ArticleProceedings of the National Academy of Sciences of the United States of America2019
CPEB3 inhibits translation of mRNA targets by localizing them to P bodies.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.
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Who cites it
49 citing papers in PubMed, 95 citations in OpenAlex.
- An Anti-Amyloidogenic Approach to Specifically Block Memory Consolidation in Mice for Therapeutic Intervention.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Functional amyloids as molecular switches: emerging roles in diverse signalling pathways.Biochemical Society transactions · 2026Review
- The Effect of Protein Tagging on Aggregation and Phase Separation.Journal of cellular biochemistry · 2026Review
- The dynamic and heterogeneous composition of biomolecular condensates and its functional relevance.Nature reviews. Molecular cell biology · 2026Review
- Reshaping cancer cell plasticity by P-body dynamics and protein translation.Communications biology · 2026Review
- Multiplexed smFISH Reveals the Spatial Organization of Neuropil Localized mRNAs Is Linked to Abundance.eNeuro · 2025Article
- RNA Granules at the Crossroads of Synaptic Dysfunction and Neurodegeneration.Journal of neurochemistry · 2025Review
- Role of CPEBs in Learning and Memory.Journal of neurochemistry · 2025Review
- Structural insights into functional regulation of the human CPEB3 prion by an amyloid-forming segment.Structure (London, England : 1993) · 2025Article
- FTO-mediated mClinical and translational medicine · 2025Article
- Divergent evolution of low-complexity regions in the vertebrate CPEB protein family.Frontiers in bioinformatics · 2025Article
- Non-redundant roles for the human mRNA decapping cofactor paralogs DCP1a and DCP1b.Life science alliance · 2024Article
- Active regulation of amyloidosis.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Orb2 enables rare-codon-enriched mRNA expression during Drosophila neuron differentiation.Nature communications · 2024Article
- Review
- RNA target highlights in CASP15: Evaluation of predicted models by structure providers.Proteins · 2023Article
- Mass Spectrometry of RNA-Binding Proteins during Liquid-Liquid Phase Separation Reveals Distinct Assembly Mechanisms and Droplet Architectures.Journal of the American Chemical Society · 2023Article
- CPEB3 low-complexity motif regulates local protein synthesis via protein-protein interactions in neuronal ribonucleoprotein granules.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- A structural dynamics model for how CPEB3 binding to SUMO2 can regulate translational control in dendritic spines.PLoS computational biology · 2022Article
- CPEB3 suppresses gastric cancer progression by inhibiting ADAR1-mediated RNA editing via localizing ADAR1 mRNA to P bodies.Oncogene · 2022Article
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Authors and funding
4 authors at 3 institutions in 2 countries.
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Abstract
Protein synthesis is crucial for the maintenance of long-term memory-related synaptic plasticity. The cytoplasmic polyadenylation element-binding protein 3 (CPEB3) regulates the translation of several mRNAs important for long-term synaptic plasticity in the hippocampus. In previous studies, we found that the oligomerization and activity of CPEB3 are controlled by small ubiquitin-like modifier (SUMO)ylation. In the basal state, CPEB3 is SUMOylated; it is soluble and acts as a repressor of translation. Following neuronal stimulation, CPEB3 is de-SUMOylated; it now forms oligomers that are converted into an active form that promotes the translation of target mRNAs. To better understand how CPEB3 regulates the translation of its mRNA targets, we have examined CPEB3 subcellular localization. We found that basal, repressive CPEB3 is localized to membraneless cytoplasmic processing bodies (P bodies), subcellular compartments that are enriched in translationally repressed mRNA. This basal state is affected by the SUMOylation state of CPEB3. After stimulation, CPEB3 is recruited into polysomes, thus promoting the translation of its target mRNAs. Interestingly, when we examined CPEB3 recombinant protein in vitro, we found that CPEB3 phase separates when SUMOylated and binds to a specific mRNA target. These findings suggest a model whereby SUMO regulates the distribution, oligomerization, and activity of oligomeric CPEB3, a critical player in the persistence of memory.
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