Publikation:

NEDD8 Ultimate Buster-1L Interacts with the Ubiquitin-like Protein FAT10 and Accelerates Its Degradation

Lade...
Vorschaubild

Dateien

Hipp_221338.pdf
Hipp_221338.pdfGröße: 302.94 KBDownloads: 251

Datum

2004

Herausgeber:innen

Kontakt

ISSN der Zeitschrift

Electronic ISSN

ISBN

Bibliografische Daten

Verlag

Schriftenreihe

Auflagebezeichnung

ArXiv-ID

Internationale Patentnummer

Angaben zur Forschungsförderung

Projekt

Open Access-Veröffentlichung
Open Access Green
Core Facility der Universität Konstanz

Gesperrt bis

Titel in einer weiteren Sprache

Publikationstyp
Zeitschriftenartikel
Publikationsstatus
Published

Erschienen in

Journal of Biological Chemistry. 2004, 279(16), pp. 16503-16510. ISSN 0021-9258. eISSN 1083-351X. Available under: doi: 10.1074/jbc.M310114200

Zusammenfassung

FAT10 is an interferon-gamma-inducible ubiquitin-like protein that consists of two ubiquitin-like domains. FAT10 bears a diglycine motif at its C terminus that can form isopeptide bonds to so far unidentified target proteins. Recently we found that FAT10 and its conjugates are rapidly degraded by the proteasome and that the Nterminal fusion of FAT10 to a long lived protein markedly reduces its half-life. FAT10 may hence direct target proteins to the proteasome for degradation. In this study we report a new interaction partner of FAT10 that may link FAT10 to the proteasome. A yeast two-hybrid screen identified NEDD8 ultimate buster-1L (NUB1L) as a non-covalent binding partner of FAT10, and this interaction was confirmed by coimmunoprecipitation and glutathione S-transferase pull-down experiments. NUB1L is also an interferon-inducible protein that has been reported to interact with the ubiquitin-like protein NEDD8, thus leading to accelerated NEDD8 degradation. Here we show that NUB1L binds to FAT10 much stronger than to NEDD8 and that NEDD8 cannot compete with FAT10 for NUB1L binding. The interaction of FAT10 and NUB1L is specific as green fluorescent fusion proteins containing ubiquitin or SUMO-1 do not bind to NUB1L. The coexpression of NUB1L enhanced the degradation rate of FAT10 8-fold, whereas NEDD8 degradation was only accelerated 2-fold. Because NUB1 was shown to bind to the proteasome subunit RPN10 in vitro and to be contained in 26 S proteasome preparations, it may function as a linker that targets FAT10 for degradation by the proteasome.

Zusammenfassung in einer weiteren Sprache

Fachgebiet (DDC)
570 Biowissenschaften, Biologie

Schlagwörter

Konferenz

Rezension
undefined / . - undefined, undefined

Forschungsvorhaben

Organisationseinheiten

Zeitschriftenheft

Zugehörige Datensätze in KOPS

Zitieren

ISO 690HIPP, Mark-Steffen, Shahri RAASI, Marcus GRÖTTRUP, Gunter SCHMIDTKE, 2004. NEDD8 Ultimate Buster-1L Interacts with the Ubiquitin-like Protein FAT10 and Accelerates Its Degradation. In: Journal of Biological Chemistry. 2004, 279(16), pp. 16503-16510. ISSN 0021-9258. eISSN 1083-351X. Available under: doi: 10.1074/jbc.M310114200
BibTex
@article{Hipp2004-04-16NEDD8-22133,
  year={2004},
  doi={10.1074/jbc.M310114200},
  title={NEDD8 Ultimate Buster-1L Interacts with the Ubiquitin-like Protein FAT10 and Accelerates Its Degradation},
  number={16},
  volume={279},
  issn={0021-9258},
  journal={Journal of Biological Chemistry},
  pages={16503--16510},
  author={Hipp, Mark-Steffen and Raasi, Shahri and Gröttrup, Marcus and Schmidtke, Gunter}
}
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/123456789/22133">
    <dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2013-03-15T10:09:02Z</dcterms:available>
    <dc:contributor>Gröttrup, Marcus</dc:contributor>
    <dc:contributor>Schmidtke, Gunter</dc:contributor>
    <dcterms:issued>2004-04-16</dcterms:issued>
    <dcterms:isPartOf rdf:resource="https://kops.uni-konstanz.de/server/rdf/resource/123456789/28"/>
    <dcterms:title>NEDD8 Ultimate Buster-1L Interacts with the Ubiquitin-like Protein FAT10 and Accelerates Its Degradation</dcterms:title>
    <void:sparqlEndpoint rdf:resource="http://localhost/fuseki/dspace/sparql"/>
    <dc:contributor>Hipp, Mark-Steffen</dc:contributor>
    <dspace:hasBitstream rdf:resource="https://kops.uni-konstanz.de/bitstream/123456789/22133/2/Hipp_221338.pdf"/>
    <bibo:uri rdf:resource="http://kops.uni-konstanz.de/handle/123456789/22133"/>
    <dspace:isPartOfCollection rdf:resource="https://kops.uni-konstanz.de/server/rdf/resource/123456789/28"/>
    <dcterms:bibliographicCitation>The journal of biological chemistry : JBC ; 279 (2004), 16. - S. 16503-16510</dcterms:bibliographicCitation>
    <dc:creator>Hipp, Mark-Steffen</dc:creator>
    <dc:creator>Schmidtke, Gunter</dc:creator>
    <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2013-03-15T10:09:02Z</dc:date>
    <dc:creator>Raasi, Shahri</dc:creator>
    <foaf:homepage rdf:resource="http://localhost:8080/"/>
    <dc:creator>Gröttrup, Marcus</dc:creator>
    <dcterms:hasPart rdf:resource="https://kops.uni-konstanz.de/bitstream/123456789/22133/2/Hipp_221338.pdf"/>
    <dc:contributor>Raasi, Shahri</dc:contributor>
    <dcterms:abstract xml:lang="eng">FAT10 is an interferon-gamma-inducible ubiquitin-like protein that consists of two ubiquitin-like domains. FAT10 bears a diglycine motif at its C terminus that can form isopeptide bonds to so far unidentified target proteins. Recently we found that FAT10 and its conjugates are rapidly degraded by the proteasome and that the Nterminal fusion of FAT10 to a long lived protein markedly reduces its half-life. FAT10 may hence direct target proteins to the proteasome for degradation. In this study we report a new interaction partner of FAT10 that may link FAT10 to the proteasome. A yeast two-hybrid screen identified NEDD8 ultimate buster-1L (NUB1L) as a non-covalent binding partner of FAT10, and this interaction was confirmed by coimmunoprecipitation and glutathione S-transferase pull-down experiments. NUB1L is also an interferon-inducible protein that has been reported to interact with the ubiquitin-like protein NEDD8, thus leading to accelerated NEDD8 degradation. Here we show that NUB1L binds to FAT10 much stronger than to NEDD8 and that NEDD8 cannot compete with FAT10 for NUB1L binding. The interaction of FAT10 and NUB1L is specific as green fluorescent fusion proteins containing ubiquitin or SUMO-1 do not bind to NUB1L. The coexpression of NUB1L enhanced the degradation rate of FAT10 8-fold, whereas NEDD8 degradation was only accelerated 2-fold. Because NUB1 was shown to bind to the proteasome subunit RPN10 in vitro and to be contained in 26 S proteasome preparations, it may function as a linker that targets FAT10 for degradation by the proteasome.</dcterms:abstract>
    <dc:rights>terms-of-use</dc:rights>
    <dc:language>eng</dc:language>
    <dcterms:rights rdf:resource="https://rightsstatements.org/page/InC/1.0/"/>
  </rdf:Description>
</rdf:RDF>

Interner Vermerk

xmlui.Submission.submit.DescribeStep.inputForms.label.kops_note_fromSubmitter

Kontakt
URL der Originalveröffentl.

Prüfdatum der URL

Prüfungsdatum der Dissertation

Finanzierungsart

Kommentar zur Publikation

Allianzlizenz
Corresponding Authors der Uni Konstanz vorhanden
Internationale Co-Autor:innen
Universitätsbibliographie
Ja
Begutachtet
Diese Publikation teilen