ArticleProceedings of the National Academy of Sciences of the United States of America2020
Exploring the F-actin/CPEB3 interaction and its possible role in the molecular mechanism of long-term memory.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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11 citing papers in PubMed, 19 citations in OpenAlex.
- Ondansetron reduces seizures and improves cognitive impairment in a rat model of temporal lobe epilepsy.IBRO neuroscience reports · 2026Article
- 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
- Frustration in physiology and molecular medicine.Molecular aspects of medicine · 2025Review
- Generating the polymorph landscapes of amyloid fibrils using AI: RibbonFold.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- SUMOylation balance: a key determinant in synapse physiology.Frontiers in physiology · 2025Review
- DEHP-Induced Glioblastoma in Zebrafish Is Associated with Circadian Dysregulation of PER3.Toxics · 2024Article
- Review
- Inhibition ofeLife · 2024Article
- A structural dynamics model for how CPEB3 binding to SUMO2 can regulate translational control in dendritic spines.PLoS computational biology · 2022Article
- Vectorial channeling as a mechanism for translational control by functional prions and condensates.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
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Authors and funding
7 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Dendritic spines are tiny membranous protrusions on the dendrites of neurons. Dendritic spines change shape in response to input signals, thereby strengthening the connections between neurons. The growth and stabilization of dendritic spines is thought to be essential for maintaining long-term memory. Actin cytoskeleton remodeling in spines is a key element of their formation and growth. More speculatively, the aggregation of CPEB3, a functional prion that binds RNA, has been reported to be involved in the maintenance of long-term memory. Here we study the interaction between actin and CPEB3 and propose a molecular model for the complex structure of CPEB3 and an actin filament (F-actin). The results of our computational modeling, including both energetic and structural analyses, are compared with novel data from peptide array experiments. Our model of the CPEB3/F-actin interaction suggests that F-actin potentially triggers the aggregation-prone structural transition of a short CPEB3 sequence by zipping it into a beta-hairpin form. We also propose that the CPEB3/F-actin interaction might be regulated by the SUMOylation of CPEB3, based on bioinformatic searches for potential SUMOylation sites as well as SUMO interacting motifs in CPEB3. On the basis of these results and the existing literature, we put forward a possible molecular mechanism underlying long-term memory that involves CPEB3's binding to actin, its aggregation, and its regulation by SUMOylation.
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