Aplysia CPEB Can Form Prion-like Multimers in Sensory Neurons that Contribute to Long-Term Facilitation

  title={Aplysia CPEB Can Form Prion-like Multimers in Sensory Neurons that Contribute to Long-Term Facilitation},
  author={Kausik Si and Yun-Beom Choi and Erica White-Grindley and A. Majumdar and E. Kandel},
  • Kausik Si, Yun-Beom Choi, +2 authors E. Kandel
  • Published 2010
  • Biology, Medicine
  • Cell
  • Prions are proteins that can assume at least two distinct conformational states, one of which is dominant and self-perpetuating. Previously we found that a translation regulator CPEB from Aplysia, ApCPEB, that stabilizes activity-dependent changes in synaptic efficacy can display prion-like properties in yeast. Here we find that, when exogenously expressed in sensory neurons, ApCPEB can form an amyloidogenic self-sustaining multimer, consistent with it being a prion-like protein. In addition… CONTINUE READING
    315 Citations

    Figures and Topics from this paper

    The CPEB3 Protein Is a Functional Prion that Interacts with the Actin Cytoskeleton.
    • 77
    Synaptic plasticity: Polymerize and learn?
    • C. Bodo
    • Biology
    • Nature Reviews Neuroscience
    • 2010
    Protein-only mechanism induces self-perpetuating changes in the activity of neuronal Aplysia cytoplasmic polyadenylation element binding protein (CPEB)
    • 78
    • Highly Influenced
    • PDF
    Divergent CPEB prion-like domains reveal different assembly mechanisms for a generic amyloid-like fold
    • 4
    • Highly Influenced
    • PDF
    Critical Role of Amyloid-like Oligomers of Drosophila Orb2 in the Persistence of Memory
    • 207
    Functional Prions in the Brain.
    • 27
    • PDF


    A Neuronal Isoform of the Aplysia CPEB Has Prion-Like Properties
    • 509
    • PDF
    Dissection and Design of Yeast Prions
    • 178
    • PDF
    The utility of prions.
    • 56
    Rnq1: an epigenetic modifier of protein function in yeast.
    • 461
    • Highly Influential
    • PDF
    Oligopeptide repeats in the yeast protein Sup35p stabilize intermolecular prion interactions
    • 110
    • PDF
    Multiple Gln/Asn-Rich Prion Domains Confer Susceptibility to Induction of the Yeast [PSI+] Prion
    • 287
    • Highly Influential
    • PDF
    Prions as adaptive conduits of memory and inheritance
    • 476
    • PDF
    Amyloid aggregates of the HET-s prion protein are infectious
    • 257
    • PDF
    Aggregation of huntingtin in yeast varies with the length of the polyglutamine expansion and the expression of chaperone proteins.
    • S. Krobitsch, S. Lindquist
    • Biology, Medicine
    • Proceedings of the National Academy of Sciences of the United States of America
    • 2000
    • 494
    • PDF