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p27, a novel inhibitor of G1 cyclin-Cdk protein kinase activity, is related to p21.

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Affiliations

  • 1. Molecular Biology and Virology Laboratory, Salk Institute, La Jolla, California 92037.
      Authors
    • Toyoshima H 1
    (1 author)

Cell, 01 Jul 1994, 78(1):67-74
https://doi.org/10.1016/0092-8674(94)90573-8 PMID: 8033213 

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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NCI NIH HHS (2)