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TitleStructural insights into functional regulation of the human CPEB3 prion by an amyloid-forming segment.
Journal, issue, pagesStructure, Vol. 33, Issue 8, Page 1314-11324.e5, Year 2025
Publish dateAug 7, 2025
AuthorsMaria D Flores / Michael R Sawaya / David R Boyer / Samantha Zink / Susanna Tovmasyan / Adrian Saucedo / Logan S Richards / Chih-Te Zee / Jorge Cardenas / Luana Fioriti / Jose A Rodriguez /
PubMed AbstractThe 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 ...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.
External linksStructure / PubMed:40480223
MethodsEM (helical sym.)
Resolution3.0 Å
Structure data

40677

8spa

EMDB-40677, PDB-8spa:
Structural insights into cellular control of the human CPEB3 prion, functionally regulated by a labile-amyloid-forming segment
Method: EM (helical sym.) / Resolution: 3.0 Å

Source
  • homo sapiens (human)
KeywordsPROTEIN FIBRIL / prion / amyloid / reversible / helical

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