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dc.contributor.authorLaman, Heike
dc.contributor.authorPeters, Gordon
dc.contributor.authorJones, Nic
dc.date.accessioned2009-11-06T16:53:33Z
dc.date.available2009-11-06T16:53:33Z
dc.date.issued2001-12-10
dc.identifier.citationCyclin-mediated export of human Orc1. 2001, 271 (2):230-7 Exp. Cell Res.en
dc.identifier.issn0014-4827
dc.identifier.pmid11716535
dc.identifier.doi10.1006/excr.2001.5360
dc.identifier.urihttp://hdl.handle.net/10541/85615
dc.description.abstractViral cyclin/cdk6 complexes interact with and phosphorylate human Orc1, a component of the origin recognition complex (ORC) that functions in DNA replication. Here we assess the effect that viral cyclin has on the intracellular location of human Orc1, which is present in both nuclear and cytoplasmic pools. Overexpression of K cyclin or cyclin A results in Crm1-dependent export of Orc1 to the cytoplasm, and this process is dependent on the phosphorylation status of several cdk target sites in Orc1. These findings support a model where S phase promoting cyclin activity drives the export of a component of replication complexes.
dc.language.isoenen
dc.subjectCultured Tumour Cellsen
dc.subject.meshAmino Acid Sequence
dc.subject.meshAntineoplastic Agents
dc.subject.meshAspartic Acid
dc.subject.meshCell Compartmentation
dc.subject.meshCell Nucleus
dc.subject.meshCyclin A
dc.subject.meshCyclin E
dc.subject.meshCyclin-Dependent Kinases
dc.subject.meshCyclins
dc.subject.meshCytoplasm
dc.subject.meshDNA Replication
dc.subject.meshDNA-Binding Proteins
dc.subject.meshFatty Acids, Unsaturated
dc.subject.meshGene Expression Regulation
dc.subject.meshGenetic Vectors
dc.subject.meshGreen Fluorescent Proteins
dc.subject.meshHumans
dc.subject.meshIndicators and Reagents
dc.subject.meshLuminescent Proteins
dc.subject.meshMutation
dc.subject.meshOrigin Recognition Complex
dc.subject.meshPhosphorylation
dc.subject.meshProtein Transport
dc.subject.meshS Phase
dc.subject.meshTumor Cells, Cultured
dc.subject.meshViral Proteins
dc.titleCyclin-mediated export of human Orc1.en
dc.typeArticleen
dc.contributor.departmentMolecular Oncology Laboratory, Gene Regulation Laboratory, Imperial Cancer Research Fund, 44 Lincoln's Inn Fields, London, WC2A 3PX, United Kingdom.en
dc.identifier.journalExperimental Cell Researchen
html.description.abstractViral cyclin/cdk6 complexes interact with and phosphorylate human Orc1, a component of the origin recognition complex (ORC) that functions in DNA replication. Here we assess the effect that viral cyclin has on the intracellular location of human Orc1, which is present in both nuclear and cytoplasmic pools. Overexpression of K cyclin or cyclin A results in Crm1-dependent export of Orc1 to the cytoplasm, and this process is dependent on the phosphorylation status of several cdk target sites in Orc1. These findings support a model where S phase promoting cyclin activity drives the export of a component of replication complexes.


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