Since their discovery in 1982, prions have been mostly associated with deadly and devastating neurodegenerative disorders—notably variant Creutzfeld-Jakob disease and bovine spongiform encephalopathy. Nevertheless, some maintain that the mechanism by which prions change their shape and aggregate might be put to good use in biological systems. In back-to-back papers in the December 26 issue of
Susan Lindquist, director of the Whitehead Institute, and Eric Kandel, professor of physiology and psychiatry at Columbia University College of Physicians and Surgeons, describe a protein, cytoplasmic polyadenylation element-binding protein (CPEB), which appears to mark active synapses. The protein behaves like a prion in yeast cultures, and its alternative self-perpetuating form—generally associated with disease states for other prions—appears to be the protein's active form.
Researchers, in looking to understand memory formation, have struggled to comprehend how a neuron can strengthen specific synapses ...
