Degradation of FAT10 by the 26S proteasome is independent of ubiquitylation but relies on NUB1L.

@article{Schmidtke2009DegradationOF,
  title={Degradation of FAT10 by the 26S proteasome is independent of ubiquitylation but relies on NUB1L.},
  author={Gunter Schmidtke and Birte Kalveram and Marcus Groettrup},
  journal={FEBS letters},
  year={2009},
  volume={583 3},
  pages={591-4}
}
The ubiquitin-like modifier FAT10 targets proteins for degradation by the proteasome, a process accelerated by the UBL-UBA domain protein NEDD8 ultimate buster 1-long. Here, we show that FAT10-mediated degradation occurs independently of poly-ubiquitylation as purified 26S proteasome readily degraded FAT10-dihydrofolate reductase (DHFR) but not ubiquitin-DHFR in vitro. Interestingly, the 26S proteasome could only degrade FAT10-DHFR when NUB1L was present. Knock-down of NUB1L attenuated the… CONTINUE READING

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