Evidence map›Paper›PMID 40480223›Full record

ArticleStructure (London, England : 1993)2025

Structural insights into functional regulation of the human CPEB3 prion by an amyloid-forming segment.

Maria D Flores, Michael R Sawaya, David R Boyer, Samantha Zink, Susanna Tovmasyan, Adrian Saucedo, Logan S Richards, Chih-Te Zee, Jorge Cardenas, Luana Fioriti and 1 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Structure (London, England : 1993), 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed, 1 pooled it
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

4 citing papers in PubMed, 1 synthesis or guideline pooled it.

  1. Pooled it
  2. Article
  3. Review
  4. Role of CPEBs in Learning and Memory.Journal of neurochemistry · 2025
    Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

11 authors.

Maria D FloresDepartment of Chemistry and Biochemistry, UCLA-DOE Institute for Genomics and Proteomics, STROBE, NSF Science and Technology Center, University of California, Los Angeles (UCLA), Los Angeles, CA 90095, USA. Electronic address: mflores@mbi.ucla.edu.
Michael R SawayaDepartment of Biological Chemistry and Department of Chemistry and Biochemistry, University of California, Los Angeles (UCLA), Howard Hughes Medical Institute (HHMI), UCLA-DOE Institute for Genomics and Proteomics, Los Angeles, CA 90095, USA.
David R BoyerDepartment of Biological Chemistry and Department of Chemistry and Biochemistry, University of California, Los Angeles (UCLA), Howard Hughes Medical Institute (HHMI), UCLA-DOE Institute for Genomics and Proteomics, Los Angeles, CA 90095, USA.
Samantha ZinkDepartment of Chemistry and Biochemistry, UCLA-DOE Institute for Genomics and Proteomics, STROBE, NSF Science and Technology Center, University of California, Los Angeles (UCLA), Los Angeles, CA 90095, USA.
Susanna TovmasyanDepartment of Chemistry and Biochemistry, UCLA-DOE Institute for Genomics and Proteomics, STROBE, NSF Science and Technology Center, University of California, Los Angeles (UCLA), Los Angeles, CA 90095, USA.
Adrian SaucedoDepartment of Chemistry and Biochemistry, UCLA-DOE Institute for Genomics and Proteomics, STROBE, NSF Science and Technology Center, University of California, Los Angeles (UCLA), Los Angeles, CA 90095, USA.
Logan S RichardsDepartment of Chemistry and Biochemistry, UCLA-DOE Institute for Genomics and Proteomics, STROBE, NSF Science and Technology Center, University of California, Los Angeles (UCLA), Los Angeles, CA 90095, USA.
Chih-Te ZeeDepartment of Chemistry and Biochemistry, UCLA-DOE Institute for Genomics and Proteomics, STROBE, NSF Science and Technology Center, University of California, Los Angeles (UCLA), Los Angeles, CA 90095, USA.
Jorge CardenasDepartment of Chemistry and Biochemistry, UCLA-DOE Institute for Genomics and Proteomics, STROBE, NSF Science and Technology Center, University of California, Los Angeles (UCLA), Los Angeles, CA 90095, USA.
Luana FioritiDepartment of Neuroscience, Istituto di Ricerche Farmacologiche Mario Negri, IRCCS, 20156 Milano MI, Italy; Department of Neuroscience, Columbia University, New York, NY 10027, USA. Electronic address: luana.fioriti@marionegri.it.
Jose A RodriguezDepartment of Chemistry and Biochemistry, UCLA-DOE Institute for Genomics and Proteomics, STROBE, NSF Science and Technology Center, University of California, Los Angeles (UCLA), Los Angeles, CA 90095, USA. Electronic address: jrodriguez@mbi.ucla.edu.

Funding

Micro Electron Diffraction of Toxic and/or Infectious Macromolecular NanoassembliesR35GM128867 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI Jose Alfonso Rodriguez · 2018 to 2026
$3.1M
NIGMS NIH HHS R35 GM128867
6 · The paper itself

Abstract

The cytoplasmic polyadenylation-element-binding-protein-3 (CPEB3) is a functional prion thought to modulate protein synthesis and enable consolidation of long-term memory in neurons. We report a cryoelectron microscopy (cryo-EM) structure of amyloid fibrils grown in vitro from the first prion-like domain of human CPEB3 (hCPEB3), revealing their ordered 49-residue core, spanning L103 to F151. CPEB3 lacking that segment coalesces into abnormal puncta in cells compared to wild-type CPEB3, localizes away from dormant p-bodies and toward stress granules, and lacks the ability to influence protein synthesis in neurons. Fluorescence-guided cryo-focused ion beam (cryo-FIB) milling and cryo-electron tomography (cryo-ET) applied to neuronal cells expressing CPEB3 reveal CPEB3-GFP signal from lamellae enriched in multivesicular bodies (MVBs), cavernous multilamellar compartments, and bundled filaments, suggesting a state of induced cellular stress. Accordingly, cells expressing wild-type CPEB3 are less viable than those expressing CPEB3 without its amyloid core, suggesting human CPEB3 regulation may be required to overcome the liability associated with its self-assembly in cells.

Indexed as

AmyloidPrionsRNA-Binding ProteinsCryoelectron MicroscopyHumansModels, MolecularNeuronsProtein DomainsAmyloidCPEB3 protein, humanPrionsRNA-Binding Proteinsamyloidcryo-emfibrilsgranulesmemorypriontomographytranslation

Identifiers

PMID40480223
PMCPMC13344147

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

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.