A neuronal isoform of the aplysia CPEB has prion-like properties
- PMID: 14697205
- DOI: 10.1016/s0092-8674(03)01020-1
A neuronal isoform of the aplysia CPEB has prion-like properties
Abstract
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.
Comment in
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Memory, synaptic translation, and...prions?Cell. 2003 Dec 26;115(7):767-8. doi: 10.1016/s0092-8674(03)01022-5. Cell. 2003. PMID: 14697195
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