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

@article{Si2010AplysiaCC,
  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},
  journal={Cell},
  year={2010},
  volume={140},
  pages={421-435}
}
  • 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
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    References

    SHOWING 1-10 OF 58 REFERENCES
    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