Source:http://linkedlifedata.com/resource/pubmed/id/10226032
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
8
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| pubmed:dateCreated |
1999-6-1
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| pubmed:abstractText |
Cyclin-dependent kinases (Cdks) are fully active only when phosphorylated by a Cdk-activating kinase (CAK) [1]. Metazoan CAK is itself a Cdk, Cdk7, whereas the CAK of Saccharomyces cerevisiae is a distinct enzyme unrelated to Cdks [1]. The Mcs6-Mcs2 complex of Schizosaccharomyces pombe is a putative CAK related to the metazoan enzyme [2] [3]. Although the loss of Mcs6 is lethal, it results in a phenotype that is inconsistent with a failure to activate Cdc2, the major Cdk in S. pombe [3]. We therefore tested the ability of Csk1, a putative regulator of Mcs6 [4], to activate Cdk-cyclin complexes in vitro. Csk1 activated both the monomeric and the Mcs2-bound forms of Mcs6. Surprisingly, Csk1 also activated Cdc2 in complexes with either Cdc13 or Cig2 cyclins. When a double mutant carrying a csk1 deletion and a temperature-sensitive mcs6 allele was incubated at the restrictive temperature, Cdc2 was not activated and the cells underwent a cell division arrest prior to mitosis. Cdc2-cyclin complexes isolated from the arrested cells could be activated in vitro by recombinant CAK, whereas complexes from wild-type cells or either of the single mutants were refractory to activation. Thus, fission yeast contains two partially redundant CAKs: the Mcs6-Mcs2 complex and Csk1. Inactivation of both CAKs is necessary and sufficient to prevent Cdc2 activation and cause a cell-cycle arrest. Mcs6, which is essential, may therefore have required functions other than Cdk activation.
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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/Adenosine Triphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/CDC2 Protein Kinase,
http://linkedlifedata.com/resource/pubmed/chemical/Csk1 protein, S pombe,
http://linkedlifedata.com/resource/pubmed/chemical/Cyclin-Dependent Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Fungal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Hemagglutinins,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Protein-Serine-Threonine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Schizosaccharomyces pombe Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/cyclin-dependent kinase-activating...
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| pubmed:status |
MEDLINE
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| pubmed:month |
Apr
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| pubmed:issn |
0960-9822
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| pubmed:author | |
| pubmed:issnType |
Print
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| pubmed:day |
22
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| pubmed:volume |
9
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
441-4
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| pubmed:dateRevised |
2009-11-19
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| pubmed:meshHeading |
pubmed-meshheading:10226032-Adenosine Triphosphate,
pubmed-meshheading:10226032-Animals,
pubmed-meshheading:10226032-CDC2 Protein Kinase,
pubmed-meshheading:10226032-Cell Cycle,
pubmed-meshheading:10226032-Cell Division,
pubmed-meshheading:10226032-Cells, Cultured,
pubmed-meshheading:10226032-Cyclin-Dependent Kinases,
pubmed-meshheading:10226032-Enzyme Activation,
pubmed-meshheading:10226032-Fungal Proteins,
pubmed-meshheading:10226032-Hemagglutinins,
pubmed-meshheading:10226032-Mutation,
pubmed-meshheading:10226032-Protein Kinases,
pubmed-meshheading:10226032-Protein-Serine-Threonine Kinases,
pubmed-meshheading:10226032-Recombinant Fusion Proteins,
pubmed-meshheading:10226032-Schizosaccharomyces,
pubmed-meshheading:10226032-Schizosaccharomyces pombe Proteins,
pubmed-meshheading:10226032-Temperature
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| pubmed:year |
1999
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| pubmed:articleTitle |
Cdc2 activation in fission yeast depends on Mcs6 and Csk1, two partially redundant Cdk-activating kinases (CAKs).
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| pubmed:affiliation |
Cell Biology Program, Memorial Sloan-Kettering Cancer Center, 1275 York Avenue, New York, New York 10021, USA.
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| pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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