P27, A NOVEL INHIBITOR OF G1 CYCLIN-CDK PROTEIN-KINASE ACTIVITY, IS RELATED TO P21
P27, A NOVEL INHIBITOR OF G1 CYCLIN-CDK PROTEIN-KINASE ACTIVITY, IS RELATED TO P21
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DOI:
10.1016/0092-8674(94)90573-8
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发表时间:
1994-07-15
期刊:
影响因子:
64.5
通讯作者:
HUNTER, T
中科院分区:
文献类型:
--
作者:
TOYOSHIMA, H;HUNTER, T
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 p27(Kip1), 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.