysis of KH Family Genes Response to ABA and SA inInternational journal of molecular sciences · 2022Article
- KH domain proteins: Another family of bacterial RNA matchmakers?Molecular microbiology · 2022Review
- The Human Fragile X Mental Retardation Protein Inhibits the Elongation Step of Translation through Its RGG and C-Terminal Domains.Biochemistry · 2020Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Fragile X syndrome is the most common form of inherited intellectual disability and is caused by a deficiency of the fragile X mental retardation protein (FMRP) in neurons. FMRP regulates the translation of numerous mRNAs within dendritic synapses, but how FMRP recognizes these target mRNAs remains unknown. FMRP has KH0, KH1, KH2, and RGG domains, which are thought to bind to specific RNA recognition elements (RREs). Several studies used high-throughput methods to identify various RREs in mRNAs that FMRP may bind to in vivo. However, there is little overlap in the mRNA targets identified by each study, suggesting that the RNA-binding specificity of FMRP is still unknown. To determine the specificity of FMRP for the RREs, we performed quantitative in vitroRNA binding studies with various constructs of human FMRP. Unexpectedly, our studies show that the KH domains do not bind to the previously identified RREs. To further investigate the RNA-binding specificity of FMRP, we developed a new method called Motif Identification by Analysis of Simple sequences (MIDAS) to identify single-stranded RNA sequences bound by KH domains. We find that the FMRP KH0, KH1, and KH2 domains bind weakly to the single-stranded RNA sequences suggesting that they may have evolved to bind more complex RNA structures. Additionally, we find that the RGG motif of human FMRP binds with a high affinity to an RNAG-quadruplex structure that lacks single-stranded loops, double-stranded stems, or junctions.
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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.