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
Celljournal_title
Cellauthors
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 Kdoi
10.1016/j.cell.2012.01.004subject
Has Abstractpub_date
2012-02-03 00:00:00pages
515-29issue
3eissn
0092-8674issn
1097-4172pii
S0092-8674(12)00005-0journal_volume
148pub_type
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