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- Publisher Website: 10.1126/science.aba3526
- Scopus: eid_2-s2.0-85081885950
- PMID: 32165583
- WOS: WOS:000520023800038
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Article: Cryo-EM structure of a neuronal functional amyloid implicated in memory persistence in Drosophila
Title | Cryo-EM structure of a neuronal functional amyloid implicated in memory persistence in Drosophila |
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Authors | |
Issue Date | 2020 |
Citation | Science, 2020, v. 367, n. 6483, p. 1230-1234 How to Cite? |
Abstract | How long-lived memories withstand molecular turnover is a fundamental question. Aggregates of a prion-like RNA-binding protein, cytoplasmic polyadenylation element-binding (CPEB) protein, is a putative substrate of long-lasting memories. We isolated aggregated Drosophila CPEB, Orb2, from adult heads and determined its activity and atomic structure, at 2.6-angstrom resolution, using cryo-electron microscopy. Orb2 formed ∼75-nanometer-long threefold-symmetric amyloid filaments. Filament formation transformed Orb2 from a translation repressor to an activator and "seed" for further translationally active aggregation. The 31-amino acid protofilament core adopted a cross-b unit with a single hydrophilic hairpin stabilized through interdigitated glutamine packing. Unlike the hydrophobic core of pathogenic amyloids, the hydrophilic core of Orb2 filaments suggests how some neuronal amyloids could be a stable yet regulatable substrate ofmemory. |
Persistent Identifier | http://hdl.handle.net/10722/299618 |
ISSN | 2023 Impact Factor: 44.7 2023 SCImago Journal Rankings: 11.902 |
PubMed Central ID | |
ISI Accession Number ID |
DC Field | Value | Language |
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dc.contributor.author | Hervas, Ruben | - |
dc.contributor.author | Rau, Michael J. | - |
dc.contributor.author | Park, Younshim | - |
dc.contributor.author | Zhang, Wenjuan | - |
dc.contributor.author | Murzin, Alexey G. | - |
dc.contributor.author | Fitzpatrick, James A.J. | - |
dc.contributor.author | Scheres, Sjors H.W. | - |
dc.contributor.author | Si, Kausik | - |
dc.date.accessioned | 2021-05-21T03:34:48Z | - |
dc.date.available | 2021-05-21T03:34:48Z | - |
dc.date.issued | 2020 | - |
dc.identifier.citation | Science, 2020, v. 367, n. 6483, p. 1230-1234 | - |
dc.identifier.issn | 0036-8075 | - |
dc.identifier.uri | http://hdl.handle.net/10722/299618 | - |
dc.description.abstract | How long-lived memories withstand molecular turnover is a fundamental question. Aggregates of a prion-like RNA-binding protein, cytoplasmic polyadenylation element-binding (CPEB) protein, is a putative substrate of long-lasting memories. We isolated aggregated Drosophila CPEB, Orb2, from adult heads and determined its activity and atomic structure, at 2.6-angstrom resolution, using cryo-electron microscopy. Orb2 formed ∼75-nanometer-long threefold-symmetric amyloid filaments. Filament formation transformed Orb2 from a translation repressor to an activator and "seed" for further translationally active aggregation. The 31-amino acid protofilament core adopted a cross-b unit with a single hydrophilic hairpin stabilized through interdigitated glutamine packing. Unlike the hydrophobic core of pathogenic amyloids, the hydrophilic core of Orb2 filaments suggests how some neuronal amyloids could be a stable yet regulatable substrate ofmemory. | - |
dc.language | eng | - |
dc.relation.ispartof | Science | - |
dc.title | Cryo-EM structure of a neuronal functional amyloid implicated in memory persistence in Drosophila | - |
dc.type | Article | - |
dc.description.nature | link_to_OA_fulltext | - |
dc.identifier.doi | 10.1126/science.aba3526 | - |
dc.identifier.pmid | 32165583 | - |
dc.identifier.pmcid | PMC7182444 | - |
dc.identifier.scopus | eid_2-s2.0-85081885950 | - |
dc.identifier.volume | 367 | - |
dc.identifier.issue | 6483 | - |
dc.identifier.spage | 1230 | - |
dc.identifier.epage | 1234 | - |
dc.identifier.eissn | 1095-9203 | - |
dc.identifier.isi | WOS:000520023800038 | - |