p27, a novel inhibitor of G1 cyclin-Cdk protein kinase activity, is related to p21.
basic_science · Level V
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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.
Medical subject headings
- CDC2-CDC28 Kinases
- Cell Cycle Proteins
- Cyclin-Dependent Kinases
- Cyclins
- Fungal Proteins
- G1 Phase
- Microtubule-Associated Proteins
- Protein Kinase Inhibitors
- Protein Serine-Threonine Kinases
- Proto-Oncogene Proteins
- Tumor Suppressor Proteins