Molecular Genetics of the Ubiquitin-Proteasome System : Lessons from Yeast

Lade...
Vorschaubild
Dateien
Zu diesem Dokument gibt es keine Dateien.
Datum
2009
Autor:innen
Hochstrasser, Mark
Deng, M.
Kusmierczyk, Andrew R
Li, X.
Ravid, T.
Funakoshi, M.
Kunjappu, Mary
Xie, Y.
Herausgeber:innen
Kontakt
ISSN der Zeitschrift
Electronic ISSN
ISBN
Bibliografische Daten
Verlag
Schriftenreihe
Auflagebezeichnung
URI (zitierfähiger Link)
ArXiv-ID
Internationale Patentnummer
EU-Projektnummer
DFG-Projektnummer
Projekt
Open Access-Veröffentlichung
Sammlungen
Gesperrt bis
Titel in einer weiteren Sprache
Forschungsvorhaben
Organisationseinheiten
Zeitschriftenheft
Publikationstyp
Beitrag zu einem Sammelband
Publikationsstatus
unikn.publication.listelement.citation.prefix.version.undefined
STEFAN JENTSCH ..., , ed.. The Ubiquitin System in Health and Disease. Berlin [u.a.]: Springer, 2009, pp. 41-66. ISBN 978-3-540-85106-6. Available under: doi: 10.1007/2789_2008_100
Zusammenfassung

Our studies with the yeast Saccharomyces cerevisiae have uncovered a number of general principles governing substrate selectivity and proteolysis by the ubiquitin-proteasome system. The initial work focused on the degradation of a transcription factor, the MATα2 repressor, but the pathways uncovered have a much broader range of targets. At least two distinct ubiquitination mechanisms contribute to α2 turnover. One of them depends on a large integral membrane ubiquitin ligase (E3) and a pair of ubiquitin-conjugating enzymes (E2s). The transmembrane E3 and E2 proteins must travel from their site of synthesis in the ER to the inner nuclear membrane in order to reach nuclear substrates such as α2. The 26S proteasome is responsible for α2 degradation, and several important features of proteasome assembly and active site formation were uncovered. Most recently, we have delineated major steps in 20S proteasome assembly and have also identified several novel 20S proteasome assembly factors. Surprisingly, alterations in 20S proteasome assembly lead to defects in the assembly of the proteasome regulatory particle (RP). The RP associates with the 20S proteasome to form the 26S proteasome. Our data suggest that the 20S proteasome can function as an assembly factor for the RP, which would make it the first such factor for RP assembly identified to date.

Zusammenfassung in einer weiteren Sprache
Fachgebiet (DDC)
570 Biowissenschaften, Biologie
Schlagwörter
Konferenz
Rezension
undefined / . - undefined, undefined
Zitieren
ISO 690HOCHSTRASSER, Mark, M. DENG, Andrew R KUSMIERCZYK, X. LI, Stefan G. KREFT, T. RAVID, M. FUNAKOSHI, Mary KUNJAPPU, Y. XIE, 2009. Molecular Genetics of the Ubiquitin-Proteasome System : Lessons from Yeast. In: STEFAN JENTSCH ..., , ed.. The Ubiquitin System in Health and Disease. Berlin [u.a.]: Springer, 2009, pp. 41-66. ISBN 978-3-540-85106-6. Available under: doi: 10.1007/2789_2008_100
BibTex
@incollection{Hochstrasser2009Molec-29523,
  year={2009},
  doi={10.1007/2789_2008_100},
  title={Molecular Genetics of the Ubiquitin-Proteasome System : Lessons from Yeast},
  number={2008,1},
  isbn={978-3-540-85106-6},
  publisher={Springer},
  address={Berlin [u.a.]},
  series={Ernst Schering Foundation symposium proceedings},
  booktitle={The Ubiquitin System in Health and Disease},
  pages={41--66},
  editor={Stefan Jentsch ...},
  author={Hochstrasser, Mark and Deng, M. and Kusmierczyk, Andrew R and Li, X. and Kreft, Stefan G. and Ravid, T. and Funakoshi, M. and Kunjappu, Mary and Xie, Y.}
}
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/123456789/29523">
    <dcterms:isPartOf rdf:resource="https://kops.uni-konstanz.de/server/rdf/resource/123456789/28"/>
    <dc:language>eng</dc:language>
    <dc:contributor>Kunjappu, Mary</dc:contributor>
    <dc:contributor>Deng, M.</dc:contributor>
    <dcterms:abstract xml:lang="eng">Our studies with the yeast Saccharomyces cerevisiae have uncovered a number of general principles governing substrate selectivity and proteolysis by the ubiquitin-proteasome system. The initial work focused on the degradation of a transcription factor, the MATα2 repressor, but the pathways uncovered have a much broader range of targets. At least two distinct ubiquitination mechanisms contribute to α2 turnover. One of them depends on a large integral membrane ubiquitin ligase (E3) and a pair of ubiquitin-conjugating enzymes (E2s). The transmembrane E3 and E2 proteins must travel from their site of synthesis in the ER to the inner nuclear membrane in order to reach nuclear substrates such as α2. The 26S proteasome is responsible for α2 degradation, and several important features of proteasome assembly and active site formation were uncovered. Most recently, we have delineated major steps in 20S proteasome assembly and have also identified several novel 20S proteasome assembly factors. Surprisingly, alterations in 20S proteasome assembly lead to defects in the assembly of the proteasome regulatory particle (RP). The RP associates with the 20S proteasome to form the 26S proteasome. Our data suggest that the 20S proteasome can function as an assembly factor for the RP, which would make it the first such factor for RP assembly identified to date.</dcterms:abstract>
    <foaf:homepage rdf:resource="http://localhost:8080/"/>
    <dc:creator>Kreft, Stefan G.</dc:creator>
    <dcterms:issued>2009</dcterms:issued>
    <dc:creator>Ravid, T.</dc:creator>
    <dc:creator>Funakoshi, M.</dc:creator>
    <dc:contributor>Li, X.</dc:contributor>
    <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2015-01-16T09:18:43Z</dc:date>
    <dc:creator>Deng, M.</dc:creator>
    <dc:contributor>Funakoshi, M.</dc:contributor>
    <dcterms:title>Molecular Genetics of the Ubiquitin-Proteasome System : Lessons from Yeast</dcterms:title>
    <dspace:isPartOfCollection rdf:resource="https://kops.uni-konstanz.de/server/rdf/resource/123456789/28"/>
    <dc:creator>Kunjappu, Mary</dc:creator>
    <dc:contributor>Hochstrasser, Mark</dc:contributor>
    <dc:creator>Xie, Y.</dc:creator>
    <dc:contributor>Xie, Y.</dc:contributor>
    <dc:creator>Hochstrasser, Mark</dc:creator>
    <bibo:uri rdf:resource="http://kops.uni-konstanz.de/handle/123456789/29523"/>
    <dc:contributor>Kusmierczyk, Andrew R</dc:contributor>
    <void:sparqlEndpoint rdf:resource="http://localhost/fuseki/dspace/sparql"/>
    <dc:creator>Li, X.</dc:creator>
    <dc:creator>Kusmierczyk, Andrew R</dc:creator>
    <dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2015-01-16T09:18:43Z</dcterms:available>
    <dc:contributor>Kreft, Stefan G.</dc:contributor>
    <dc:contributor>Ravid, T.</dc:contributor>
  </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