Regulation of p27 degradation and S-phase progression by Ro52 RING finger protein


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SABILE, Abdelmajid, Christiane WIRBELAUER, Daniel HESS, Ulrike KOGEL, Martin SCHEFFNER, Wilhelm KREK, Andrea M. MEYER, 2006. Regulation of p27 degradation and S-phase progression by Ro52 RING finger protein. In: Molecular and Cellular Biology. 26(16), pp. 5994-6004. ISSN 0270-7306. Available under: doi: 10.1128/MCB.01630-05

@article{Sabile2006-08Regul-16767, title={Regulation of p27 degradation and S-phase progression by Ro52 RING finger protein}, year={2006}, doi={10.1128/MCB.01630-05}, number={16}, volume={26}, issn={0270-7306}, journal={Molecular and Cellular Biology}, pages={5994--6004}, author={Sabile, Abdelmajid and Wirbelauer, Christiane and Hess, Daniel and Kogel, Ulrike and Scheffner, Martin and Krek, Wilhelm and Meyer, Andrea M.} }

<rdf:RDF xmlns:dcterms="" xmlns:dc="" xmlns:rdf="" xmlns:bibo="" xmlns:dspace="" xmlns:foaf="" xmlns:void="" xmlns:xsd="" > <rdf:Description rdf:about=""> <dc:creator>Sabile, Abdelmajid</dc:creator> <dspace:isPartOfCollection rdf:resource=""/> <dc:contributor>Meyer, Andrea M.</dc:contributor> <dcterms:rights rdf:resource=""/> <dcterms:bibliographicCitation>Publ. in: Molecular and Cellular Biology ; 26 (2006), 16. - S. 5994-6004</dcterms:bibliographicCitation> <dc:creator>Meyer, Andrea M.</dc:creator> <dcterms:abstract xml:lang="eng">Ubiquitin-mediated degradation of the cyclin-dependent kinase inhibitor p27 provides a powerful route for enforcing normal progression through the mammalian cell cycle. According to a current model, the ubiquitination of p27 during S-phase progression is mediated by SCFSkp2 E3 ligase that captures Thr187-phosphorylated p27 by means of the F-box protein Skp2, which in turn couples the bound substrate via Skp1 to a catalytic core complex composed of Cul1 and the Rbx/Roc RING finger protein. Here we identify Skp2 as a component of an Skp1-cullin-F-box complex that is based on a Cul1-Ro52 RING finger B-box coiled-coil motif family protein catalytic core. Ro52-containing complexes display E3 ligase activity and promote the ubiquitination of Thr187-phosphorylated p27 in a RING-dependent manner in vitro. The knockdown of Ro52 expression in human cells with small interfering RNAs causes the accumulation of p27 and the failure of cells to enter S phase. Importantly, these effects are abrogated by the simultaneous removal of p27. Taken together, these data suggest a key role for Ro52 RING finger protein in the regulation of p27 degradation and S-phase progression in mammalian cells and provide evidence for the existence of a Cul1-based catalytic core that utilizes Ro52 RING protein to promote ubiquitination.</dcterms:abstract> <dcterms:isPartOf rdf:resource=""/> <dc:creator>Scheffner, Martin</dc:creator> <bibo:uri rdf:resource=""/> <dc:creator>Krek, Wilhelm</dc:creator> <dc:creator>Kogel, Ulrike</dc:creator> <dc:date rdf:datatype="">2011-11-16T08:50:49Z</dc:date> <dcterms:hasPart rdf:resource=""/> <dc:contributor>Hess, Daniel</dc:contributor> <void:sparqlEndpoint rdf:resource="http://localhost/fuseki/dspace/sparql"/> <dcterms:issued>2006-08</dcterms:issued> <dc:contributor>Scheffner, Martin</dc:contributor> <dc:creator>Wirbelauer, Christiane</dc:creator> <dc:contributor>Sabile, Abdelmajid</dc:contributor> <dc:contributor>Wirbelauer, Christiane</dc:contributor> <dc:creator>Hess, Daniel</dc:creator> <dc:contributor>Krek, Wilhelm</dc:contributor> <dc:language>eng</dc:language> <dcterms:available rdf:datatype="">2011-11-16T08:50:49Z</dcterms:available> <foaf:homepage rdf:resource="http://localhost:8080/jspui"/> <dcterms:title>Regulation of p27 degradation and S-phase progression by Ro52 RING finger protein</dcterms:title> <dspace:hasBitstream rdf:resource=""/> <dc:contributor>Kogel, Ulrike</dc:contributor> <dc:rights>terms-of-use</dc:rights> </rdf:Description> </rdf:RDF>

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