A novel ubiquitination factor, E4, is involved in multiubiquitin chain assembly

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KOEGL, Manfred, Thorsten HOPPE, Stephan SCHLENKER, Helle D. ULRICH, Thomas U. MAYER, Stefan JENTSCH, 1999. A novel ubiquitination factor, E4, is involved in multiubiquitin chain assembly. In: Cell. 96(5), pp. 635-644. ISSN 0092-8674

@article{Koegl1999novel-14057, title={A novel ubiquitination factor, E4, is involved in multiubiquitin chain assembly}, year={1999}, doi={10.1016/S0092-8674(00)80574-7}, number={5}, volume={96}, issn={0092-8674}, journal={Cell}, pages={635--644}, author={Koegl, Manfred and Hoppe, Thorsten and Schlenker, Stephan and Ulrich, Helle D. and Mayer, Thomas U. and Jentsch, Stefan} }

<rdf:RDF xmlns:rdf="http://www.w3.org/1999/02/22-rdf-syntax-ns#" xmlns:bibo="http://purl.org/ontology/bibo/" xmlns:dc="http://purl.org/dc/elements/1.1/" xmlns:dcterms="http://purl.org/dc/terms/" xmlns:xsd="http://www.w3.org/2001/XMLSchema#" > <rdf:Description rdf:about="https://kops.uni-konstanz.de/rdf/resource/123456789/14057"> <dcterms:issued>1999</dcterms:issued> <dc:creator>Ulrich, Helle D.</dc:creator> <dcterms:rights rdf:resource="http://nbn-resolving.org/urn:nbn:de:bsz:352-20140905103605204-4002607-1"/> <dc:contributor>Koegl, Manfred</dc:contributor> <dc:creator>Jentsch, Stefan</dc:creator> <dc:creator>Hoppe, Thorsten</dc:creator> <dc:contributor>Schlenker, Stephan</dc:contributor> <dc:contributor>Hoppe, Thorsten</dc:contributor> <dc:rights>deposit-license</dc:rights> <dcterms:title>A novel ubiquitination factor, E4, is involved in multiubiquitin chain assembly</dcterms:title> <dc:creator>Koegl, Manfred</dc:creator> <dc:creator>Schlenker, Stephan</dc:creator> <dc:contributor>Mayer, Thomas U.</dc:contributor> <dc:contributor>Jentsch, Stefan</dc:contributor> <dc:creator>Mayer, Thomas U.</dc:creator> <bibo:uri rdf:resource="http://kops.uni-konstanz.de/handle/123456789/14057"/> <dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2012-01-11T11:28:07Z</dcterms:available> <dc:language>eng</dc:language> <dcterms:abstract xml:lang="eng">Proteins modified by multiubiquitin chains are the preferred substrates of the proteasome. Ubiquitination involves a ubiquitin-activating enzyme, E1, a ubiquitin-conjugating enzyme, E2, and often a substrate-specific ubiquitin-protein ligase, E3. Here we show that efficient multiubiquitination needed for proteasomal targeting of a model substrate requires an additional conjugation factor, named E4. This protein, previously known as UFD2 in yeast, binds to the ubiquitin moieties of preformed conjugates and catalyzes ubiquitin chain assembly in conjunction with E1, E2, and E3. Intriguingly, E4 defines a novel protein family that includes two human members and the regulatory protein NOSA from Dictyostelium required for fruiting body development. In yeast, E4 activity is linked to cell survival under stress conditions, indicating that eukaryotes utilize E4-dependent proteolysis pathways for multiple cellular functions.</dcterms:abstract> <dcterms:bibliographicCitation>Publ. in: Cell ; 96 (1999), 5. - S. 635-644</dcterms:bibliographicCitation> <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2012-01-11T11:28:07Z</dc:date> <dc:contributor>Ulrich, Helle D.</dc:contributor> </rdf:Description> </rdf:RDF>

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