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PMID:8033213

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Citation

Toyoshima, H and Hunter, T (1994) p27, a novel inhibitor of G1 cyclin-Cdk protein kinase activity, is related to p21. Cell 78:67-74

Abstract

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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Keywords

3T3 Cells; Amino Acid Sequence; Animals; Base Sequence; CDC2-CDC28 Kinases; Cell Cycle/drug effects; Cell Cycle Proteins; Cell Line; Cloning, Molecular; Cyclin D1; Cyclin-Dependent Kinase 2; Cyclin-Dependent Kinase 4; Cyclin-Dependent Kinase Inhibitor p27; Cyclin-Dependent Kinases; Cyclins/genetics; Cyclins/metabolism; Fungal Proteins/genetics; Fungal Proteins/metabolism; Fungal Proteins/pharmacology; G1 Phase/drug effects; Gene Expression Regulation; Mice; Microtubule-Associated Proteins/genetics; Microtubule-Associated Proteins/metabolism; Microtubule-Associated Proteins/pharmacology; Molecular Sequence Data; Oncogene Proteins/genetics; Oncogene Proteins/metabolism; Open Reading Frames; Protein Kinase Inhibitors; Protein-Serine-Threonine Kinases; Proto-Oncogene Proteins; RNA, Messenger/analysis; Recombinant Fusion Proteins/metabolism; Sequence Analysis, DNA; Tumor Suppressor Proteins; Yeasts/metabolism

Significance

Annotations

Gene product Qualifier GO ID GO term name Evidence Code with/from Aspect Notes Status


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