A neuronal isoform of the aplysia CPEB has prion-like properties

Cell. 2003 Dec 26;115(7):879-91. doi: 10.1016/s0092-8674(03)01020-1.


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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Aplysia
  • Glutamine / metabolism
  • Memory / physiology
  • Neuronal Plasticity / physiology
  • Neurons / metabolism*
  • Prions / genetics
  • Prions / metabolism*
  • Protein Biosynthesis / physiology*
  • Protein Conformation
  • Protein Folding
  • Protein Isoforms / genetics
  • Protein Isoforms / metabolism
  • Protein Structure, Tertiary / physiology
  • RNA, Messenger / metabolism
  • Saccharomyces cerevisiae
  • Synaptic Transmission / physiology
  • Transcription Factors / genetics
  • Transcription Factors / metabolism*
  • Xenopus Proteins / genetics
  • Xenopus Proteins / metabolism*
  • mRNA Cleavage and Polyadenylation Factors


  • Cpeb1 protein, Xenopus
  • Prions
  • Protein Isoforms
  • RNA, Messenger
  • Transcription Factors
  • Xenopus Proteins
  • mRNA Cleavage and Polyadenylation Factors
  • Glutamine