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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
11
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pubmed:dateCreated |
2003-3-10
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pubmed:abstractText |
The capacity of the cyclin D-dependent kinase to promote G(1) progression through modulation of RB.E2F is well documented. We now demonstrate that the cyclin D1/CDK4 kinase binds to components of the MCM complex. MCM7 and MCM3 were identified as cyclin D1-binding proteins. Catalytically active cyclin D1/CDK4 complexes were incorporated into chromatin-bound protein complexes with the same kinetics as MCM7 and MCM3, where they associated specifically with MCM7. Although the cyclin D1-dependent kinase did not phosphorylate MCM7, active cyclin D1/CDK4, but not cyclin E/CDK2, did catalyze the dissociation of an RB.MCM7 complex. Finally, expression of an active D1/CDK4 kinase but not cyclin E/CDK2 promoted the removal of RB from chromatin-bound protein complexes. Our data suggest that D1/CDK4 complexes play a direct role in altering an inhibitory RB.MCM7 complex possibly allowing for setting of the origin in preparation for DNA replication.
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pubmed:grant |
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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/Cdk4 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Cell Cycle Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Chromatin,
http://linkedlifedata.com/resource/pubmed/chemical/Cyclin D,
http://linkedlifedata.com/resource/pubmed/chemical/Cyclin D1,
http://linkedlifedata.com/resource/pubmed/chemical/Cyclin-Dependent Kinase 4,
http://linkedlifedata.com/resource/pubmed/chemical/Cyclin-Dependent Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Cyclins,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Complementary,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Mcm7 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Retinoblastoma Protein
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
14
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pubmed:volume |
278
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
9754-60
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:12519773-3T3 Cells,
pubmed-meshheading:12519773-Animals,
pubmed-meshheading:12519773-Catalysis,
pubmed-meshheading:12519773-Cell Cycle Proteins,
pubmed-meshheading:12519773-Cell Line,
pubmed-meshheading:12519773-Chromatin,
pubmed-meshheading:12519773-Cyclin D,
pubmed-meshheading:12519773-Cyclin D1,
pubmed-meshheading:12519773-Cyclin-Dependent Kinase 4,
pubmed-meshheading:12519773-Cyclin-Dependent Kinases,
pubmed-meshheading:12519773-Cyclins,
pubmed-meshheading:12519773-DNA, Complementary,
pubmed-meshheading:12519773-DNA-Binding Proteins,
pubmed-meshheading:12519773-Insects,
pubmed-meshheading:12519773-Kinetics,
pubmed-meshheading:12519773-Mice,
pubmed-meshheading:12519773-Microscopy, Fluorescence,
pubmed-meshheading:12519773-Nuclear Proteins,
pubmed-meshheading:12519773-Phosphorylation,
pubmed-meshheading:12519773-Precipitin Tests,
pubmed-meshheading:12519773-Protein Binding,
pubmed-meshheading:12519773-Protein Structure, Tertiary,
pubmed-meshheading:12519773-Proto-Oncogene Proteins,
pubmed-meshheading:12519773-Retinoblastoma Protein,
pubmed-meshheading:12519773-Time Factors,
pubmed-meshheading:12519773-Transfection,
pubmed-meshheading:12519773-Two-Hybrid System Techniques
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pubmed:year |
2003
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pubmed:articleTitle |
The cyclin D1-dependent kinase associates with the pre-replication complex and modulates RB.MCM7 binding.
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pubmed:affiliation |
Leonard and Madlyn Abramson Family Cancer Research Institute, Department of Cancer Biology, Abramson Family Cancer Center of the University of Pennsylvania, Philadelphia, Pennsylvania 19104, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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