The structure of the ubiquitin-like modifier FAT10 reveals an alternative targeting mechanism for proteasomal degradation

The structure of the ubiquitin-like modifier FAT10 reveals an alternative targeting mechanism for proteasomal degradation

The ubiquitin-like modifier FAT10 is composed of two ubiquitin-like domains (UBDs). Here the authors present the FAT10 UBD structures and show that the unstructured FAT10 N-terminal heptapeptide together with the poor stability of FAT10 facilitate the rapid proteasomal targeting of FAT10 along with...

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Bibliographic Details
Main Authors: Annette Aichem, Samira Anders, Nicola Catone, Philip Rößler, Sophie Stotz, Andrej Berg, Ricarda Schwab, Sophia Scheuermann, Johanna Bialas, Mira C. Schütz-Stoffregen, Gunter Schmidtke, Christine Peter, Marcus Groettrup, Silke Wiesner
Format: Article
Language:English
Published: Nature Publishing Group 2018-08-01
Series:Nature Communications
Online Access:https://doi.org/10.1038/s41467-018-05776-3

Internet

https://doi.org/10.1038/s41467-018-05776-3

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