A Neuronal Isoform of the Aplysia CPEB Has Prion-Like Properties

426Citations
Citations of this article
468Readers
Mendeley users who have this article in their library.

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.

Cite

CITATION STYLE

APA

Si, K., Lindquist, S., & Kandel, E. R. (2003). A Neuronal Isoform of the Aplysia CPEB Has Prion-Like Properties. Cell, 115(7), 879–891. https://doi.org/10.1016/S0092-8674(03)01020-1

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free