@article{Aichem2018-08-20struc-43140,
  year={2018},
  doi={10.1038/s41467-018-05776-3},
  title={The structure of the ubiquitin-like modifier FAT10 reveals an alternative targeting mechanism for proteasomal degradation},
  volume={9},
  journal={Nature Communications},
  author={Aichem, Annette and Catone, Nicola and Berg, Andrej and Schwab, Ricarda and Scheuermann, Sophia and Bialas, Johanna and Schmidtke, Gunter and Peter, Christine and Gröttrup, Marcus and Wiesner, Silke},
  note={Author Correction zu diesem Artikel: https://doi.org/10.1038/s41467-018-07183-0 Article Number: 3321}
}

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    <dcterms:abstract xml:lang="eng">FAT10 is a ubiquitin-like modifier that directly targets proteins for proteasomal degradation. Here, we report the high-resolution structures of the two individual ubiquitin-like domains (UBD) of FAT10 that are joined by a flexible linker. While the UBDs of FAT10 show the typical ubiquitin-fold, their surfaces are entirely different from each other and from ubiquitin explaining their unique binding specificities. Deletion of the linker abrogates FAT10-conjugation while its mutation blocks auto-FAT10ylation of the FAT10-conjugating enzyme USE1 but not bulk conjugate formation. FAT10- but not ubiquitin-mediated degradation is independent of the segregase VCP/p97 in the presence but not the absence of FAT10's unstructured N-terminal heptapeptide. Stabilization of the FAT10 UBDs strongly decelerates degradation suggesting that the intrinsic instability of FAT10 together with its disordered N-terminus enables the rapid, joint degradation of FAT10 and its substrates without the need for FAT10 de-conjugation and partial substrate unfolding.</dcterms:abstract>
    <dc:rights>Attribution 4.0 International</dc:rights>
    <dc:creator>Schmidtke, Gunter</dc:creator>
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    <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2018-08-28T14:56:38Z</dc:date>
    <dc:contributor>Schwab, Ricarda</dc:contributor>
    <dc:contributor>Catone, Nicola</dc:contributor>
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    <dc:creator>Catone, Nicola</dc:creator>
    <dc:creator>Peter, Christine</dc:creator>
    <dc:creator>Berg, Andrej</dc:creator>
    <dc:contributor>Peter, Christine</dc:contributor>
    <dc:creator>Scheuermann, Sophia</dc:creator>
    <dc:contributor>Gröttrup, Marcus</dc:contributor>
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    <dc:contributor>Wiesner, Silke</dc:contributor>
    <dc:creator>Aichem, Annette</dc:creator>
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    <dc:contributor>Schmidtke, Gunter</dc:contributor>
    <dc:creator>Bialas, Johanna</dc:creator>
    <dc:creator>Wiesner, Silke</dc:creator>
    <dc:creator>Gröttrup, Marcus</dc:creator>
    <dc:contributor>Berg, Andrej</dc:contributor>
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    <dc:contributor>Aichem, Annette</dc:contributor>
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    <dcterms:title>The structure of the ubiquitin-like modifier FAT10 reveals an alternative targeting mechanism for proteasomal degradation</dcterms:title>
    <dc:contributor>Scheuermann, Sophia</dc:contributor>
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    <dcterms:issued>2018-08-20</dcterms:issued>
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