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prions may function in memory



The article below  suggests that prions, related to mad cow disease
protein, may function in memory.
Cell, Vol 115, 879-891, 26 December 2003

A Neuronal Isoform of the Aplysia CPEB Has Prion-Like Properties
Kausik Si , Susan Lindquist , and Eric R. Kandel

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.

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