FAT10 and NUB1L bind to the VWA domain of Rpn10 and Rpn1 to enable proteasome-mediated proteolysis

Rani, Neha; Aichem, Annette; Schmidtke, Gunter; Kreft, Stefan G.; Gröttrup, Marcus

FAT10 and NUB1L bind to the VWA domain of Rpn10 and Rpn1 to enable proteasome-mediated proteolysis

Dateien

Rani_210170.pdfGröße: 1.09 MBDownloads: 278

Datum

2012

Publikationstyp

Zeitschriftenartikel

unikn.publication.listelement.citation.prefix.version.undefined

Nature Communications. 2012, 3, 749. eISSN 2041-1723. Available under: doi: 10.1038/ncomms1752

Zusammenfassung

FAT10 is the only ubiquitin-like modifier that can target proteins for degradation by the proteasome in a ubiquitin-independent manner. The degradation of FAT10-linked proteins by the proteasome is strongly accelerated by the ubiquitin-like–ubiquitin-associated protein NEDD8 ultimate buster-1 long (NUB1L). Here we show how FAT10 and NUB1L dock with the 26S proteasome to initiate proteolysis. We identify the 26S proteasome subunit hRpn10/S5a as the receptor for FAT10, whereas NUB1L can bind to both Rpn10 and Rpn1/S2. Unexpectedly, FAT10 and NUB1L both interact with hRpn10 via the VWA domain. FAT10 degradation in yeast shows that human Rpn10 can functionally reconstitute Rpn10-deficient yeast and that the VWA domain of hRpn10 suffices to enable FAT10 degradation. Depletion of hRpn10 causes an accumulation of FAT10-conjugates also in human cells. In conclusion, we identify the VWA domain of hRpn10 as a receptor for ubiquitin-like proteins within the 26S proteasome and elucidate how FAT10 mediates efficient proteolysis by the proteasome.

Fachgebiet (DDC)

570 Biowissenschaften, Biologie

Zitieren

ISO 690

RANI, Neha, Annette AICHEM, Gunter SCHMIDTKE, Stefan G. KREFT, Marcus GRÖTTRUP, 2012. FAT10 and NUB1L bind to the VWA domain of Rpn10 and Rpn1 to enable proteasome-mediated proteolysis. In: Nature Communications. 2012, 3, 749. eISSN 2041-1723. Available under: doi: 10.1038/ncomms1752

BibTex

@article{Rani2012FAT10-21017,
  year={2012},
  doi={10.1038/ncomms1752},
  title={FAT10 and NUB1L bind to the VWA domain of Rpn10 and Rpn1 to enable proteasome-mediated proteolysis},
  volume={3},
  journal={Nature Communications},
  author={Rani, Neha and Aichem, Annette and Schmidtke, Gunter and Kreft, Stefan G. and Gröttrup, Marcus},
  note={Article Number: 749}
}

RDF

<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/server/rdf/resource/123456789/21017">
    <dcterms:isPartOf rdf:resource="https://kops.uni-konstanz.de/server/rdf/resource/123456789/28"/>
    <dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2012-12-12T14:40:32Z</dcterms:available>
    <dspace:hasBitstream rdf:resource="https://kops.uni-konstanz.de/bitstream/123456789/21017/2/Rani_210170.pdf"/>
    <dc:creator>Rani, Neha</dc:creator>
    <dc:creator>Gröttrup, Marcus</dc:creator>
    <dcterms:rights rdf:resource="https://rightsstatements.org/page/InC/1.0/"/>
    <dc:language>eng</dc:language>
    <dcterms:bibliographicCitation>Nature Communications ; 3 (2012). - 749</dcterms:bibliographicCitation>
    <dc:creator>Kreft, Stefan G.</dc:creator>
    <dc:contributor>Gröttrup, Marcus</dc:contributor>
    <dc:creator>Aichem, Annette</dc:creator>
    <bibo:uri rdf:resource="http://kops.uni-konstanz.de/handle/123456789/21017"/>
    <dc:contributor>Schmidtke, Gunter</dc:contributor>
    <dcterms:issued>2012</dcterms:issued>
    <dc:contributor>Aichem, Annette</dc:contributor>
    <dc:rights>terms-of-use</dc:rights>
    <dc:contributor>Rani, Neha</dc:contributor>
    <dcterms:title>FAT10 and NUB1L bind to the VWA domain of Rpn10 and Rpn1 to enable proteasome-mediated proteolysis</dcterms:title>
    <dcterms:abstract xml:lang="eng">FAT10 is the only ubiquitin-like modifier that can target proteins for degradation by the proteasome in a ubiquitin-independent manner. The degradation of FAT10-linked proteins by the proteasome is strongly accelerated by the ubiquitin-like–ubiquitin-associated protein NEDD8 ultimate buster-1 long (NUB1L). Here we show how FAT10 and NUB1L dock with the 26S proteasome to initiate proteolysis. We identify the 26S proteasome subunit hRpn10/S5a as the receptor for FAT10, whereas NUB1L can bind to both Rpn10 and Rpn1/S2. Unexpectedly, FAT10 and NUB1L both interact with hRpn10 via the VWA domain. FAT10 degradation in yeast shows that human Rpn10 can functionally reconstitute Rpn10-deficient yeast and that the VWA domain of hRpn10 suffices to enable FAT10 degradation. Depletion of hRpn10 causes an accumulation of FAT10-conjugates also in human cells. In conclusion, we identify the VWA domain of hRpn10 as a receptor for ubiquitin-like proteins within the 26S proteasome and elucidate how FAT10 mediates efficient proteolysis by the proteasome.</dcterms:abstract>
    <dspace:isPartOfCollection rdf:resource="https://kops.uni-konstanz.de/server/rdf/resource/123456789/28"/>
    <void:sparqlEndpoint rdf:resource="http://localhost/fuseki/dspace/sparql"/>
    <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2012-12-12T14:40:32Z</dc:date>
    <dc:creator>Schmidtke, Gunter</dc:creator>
    <dcterms:hasPart rdf:resource="https://kops.uni-konstanz.de/bitstream/123456789/21017/2/Rani_210170.pdf"/>
    <dc:contributor>Kreft, Stefan G.</dc:contributor>
    <foaf:homepage rdf:resource="http://localhost:8080/"/>
  </rdf:Description>
</rdf:RDF>

Universitätsbibliographie

Ja