http://purl.uniprot.org/citations/16880511 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/16880511 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/16880511 | http://www.w3.org/2000/01/rdf-schema#comment | "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 SCF(Skp2) 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."xsd:string |
http://purl.uniprot.org/citations/16880511 | http://purl.org/dc/terms/identifier | "doi:10.1128/mcb.01630-05"xsd:string |
http://purl.uniprot.org/citations/16880511 | http://purl.org/dc/terms/identifier | "doi:10.1128/mcb.01630-05"xsd:string |
http://purl.uniprot.org/citations/16880511 | http://purl.uniprot.org/core/author | "Hess D."xsd:string |
http://purl.uniprot.org/citations/16880511 | http://purl.uniprot.org/core/author | "Hess D."xsd:string |
http://purl.uniprot.org/citations/16880511 | http://purl.uniprot.org/core/author | "Meyer A.M."xsd:string |
http://purl.uniprot.org/citations/16880511 | http://purl.uniprot.org/core/author | "Meyer A.M."xsd:string |
http://purl.uniprot.org/citations/16880511 | http://purl.uniprot.org/core/author | "Sabile A."xsd:string |
http://purl.uniprot.org/citations/16880511 | http://purl.uniprot.org/core/author | "Sabile A."xsd:string |
http://purl.uniprot.org/citations/16880511 | http://purl.uniprot.org/core/author | "Krek W."xsd:string |
http://purl.uniprot.org/citations/16880511 | http://purl.uniprot.org/core/author | "Krek W."xsd:string |
http://purl.uniprot.org/citations/16880511 | http://purl.uniprot.org/core/author | "Wirbelauer C."xsd:string |
http://purl.uniprot.org/citations/16880511 | http://purl.uniprot.org/core/author | "Wirbelauer C."xsd:string |
http://purl.uniprot.org/citations/16880511 | http://purl.uniprot.org/core/author | "Scheffner M."xsd:string |
http://purl.uniprot.org/citations/16880511 | http://purl.uniprot.org/core/author | "Scheffner M."xsd:string |
http://purl.uniprot.org/citations/16880511 | http://purl.uniprot.org/core/author | "Kogel U."xsd:string |
http://purl.uniprot.org/citations/16880511 | http://purl.uniprot.org/core/author | "Kogel U."xsd:string |
http://purl.uniprot.org/citations/16880511 | http://purl.uniprot.org/core/date | "2006"xsd:gYear |
http://purl.uniprot.org/citations/16880511 | http://purl.uniprot.org/core/date | "2006"xsd:gYear |
http://purl.uniprot.org/citations/16880511 | http://purl.uniprot.org/core/name | "Mol. Cell. Biol."xsd:string |
http://purl.uniprot.org/citations/16880511 | http://purl.uniprot.org/core/name | "Mol. Cell. Biol."xsd:string |
http://purl.uniprot.org/citations/16880511 | http://purl.uniprot.org/core/pages | "5994-6004"xsd:string |
http://purl.uniprot.org/citations/16880511 | http://purl.uniprot.org/core/pages | "5994-6004"xsd:string |