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The p21 Cdk-interacting protein Cip1 is a potent inhibitor of G1 cyclin-dependent kinases.

Cell | Nov 19, 1993

The cyclin-dependent kinase Cdk2 associates with cyclins A, D, and E and has been implicated in the control of the G1 to S phase transition in mammals. To identify potential Cdk2 regulators, we have employed an improved two-hybrid system to isolate human genes encoding Cdk-interacting proteins (Cips). CIP1 encodes a novel 21 kd protein that is found in cyclin A, cyclin D1, cyclin E, and Cdk2 immunoprecipitates. p21CIP1 is a potent, tight-binding inhibitor of Cdks and can inhibit the phosphorylation of Rb by cyclin A-Cdk2, cyclin E-Cdk2, cyclin D1-Cdk4, and cyclin D2-Cdk4 complexes. Cotransfection experiments indicate that CIP1 and SV40 T antigen function in a mutually antagonistic manner to control cell cycle progression.

Pubmed ID: 8242751 RIS Download

Mesh terms: Amino Acid Sequence | Antigens, Polyomavirus Transforming | Base Sequence | CDC2-CDC28 Kinases | Cell Cycle | Cloning, Molecular | Cyclin-Dependent Kinase 2 | Cyclin-Dependent Kinase Inhibitor p21 | Cyclin-Dependent Kinases | Cyclins | Humans | Molecular Sequence Data | Phosphorylation | Protein Binding | Protein Kinase Inhibitors | Protein-Serine-Threonine Kinases | Recombinant Proteins | Retinoblastoma Protein

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Associated grants

  • Agency: NIA NIH HHS, Id: AG-11085
  • Agency: NIA NIH HHS, Id: R01-AG 11066

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