Source:http://linkedlifedata.com/resource/pubmed/id/12429912
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
2002-11-13
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pubmed:abstractText |
Centrosome duplication in mammalian cells is a highly regulated process, occurs in coordination of other cell cycle events. However, molecular exploration of this important cellular process had been difficult due to unavailability of a simple assay system. Here, using centrosomes loosely associated with nuclei isolated from cultured cells, we developed a cell-free centriole (duplication unit of the centrosome) duplication system: unduplicated centrosomes bound to the nuclei are able to undergo duplication in the presence of G1/S extracts. We show that the ability of G1/S extracts to induce centriole duplication in vitro depends on the presence of active CDK2/cyclin E. It has been shown that dissociation of centro-somal nucleophosmin (NPM)/B23 triggered by CDK2/cyclin E-mediated phosphorylation is required for initiation of centrosome duplication. We show that centriole duplication is blocked when nuclei were preincubated with the anti-NPM/B23 antibody that prevents phosphorylation of NPM/B23 by CDK2/cyclin E. These studies provide not only direct evidence for the requirement of CDK2/cyclin E and phosphorylation of NPM/B23 for centrosomes to initiate duplication, but a valuable experimental system for further exploration of the molecular regulation of centrosome duplication in somatic cells of higher animals.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/CDC2-CDC28 Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Cdk2 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Cyclin E,
http://linkedlifedata.com/resource/pubmed/chemical/Cyclin-Dependent Kinase 2,
http://linkedlifedata.com/resource/pubmed/chemical/Cyclin-Dependent Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Protein-Serine-Threonine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/nucleophosmin
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
1538-4101
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
1
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
75-81
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:12429912-3T3 Cells,
pubmed-meshheading:12429912-Animals,
pubmed-meshheading:12429912-CDC2-CDC28 Kinases,
pubmed-meshheading:12429912-Cell Cycle,
pubmed-meshheading:12429912-Centrioles,
pubmed-meshheading:12429912-Centrosome,
pubmed-meshheading:12429912-Cyclin E,
pubmed-meshheading:12429912-Cyclin-Dependent Kinase 2,
pubmed-meshheading:12429912-Cyclin-Dependent Kinases,
pubmed-meshheading:12429912-G1 Phase,
pubmed-meshheading:12429912-Mice,
pubmed-meshheading:12429912-Nuclear Proteins,
pubmed-meshheading:12429912-Phosphorylation,
pubmed-meshheading:12429912-Protein-Serine-Threonine Kinases,
pubmed-meshheading:12429912-S Phase
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pubmed:year |
2002
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pubmed:articleTitle |
A mammalian in vitro centriole duplication system: evidence for involvement of CDK2/cyclin E and nucleophosmin/B23 in centrosome duplication.
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pubmed:affiliation |
Department of Cell Biology, University of Cincinnati College of Medicine, P.O. Box 670521, Ohio 45267-0521, USA.
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pubmed:publicationType |
Journal Article
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