The Role of Functional Prion-Like Proteins in the Persistence of Memory

  1. Eric R. Kandel3,4,5,6
  1. 1Stowers Institute for Medical Research, Kansas City, Missouri 64113
  2. 2Department of Physiology, School of Medicine, University of Kansas Medical Center, Kansas City, Kansas 66160
  3. 3Howard Hughes Medical Institute, Chevy Chase, Maryland 20815-6789
  4. 4Departments of Neuroscience and Psychiatry, College of Physicians and Surgeons of Columbia University, New York, New York 10027
  5. 5Zuckerman Mind Brain Behavior Institute, New York State Psychiatric Institute, New York, New York 10032
  6. 6Kavli Institute for Brain Sciences, New York, New York 10032
  1. Correspondence: ksi{at}stowers.org

Abstract

Prions are a self-templating amyloidogenic state of normal cellular proteins, such as prion protein (PrP). They have been identified as the pathogenic agents, contributing to a number of diseases of the nervous system. However, the discovery that the neuronal RNA-binding protein, cytoplasmic polyadenylation element-binding protein (CPEB), has a prion-like state that is involved in the stabilization of memory raised the possibility that prion-like proteins can serve normal physiological functions in the nervous system. Here, we review recent experimental evidence of prion-like properties of neuronal CPEB in various organisms and propose a model of how the prion-like state may stabilize memory.



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