Proteasomal degradation of tau protein.

@article{David2002ProteasomalDO,
  title={Proteasomal degradation of tau protein.},
  author={Della C. David and Robert Layfield and Louise C. Serpell and Yolanda Narain and Michel Goedert and Maria Grazia Spillantini},
  journal={Journal of neurochemistry},
  year={2002},
  volume={83 1},
  pages={176-85}
}
Filamentous inclusions composed of the microtubule-associated protein tau are a defining characteristic of a large number of neurodegenerative diseases. Here we show that tau degradation in stably transfected and non-transfected SH-SY5Y cells is blocked by the irreversible proteasome inhibitor lactacystin. Further, we find that in vitro, natively unfolded tau can be directly processed by the 20S proteasome without a requirement for ubiquitylation, and that a highly reproducible pattern of… CONTINUE READING

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