ArticleNucleic acids research2021
G3BP1 binds to guanine quadruplexes in mRNAs to modulate their stabilities.
Article in Nucleic acids research, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.
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Who cites it
40 citing papers in PubMed, 47 citations in OpenAlex.
- RNA G-quadruplex-protein interactions: from nuclear RNA processing to cytoplasmic stress response and neurodegeneration.RNA biology · 2026Review
- Massively parallel characterization of RNA G-quadruplex stability and molecular recognition.Nucleic acids research · 2026Article
- Tumor-derived PCSK9-enriched exosomes reprogram adipocytes to drive metabolic dysregulation and immune evasion in triple-negative breast cancer.Cell death & disease · 2026Article
- Stress granule dynamics orchestrate colitis-to-cancer transition via TOM1-mediated disassembly and driven oncogenesis in response to inflammatory oxidative stress.Redox biology · 2026Article
- A novel NLP-based method and algorithm to discover RNA-binding protein (RBP) motifs, contexts, binding preferences, and interactions.RNA (New York, N.Y.) · 2026Article
- RNA G-quadruplexes mediate cooperativity in HNRNPH binding and splicing regulation.bioRxiv : the preprint server for biology · 2026Article
- A deep learning framework for comprehensive prediction of human RNA G-quadruplex-binding proteins.Bioinformatics (Oxford, England) · 2026Article
- Impact of G-quadruplex RNA oxidation on its conformational dynamics and interaction with ALS-associated TDP-43.Scientific reports · 2026Article
- G3BP1 methylation by PRMT5 facilitates its recruitment of TBK1 for IRF3 activation during host response to foreign ribonucleic acids.Frontiers in immunology · 2026Article
- Pharmacological modulation of stress granulesFrontiers in pharmacology · 2026Review
- G3BP1 reduction during cellular senescence promotes SVIL expression and selected senescence-associated phenotypes.Frontiers in cell and developmental biology · 2026Article
- Revealing G4 Structures as Drug Targets: Exploring the Potential of Novel Therapeutic Agents.Research (Washington, D.C.) · 2026Review
- Co-profiling of in situ RNA-protein interactions and transcriptome in single cells and tissues.Nature methods · 2025Article
- Article
- Coding relationship links RNA G-quadruplexes and protein RGG motifs in RNA-binding protein autoregulation.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Stress Granules in Infectious Disease: Cellular Principles and Dynamic Roles in Immunity and Organelles.International journal of molecular sciences · 2024Review
- The RNA-binding Selectivity of the RGG/RG Motifs of hnRNP U is Abolished by Elements Within the C-terminal Intrinsically Disordered Region.Journal of molecular biology · 2024Article
- RNA G-quadruplexes and stress: emerging mechanisms and functions.Trends in cell biology · 2024Review
- HMGB3 and SUB1 Bind to and Facilitate the Repair ofJournal of the American Chemical Society · 2024Article
- Single-cell total-RNA profiling unveils regulatory hubs of transcription factors.Nature communications · 2024Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
RNA guanine quadruplexes (rG4) assume important roles in post-transcriptional regulations of gene expression, which are often modulated by rG4-binding proteins. Hence, understanding the biological functions of rG4s requires the identification and functional characterizations of rG4-recognition proteins. By employing a bioinformatic approach based on the analysis of overlap between peaks obtained from rG4-seq analysis and those detected in >230 eCLIP-seq datasets for RNA-binding proteins generated from the ENCODE project, we identified a large number of candidate rG4-binding proteins. We showed that one of these proteins, G3BP1, is able to bind directly to rG4 structures with high affinity and selectivity, where the binding entails its C-terminal RGG domain and is further enhanced by its RRM domain. Additionally, our seCLIP-Seq data revealed that pyridostatin, a small-molecule rG4 ligand, could displace G3BP1 from mRNA in cells, with the most pronounced effects being observed for the 3'-untranslated regions (3'-UTR) of mRNAs. Moreover, luciferase reporter assay results showed that G3BP1 positively regulates mRNA stability through its binding with rG4 structures. Together, we identified a number of candidate rG4-binding proteins and validated that G3BP1 can bind directly with rG4 structures and regulate the stabilities of mRNAs.
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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.