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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
6
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pubmed:dateCreated |
2008-6-3
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pubmed:abstractText |
Separation of duplicated centrosomes (spindle-pole bodies or SPBs in yeast) is a crucial step in the biogenesis of the mitotic spindle. In vertebrates, centrosome separation requires the BimC family kinesin Eg5 and the activities of Cdk1 and polo kinase; however, the roles of these kinases are not fully understood. In Saccharomyces cerevisiae, SPB separation also requires activated Cdk1 and the plus-end kinesins Cin8 (homologous to vertebrate Eg5) and Kip1. Here we report that polo kinase has a role in the separation of SPBs. We show that adequate accumulation of Cin8 and Kip1 requires inactivation of the anaphase-promoting complex-activator Cdh1 through sequential phosphorylation by Cdk1 and polo kinase. In this process, Cdk1 functions as a priming kinase in that Cdk1-mediated phosphorylation creates a binding site for polo kinase,which further phosphorylates Cdh1. Thus, Cdh1 inactivation through the synergistic action of Cdk1 and polo kinase provides a new model for inactivation of cell-cycle effectors.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/18500339-10047524,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18500339-10882135,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18500339-11014197,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18500339-11371338,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18500339-11438652,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18500339-11438663,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18500339-12214249,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18500339-12456658,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18500339-12595692,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18500339-12738781,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18500339-1387566,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18500339-15467459,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18500339-15473833,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18500339-15678131,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18500339-15838519,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18500339-1618897,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18500339-16688214,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18500339-17016823,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18500339-17030612,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18500339-17178718,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18500339-1849457,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18500339-7622568,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18500339-7790357,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18500339-8548803,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18500339-8887667,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18500339-8991084,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18500339-9560342,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18500339-9831566
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Acm1 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/CDC2 Protein Kinase,
http://linkedlifedata.com/resource/pubmed/chemical/CDC28 Protein Kinase, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Cell Cycle Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Cyclin-Dependent Kinase 5,
http://linkedlifedata.com/resource/pubmed/chemical/Hct1 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/KIP1 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Microtubule-Associated Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Molecular Motor Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Protein-Serine-Threonine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Repressor Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Ubiquitin-Protein Ligase Complexes,
http://linkedlifedata.com/resource/pubmed/chemical/anaphase-promoting complex,
http://linkedlifedata.com/resource/pubmed/chemical/polo-like kinase 1
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
1476-4679
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:volume |
10
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
665-75
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pubmed:dateRevised |
2011-11-2
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pubmed:meshHeading |
pubmed-meshheading:18500339-CDC2 Protein Kinase,
pubmed-meshheading:18500339-CDC28 Protein Kinase, S cerevisiae,
pubmed-meshheading:18500339-Cell Cycle,
pubmed-meshheading:18500339-Cell Cycle Proteins,
pubmed-meshheading:18500339-Cell Nucleus,
pubmed-meshheading:18500339-Cyclin-Dependent Kinase 5,
pubmed-meshheading:18500339-Microtubule-Associated Proteins,
pubmed-meshheading:18500339-Mitotic Spindle Apparatus,
pubmed-meshheading:18500339-Models, Biological,
pubmed-meshheading:18500339-Models, Genetic,
pubmed-meshheading:18500339-Molecular Motor Proteins,
pubmed-meshheading:18500339-Phosphorylation,
pubmed-meshheading:18500339-Protein-Serine-Threonine Kinases,
pubmed-meshheading:18500339-Proto-Oncogene Proteins,
pubmed-meshheading:18500339-Repressor Proteins,
pubmed-meshheading:18500339-Saccharomyces cerevisiae,
pubmed-meshheading:18500339-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:18500339-Ubiquitin-Protein Ligase Complexes
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pubmed:year |
2008
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pubmed:articleTitle |
Inactivation of Cdh1 by synergistic action of Cdk1 and polo kinase is necessary for proper assembly of the mitotic spindle.
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pubmed:affiliation |
Institute of Molecular and Cell Biology, A*STAR (Agency for Science, Technology and Research), 61, Biopolis Drive, Proteos, Singapore.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
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