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 Amitabha Majumdar and Eric R. Kandel},
  journal={Cell},
  year={2010},
  volume={140},
  pages={421-435}
}

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References

SHOWING 1-10 OF 52 REFERENCES

A Neuronal Isoform of the Aplysia CPEB Has Prion-Like Properties

Dissection and Design of Yeast Prions

Novel artificial prions are designed by fusing the replication element of Sup35p to aggregation-prone sequences from other proteins, including pathogenically expanded polyglutamine, to explain why although Q/N-rich proteins are relatively common, few form heritable aggregates.

The utility of prions.

Rnq1: an epigenetic modifier of protein function in yeast.

Oligopeptide repeats in the yeast protein Sup35p stabilize intermolecular prion interactions

It is shown that a human PrP repeat (PHGGGWGQ) is able functionally to replace a Sup35p oligopeptide repeat to allow stable [PSI+] propagation in vivo and there appears to be evolutionary conservation of function of the N‐terminally located oligopePTide repeats in prion propagation.

Prions as adaptive conduits of memory and inheritance

Changes in protein conformation drive most biological processes, but none have seized the imagination of scientists and the public alike as have the self-replicating conformations of prions. Prions

Amyloid aggregates of the HET-s prion protein are infectious

It is shown that biolistic introduction of aggregated recombinant HET-s protein into fungal cells induces emergence of the [Het-s] prion with a high frequency, demonstrating that prion infectivity can be created de novo, in vitro from recombinant protein in this system.

Aggregation of huntingtin in yeast varies with the length of the polyglutamine expansion and the expression of chaperone proteins.

Yeast is established as a system for studying the causes and consequences of polyQ-dependent Ht aggregation, suggesting that the ubiquitination of Ht previously noted in mammalian cells may not inherently be required for polyQ length-dependent aggregation.
...