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http://purl.uniprot.org/citations/22935713http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/22935713http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/22935713http://www.w3.org/2000/01/rdf-schema#comment"Origin recognition complex (ORC) is highly dynamic, with several ORC subunits getting posttranslationally modified by phosphorylation or ubiquitination in a cell cycle-dependent manner. We have previously demonstrated that a WD repeat containing protein ORC-associated (ORCA/LRWD1) stabilizes the ORC on chromatin and facilitates pre-RC assembly. Further, ORCA levels are cell cycle-regulated, with highest levels during G(1), and progressively decreasing during S phase, but the mechanism remains to be elucidated. We now demonstrate that ORCA is polyubiquitinated in vivo, with elevated ubiquitination observed at the G(1)/S boundary. ORCA utilizes lysine-48 (K48) ubiquitin linkage, suggesting that ORCA ubiquitination mediates its regulated degradation. Ubiquitinated ORCA is re-localized in the form of nuclear aggregates and is predominantly associated with chromatin. We demonstrate that ORCA associates with the E3 ubiquitin ligase Cul4A-Ddb1. ORCA is ubiquitinated at the WD40 repeat domain, a region that is also recognized by Orc2. Furthermore, Orc2 associates only with the non-ubiquitinated form of ORCA, and Orc2 depletion results in the proteasome-mediated destabilization of ORCA. Based on the results, we suggest that Orc2 protects ORCA from ubiquitin-mediated degradation in vivo."xsd:string
http://purl.uniprot.org/citations/22935713http://purl.org/dc/terms/identifier"doi:10.4161/cc.21870"xsd:string
http://purl.uniprot.org/citations/22935713http://purl.org/dc/terms/identifier"doi:10.4161/cc.21870"xsd:string
http://purl.uniprot.org/citations/22935713http://purl.uniprot.org/core/author"Shen Z."xsd:string
http://purl.uniprot.org/citations/22935713http://purl.uniprot.org/core/author"Shen Z."xsd:string
http://purl.uniprot.org/citations/22935713http://purl.uniprot.org/core/author"Prasanth S.G."xsd:string
http://purl.uniprot.org/citations/22935713http://purl.uniprot.org/core/author"Prasanth S.G."xsd:string
http://purl.uniprot.org/citations/22935713http://purl.uniprot.org/core/date"2012"xsd:gYear
http://purl.uniprot.org/citations/22935713http://purl.uniprot.org/core/date"2012"xsd:gYear
http://purl.uniprot.org/citations/22935713http://purl.uniprot.org/core/name"Cell Cycle"xsd:string
http://purl.uniprot.org/citations/22935713http://purl.uniprot.org/core/name"Cell Cycle"xsd:string
http://purl.uniprot.org/citations/22935713http://purl.uniprot.org/core/pages"3578-3589"xsd:string
http://purl.uniprot.org/citations/22935713http://purl.uniprot.org/core/pages"3578-3589"xsd:string
http://purl.uniprot.org/citations/22935713http://purl.uniprot.org/core/title"Orc2 protects ORCA from ubiquitin-mediated degradation."xsd:string
http://purl.uniprot.org/citations/22935713http://purl.uniprot.org/core/title"Orc2 protects ORCA from ubiquitin-mediated degradation."xsd:string
http://purl.uniprot.org/citations/22935713http://purl.uniprot.org/core/volume"11"xsd:string
http://purl.uniprot.org/citations/22935713http://purl.uniprot.org/core/volume"11"xsd:string
http://purl.uniprot.org/citations/22935713http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/22935713
http://purl.uniprot.org/citations/22935713http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/22935713
http://purl.uniprot.org/citations/22935713http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/22935713
http://purl.uniprot.org/citations/22935713http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/22935713
http://purl.uniprot.org/uniprot/Q16531http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/22935713
http://purl.uniprot.org/uniprot/Q9UFC0http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/22935713