KOPS - Das Institutionelle Repositorium der Universität Konstanz

The Chaperone-associated Ubiquitin Ligase CHIP Is Able to Target p53 for Proteasomal Degradation

The Chaperone-associated Ubiquitin Ligase CHIP Is Able to Target p53 for Proteasomal Degradation

Zitieren

Dateien zu dieser Ressource

Prüfsumme: MD5:fc0c7bacb03ba53adff29d3061c9f76e

ESSER, Claudia, Martin SCHEFFNER, Jörg HÖHFELD, 2005. The Chaperone-associated Ubiquitin Ligase CHIP Is Able to Target p53 for Proteasomal Degradation. In: Journal of Biological Chemistry. 280(29), pp. 27443-27448. ISSN 0021-9258

@article{Esser2005-07-22Chape-16769, title={The Chaperone-associated Ubiquitin Ligase CHIP Is Able to Target p53 for Proteasomal Degradation}, year={2005}, doi={10.1074/jbc.M501574200}, number={29}, volume={280}, issn={0021-9258}, journal={Journal of Biological Chemistry}, pages={27443--27448}, author={Esser, Claudia and Scheffner, Martin and Höhfeld, Jörg} }

<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/123456789/16769"> <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2011-11-16T08:20:34Z</dc:date> <dcterms:abstract xml:lang="eng">The cellular level of the tumor suppressor p53 is tightly regulated through induced degradation via the ubiquitin/proteasome system. The ubiquitin ligase Mdm2 plays a pivotal role in stimulating p53 turnover. However, recently additional ubiquitin ligases have been identified that participate in the degradation of the tumor suppressor. Apparently, multiple degradation pathways are employed to ensure proper destruction of p53. Here we show that the chaperone-associated ubiquitin ligase CHIP is able to induce the proteasomal degradation of p53. CHIP-induced degradation was observed for mutant p53, which was previously shown to associate with the chaperones Hsc70 and Hsp90, and for the wild-type form of the tumor suppressor. Our data reveal that mutant and wild-type p53 transiently associate with molecular chaperones and can be diverted onto a degradation pathway through this association.</dcterms:abstract> <dcterms:issued>2005-07-22</dcterms:issued> <dcterms:title>The Chaperone-associated Ubiquitin Ligase CHIP Is Able to Target p53 for Proteasomal Degradation</dcterms:title> <dc:creator>Höhfeld, Jörg</dc:creator> <dc:contributor>Scheffner, Martin</dc:contributor> <dcterms:rights rdf:resource="http://nbn-resolving.org/urn:nbn:de:bsz:352-20140905103605204-4002607-1"/> <dc:creator>Esser, Claudia</dc:creator> <dc:creator>Scheffner, Martin</dc:creator> <dc:language>eng</dc:language> <dcterms:bibliographicCitation>Publ. in: The Journal of Biological Chemistry ; 280 (2005), 29. - S. 27443-27448</dcterms:bibliographicCitation> <dc:contributor>Höhfeld, Jörg</dc:contributor> <dc:rights>deposit-license</dc:rights> <bibo:uri rdf:resource="http://kops.uni-konstanz.de/handle/123456789/16769"/> <dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2011-11-16T08:20:34Z</dcterms:available> <dc:contributor>Esser, Claudia</dc:contributor> </rdf:Description> </rdf:RDF>

Dateiabrufe seit 01.10.2014 (Informationen über die Zugriffsstatistik)

Esser_167692.pdf 1

Das Dokument erscheint in:

KOPS Suche


Stöbern

Mein Benutzerkonto