Critical role of amyloid-like oligomers of Drosophila Orb2 in the persistence of memory.

Abstract:

:A long-standing question in the study of long-term memory is how a memory trace persists for years when the proteins that initiated the process turn over and disappear within days. Previously, we postulated that self-sustaining amyloidogenic oligomers of cytoplasmic polyadenylation element-binding protein (CPEB) provide a mechanism for the maintenance of activity-dependent synaptic changes and, thus, the persistence of memory. Here, we found that the Drosophila CPEB Orb2 forms amyloid-like oligomers, and oligomers are enriched in the synaptic membrane fraction. Of the two protein isoforms of Orb2, the amyloid-like oligomer formation is dependent on the Orb2A form. A point mutation in the prion-like domain of Orb2A, which reduced amyloid-like oligomerization of Orb2, did not interfere with learning or memory persisting up to 24 hr. However the mutant flies failed to stabilize memory beyond 48 hr. These results support the idea that amyloid-like oligomers of neuronal CPEB are critical for the persistence of long-term memory.

journal_name

Cell

journal_title

Cell

authors

Majumdar A,Cesario WC,White-Grindley E,Jiang H,Ren F,Khan MR,Li L,Choi EM,Kannan K,Guo F,Unruh J,Slaughter B,Si K

doi

10.1016/j.cell.2012.01.004

subject

Has Abstract

pub_date

2012-02-03 00:00:00

pages

515-29

issue

3

eissn

0092-8674

issn

1097-4172

pii

S0092-8674(12)00005-0

journal_volume

148

pub_type

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