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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

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AICHEM, Annette, Nicola CATONE, Andrej BERG, Ricarda SCHWAB, Sophia SCHEUERMANN, Johanna BIALAS, Gunter SCHMIDTKE, Christine PETER, Marcus GROETTRUP, Silke WIESNER, 2018. The structure of the ubiquitin-like modifier FAT10 reveals an alternative targeting mechanism for proteasomal degradation. In: Nature Communications. 9, 3321. eISSN 2041-1723. Available under: doi: 10.1038/s41467-018-05776-3

@article{Aichem2018-08-20struc-43140, title={The structure of the ubiquitin-like modifier FAT10 reveals an alternative targeting mechanism for proteasomal degradation}, year={2018}, doi={10.1038/s41467-018-05776-3}, 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 Groettrup, Marcus and Wiesner, Silke}, note={Author Correction zu diesem Artikel: https://doi.org/10.1038/s41467-018-07183-0 Article Number: 3321} }

<rdf:RDF xmlns:dcterms="http://purl.org/dc/terms/" xmlns:dc="http://purl.org/dc/elements/1.1/" xmlns:rdf="http://www.w3.org/1999/02/22-rdf-syntax-ns#" xmlns:bibo="http://purl.org/ontology/bibo/" xmlns:dspace="http://digital-repositories.org/ontologies/dspace/0.1.0#" xmlns:foaf="http://xmlns.com/foaf/0.1/" xmlns:void="http://rdfs.org/ns/void#" xmlns:xsd="http://www.w3.org/2001/XMLSchema#" > <rdf:Description rdf:about="https://kops.uni-konstanz.de/rdf/resource/123456789/43140"> <dc:language>eng</dc:language> <dc:contributor>Bialas, Johanna</dc:contributor> <dc:creator>Wiesner, Silke</dc:creator> <dcterms:hasPart rdf:resource="https://kops.uni-konstanz.de/bitstream/123456789/43140/1/Aichem_2-1osbbqsz3ua1.pdf"/> <dc:contributor>Berg, Andrej</dc:contributor> <dc:creator>Bialas, Johanna</dc:creator> <dcterms:isPartOf rdf:resource="https://kops.uni-konstanz.de/rdf/resource/123456789/29"/> <dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2018-08-28T14:56:38Z</dcterms:available> <dcterms:isPartOf rdf:resource="https://kops.uni-konstanz.de/rdf/resource/123456789/28"/> <dc:contributor>Peter, Christine</dc:contributor> <dspace:isPartOfCollection rdf:resource="https://kops.uni-konstanz.de/rdf/resource/123456789/29"/> <dc:creator>Catone, Nicola</dc:creator> <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2018-08-28T14:56:38Z</dc:date> <void:sparqlEndpoint rdf:resource="http://localhost/fuseki/dspace/sparql"/> <dc:contributor>Schmidtke, Gunter</dc:contributor> <dc:creator>Groettrup, Marcus</dc:creator> <dc:creator>Berg, Andrej</dc:creator> <dc:contributor>Groettrup, Marcus</dc:contributor> <dc:creator>Aichem, Annette</dc:creator> <bibo:uri rdf:resource="https://kops.uni-konstanz.de/handle/123456789/43140"/> <dc:contributor>Wiesner, Silke</dc:contributor> <dc:contributor>Aichem, Annette</dc:contributor> <dc:contributor>Catone, Nicola</dc:contributor> <dspace:hasBitstream rdf:resource="https://kops.uni-konstanz.de/bitstream/123456789/43140/1/Aichem_2-1osbbqsz3ua1.pdf"/> <dcterms:title>The structure of the ubiquitin-like modifier FAT10 reveals an alternative targeting mechanism for proteasomal degradation</dcterms:title> <dc:creator>Schmidtke, Gunter</dc:creator> <dc:creator>Peter, Christine</dc:creator> <dc:rights>Attribution 4.0 International</dc:rights> <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:creator>Schwab, Ricarda</dc:creator> <dc:contributor>Scheuermann, Sophia</dc:contributor> <dcterms:rights rdf:resource="http://creativecommons.org/licenses/by/4.0/"/> <dcterms:issued>2018-08-20</dcterms:issued> <dc:creator>Scheuermann, Sophia</dc:creator> <foaf:homepage rdf:resource="http://localhost:8080/jspui"/> <dc:contributor>Schwab, Ricarda</dc:contributor> <dspace:isPartOfCollection rdf:resource="https://kops.uni-konstanz.de/rdf/resource/123456789/28"/> </rdf:Description> </rdf:RDF>

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