The ubiquitin-like modifier FAT10 is degraded by the 20S proteasome in vitro but not in cellulo

Ubiquitin-independent protein degradation via the 20S proteasome without the 19S regulatory particle has gained increasing attention over the last years. The degradation of the ubiquitin-like modifier FAT10 by the 20S proteasome was investigated in this study. We found that FAT10 was rapidly degraded by purified 20S proteasomes in vitro, which was attributed to the weak folding of FAT10 and the N-terminally disordered tail. To confirm our results in cellulo, we established an inducible RNA interference system in which the AAA-ATPase Rpt2 of the 19S regulatory particle is knocked down to impair the function of the 26S proteasome. Using this system, degradation of FAT10 in cellulo was strongly dependent on functional 26S proteasome. Our data indicate that in vitro degradation studies with purified proteins do not necessarily reflect biological degradation mechanisms occurring in cells and, therefore, cautious data interpretation is required when 20S proteasome function is studied in vitro.

Fachgebiet (DDC)

570 Biowissenschaften, Biologie

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ISO 690

OLIVERI, Franziska, Steffen Johannes KELLER, Heike GOEBEL, Gerardo Omar ALVAREZ SALINAS, Michael BASLER, 2023. The ubiquitin-like modifier FAT10 is degraded by the 20S proteasome in vitro but not in cellulo. In: Life Science Alliance. Life Science Alliance, LLC. 6(6), e202201760. eISSN 2575-1077. Available under: doi: 10.26508/lsa.202201760

BibTex

@article{Oliveri2023-04-03ubiqu-66528,
  year={2023},
  doi={10.26508/lsa.202201760},
  title={The ubiquitin-like modifier FAT10 is degraded by the 20S proteasome in vitro but not in cellulo},
  number={6},
  volume={6},
  journal={Life Science Alliance},
  author={Oliveri, Franziska and Keller, Steffen Johannes and Goebel, Heike and Alvarez Salinas, Gerardo Omar and Basler, Michael},
  note={German Research Foundation Grant GR 1517/25-1 Article Number: e202201760}
}

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Kommentar zur Publikation

German Research Foundation Grant GR 1517/25-1

Begutachtet

Ja