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rdf:type |
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lifeskim:mentions |
umls-concept:C0205314,
umls-concept:C0249197,
umls-concept:C0288472,
umls-concept:C0439849,
umls-concept:C0445223,
umls-concept:C0598086,
umls-concept:C0598388,
umls-concept:C0679622,
umls-concept:C1150527,
umls-concept:C1415887,
umls-concept:C1419040,
umls-concept:C1420433,
umls-concept:C1420626,
umls-concept:C1424666,
umls-concept:C1552599,
umls-concept:C1704787,
umls-concept:C1999216
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pubmed:issue |
1
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pubmed:dateCreated |
1994-8-17
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pubmed:databankReference |
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pubmed:abstractText |
Using a yeast interaction screen to search for proteins that interact with cyclin D1-Cdk4, we identified a 27 kDa mouse protein related to the p21 cyclin-Cdk inhibitor. p27 interacts strongly with D-type cyclins and Cdk4 in vitro and more weakly with cyclin E and Cdk2. In mouse fibroblasts, p27 is associated predominantly with cyclin D1-Cdk4. Recombinant p27 is a potent inhibitor of cyclin D1-Cdk4 and cyclin A-Cdk2 protein kinase activity and a weaker inhibitor of cyclin B1-Cdc2. Overexpression of p27 in Saos-2 cells causes G1 arrest. p27 protein levels do not change as serum-stimulated quiescent mouse fibroblasts progress through the cell cycle. p27 is identical to p27Kip1, a cyclin-Cdk inhibitor present in TGF beta-treated cells. p27 has the hallmarks of a negative regulator of G1 progression and may mediate TGF beta-induced G1 arrest.
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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/CDC2-CDC28 Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Cdk2 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Cdk4 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Cdkn1b protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Cell Cycle Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Cyclin D1,
http://linkedlifedata.com/resource/pubmed/chemical/Cyclin-Dependent Kinase 2,
http://linkedlifedata.com/resource/pubmed/chemical/Cyclin-Dependent Kinase 4,
http://linkedlifedata.com/resource/pubmed/chemical/Cyclin-Dependent Kinase Inhibitor...,
http://linkedlifedata.com/resource/pubmed/chemical/Cyclin-Dependent Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Cyclins,
http://linkedlifedata.com/resource/pubmed/chemical/Fungal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Microtubule-Associated Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Oncogene Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinase Inhibitors,
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/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Tumor Suppressor Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0092-8674
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
78
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
67-74
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:8033213-3T3 Cells,
pubmed-meshheading:8033213-Amino Acid Sequence,
pubmed-meshheading:8033213-Animals,
pubmed-meshheading:8033213-Base Sequence,
pubmed-meshheading:8033213-CDC2-CDC28 Kinases,
pubmed-meshheading:8033213-Cell Cycle,
pubmed-meshheading:8033213-Cell Cycle Proteins,
pubmed-meshheading:8033213-Cell Line,
pubmed-meshheading:8033213-Cloning, Molecular,
pubmed-meshheading:8033213-Cyclin D1,
pubmed-meshheading:8033213-Cyclin-Dependent Kinase 2,
pubmed-meshheading:8033213-Cyclin-Dependent Kinase 4,
pubmed-meshheading:8033213-Cyclin-Dependent Kinase Inhibitor p27,
pubmed-meshheading:8033213-Cyclin-Dependent Kinases,
pubmed-meshheading:8033213-Cyclins,
pubmed-meshheading:8033213-Fungal Proteins,
pubmed-meshheading:8033213-G1 Phase,
pubmed-meshheading:8033213-Gene Expression Regulation,
pubmed-meshheading:8033213-Mice,
pubmed-meshheading:8033213-Microtubule-Associated Proteins,
pubmed-meshheading:8033213-Molecular Sequence Data,
pubmed-meshheading:8033213-Oncogene Proteins,
pubmed-meshheading:8033213-Open Reading Frames,
pubmed-meshheading:8033213-Protein Kinase Inhibitors,
pubmed-meshheading:8033213-Protein-Serine-Threonine Kinases,
pubmed-meshheading:8033213-Proto-Oncogene Proteins,
pubmed-meshheading:8033213-RNA, Messenger,
pubmed-meshheading:8033213-Recombinant Fusion Proteins,
pubmed-meshheading:8033213-Sequence Analysis, DNA,
pubmed-meshheading:8033213-Tumor Suppressor Proteins,
pubmed-meshheading:8033213-Yeasts
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pubmed:year |
1994
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pubmed:articleTitle |
p27, a novel inhibitor of G1 cyclin-Cdk protein kinase activity, is related to p21.
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pubmed:affiliation |
Molecular Biology and Virology Laboratory, Salk Institute, La Jolla, California 92037.
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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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