Non-proteolytic ubiquitylation regulates the APC/C-inhibitory function of XErp1

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HÖRMANSEDER, Eva Beate, 2011. Non-proteolytic ubiquitylation regulates the APC/C-inhibitory function of XErp1

@phdthesis{Hormanseder2011Non-p-19294, title={Non-proteolytic ubiquitylation regulates the APC/C-inhibitory function of XErp1}, year={2011}, author={Hörmanseder, Eva Beate}, address={Konstanz}, school={Universität Konstanz} }

<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/123456789/19294"> <dc:creator>Hörmanseder, Eva Beate</dc:creator> <dcterms:title>Non-proteolytic ubiquitylation regulates the APC/C-inhibitory function of XErp1</dcterms:title> <bibo:uri rdf:resource="http://kops.uni-konstanz.de/handle/123456789/19294"/> <dc:language>eng</dc:language> <dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2012-05-14T11:55:25Z</dcterms:available> <dcterms:issued>2011</dcterms:issued> <dc:contributor>Hörmanseder, Eva Beate</dc:contributor> <dc:rights>deposit-license</dc:rights> <dcterms:rights rdf:resource="http://nbn-resolving.org/urn:nbn:de:bsz:352-20140905103605204-4002607-1"/> <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2012-05-14T11:55:25Z</dc:date> <dcterms:abstract xml:lang="eng">Mature Xenopus oocytes are arrested in meiosis by the activity of XErp1/Emi2, an inhibitor of the ubiquitin-ligase anaphase-promoting complex/cyclosome (APC/C). Upon fertilization, XErp1 is degraded resulting in APC/C activation and the consequent degradation of cell cycle regulators and exit from meiosis. In this study, we show that a modest increase in the activity of the ubiquitin-conjugating enzyme UbcX overrides the meiotic arrest in an APC/C-dependent reaction. Intriguingly, XErp1 remains stable under these conditions. We observed that UbcX causes the ubiquitylation of XErp1 followed by its dissociation from the APC/C. Our data favor the idea that ubiquitylation regulates XErp1’s APC/C inhibitory activity. Similarly, UbcX can trigger activation of the APC/C in Xenopus egg extracts with an activated spindle checkpoint. This suggests that in vertebrate cells, the APC/C can liberate itself from XErp1 and spindle checkpoint inhibition in an autocatalytic manner. In addition, our findings that Cdc20 is stable during meiotic arrest suggest that the meiotic arrest is not mediated via the degradation of Cdc20.</dcterms:abstract> </rdf:Description> </rdf:RDF>

Dateiabrufe seit 01.10.2014 (Informationen über die Zugriffsstatistik)

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