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Cell December 26, 2003; 115 (7): 879-91.
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A neuronal isoform of the aplysia CPEB has prion-like properties.

Si K , Lindquist S , Kandel ER .

Prion proteins have the unusual capacity to fold into two functionally distinct conformations, one of which is self-perpetuating. When yeast prion proteins switch state, they produce heritable phenotypes. We report prion-like properties in a neuronal member of the CPEB family (cytoplasmic polyadenylation element binding protein), which regulates mRNA translation. Compared to other CPEB family members, the neuronal protein has an N-terminal extension that shares characteristics of yeast prion-determinants: a high glutamine content and predicted conformational flexibility. When fused to a reporter protein in yeast, this region confers upon it the epigenetic changes in state that characterize yeast prions. Full-length CPEB undergoes similar changes, but surprisingly it is the dominant, self-perpetuating prion-like form that has the greatest capacity to stimulate translation of CPEB-regulated mRNA. We hypothesize that conversion of CPEB to a prion-like state in stimulated synapses helps to maintain long-term synaptic changes associated with memory storage.

PubMed ID: 14697205
Article link: Cell

Species referenced: Xenopus
Genes referenced: cpeb1 prnp

References :
Darnell, Memory, synaptic translation, and...prions? 2003, Pubmed, Xenbase