ArticleNature chemical biology2023
Gelation of cytoplasmic expanded CAG RNA repeats suppresses global protein synthesis.
Article in Nature chemical biology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
What it found
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Who cites it
12 citing papers in PubMed, 20 citations in OpenAlex.
- RMRP mediates neuroprotection as a downstream effector of RBM3 in human neuroblastoma SH-SY5Y cells.Molecular genetics and genomics : MGG · 2026Article
- Programmable and Switchable RNA Scaffolds for Synthetic Condensate Engineering in Mammalian Cells.bioRxiv : the preprint server for biology · 2026Article
- Nucleolar aggregation of key neuropathological proteins in the postmortem neurodegenerative brain.Acta neuropathologica · 2025Article
- DHX8 regulates degradation of RNA by RNautophagy.Nucleic acids research · 2025Article
- Membraneless organelles in health and disease: exploring the molecular basis, physiological roles and pathological implications.Signal transduction and targeted therapy · 2024Review
- Regulation ofInternational journal of molecular sciences · 2024Review
- Fluctuations in Medium Viscosity May Affect the Stability of the CAG Tract in theBiomedicines · 2024Article
- Biomolecular condensates and disease pathogenesis.Science China. Life sciences · 2024Review
- Crosstalk between protein post-translational modifications and phase separation.Cell communication and signaling : CCS · 2024Review
- Phase transition and lysosomal degradation of expanded CAG repeat RNA suppress global protein synthesis.Autophagy · 2024Article
- Non-Coding RNA Performs Its Biological Function by Interacting with Macromolecules.International journal of molecular sciences · 2023Article
- RNA repeats stall translation.Nature chemical biology · 2023Article
Corrections and comments
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Authors and funding
11 authors at 4 institutions in 2 countries.
Funding
Abstract
RNA molecules with the expanded CAG repeat (eCAGr) may undergo sol-gel phase transitions, but the functional impact of RNA gelation is completely unknown. Here, we demonstrate that the eCAGr RNA may form cytoplasmic gel-like foci that are rapidly degraded by lysosomes. These RNA foci may significantly reduce the global protein synthesis rate, possibly by sequestering the translation elongation factor eEF2. Disrupting the eCAGr RNA gelation restored the global protein synthesis rate, whereas enhanced gelation exacerbated this phenotype. eEF2 puncta were significantly enhanced in brain slices from a knock-in mouse model and from patients with Huntington's disease, which is a CAG expansion disorder expressing eCAGr RNA. Finally, neuronal expression of the eCAGr RNA by adeno-associated virus injection caused significant behavioral deficits in mice. Our study demonstrates the existence of RNA gelation inside the cells and reveals its functional impact, providing insights into repeat expansion diseases and functional impacts of RNA phase transition.
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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.