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Cited by 294

The DOI matches its Crossref record; 32 of the 32 references it cites were found in a registry or an index.

Wild-type PrP and a mutant associated with prion disease are subject to retrograde transport and proteasome degradation

Open access
Ma, Jiyan, Lindquist, Susan·2001·Proceedings of the National Academy of Sciences
DOI 10.1073/pnas.011578098
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Abstract

The cytoplasm seems to provide an environment that favors conversion of the prion protein (PrP) to a form with the physical characteristics of the PrP Sc conformation, which is associated with transmissible spongiform encephalopathies. However, it is not clear whether PrP would ever exist in the cytoplasm under normal circumstances. We report that PrP accumulates in the cytoplasm when proteasome activity is compromised. The accumulated PrP seems to have been subjected to the normal proteolytic cleavage events associated with N- and C-terminal processing in the endoplasmic reticulum, suggesting that it arrives in the cytoplasm through retrograde transport. In the cytoplasm, PrP forms aggregates, often in association with Hsc70. With prolonged incubation, these aggregates accumulate in an “aggresome”-like state, surrounding the centrosome. A mutant (D177N), which is associated with a heritable and transmissible form of the spongiform encephalopathies, is less efficiently trafficked to the surface than wild-type PrP and accumulates in the cytoplasm even without proteasome inhibition. These results demonstrate that PrP can accumulate in the cytoplasm and is likely to enter this compartment through normal protein quality-control pathways. Its potential to accumulate in the cytoplasm has implications for pathogenesis.

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Metadata

Authors
Ma, J., & Lindquist, S.
Venue
Proceedings of the National Academy of Sciences
Publisher
Proceedings of the National Academy of Sciences
Published
2001-12-11
Volume
98
Issue
26
Pages
14955-14960
ISSN
  • 0027-8424 (ISSN-L)
  • 1091-6490
DOI
10.1073/pnas.011578098
OpenAlex
W2077672823
Cited by
294
References
32
FWCI
8.69
Type
journal article
Language
en
Open access
green

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CoChat. (2026). Citation check: Wild-type PrP and a mutant associated with prion disease are subject to retrograde transport and proteasome degradation. https://app.cochat.ai/papers/10.1073/pnas.011578098
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Ma, J., & Lindquist, S. (2001). Wild-type PrP and a mutant associated with prion disease are subject to retrograde transport and proteasome degradation. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.011578098

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