beta3-endonexin as a novel inhibitor of cyclin A-associated kinase.
Cyclin A is indispensable for S phase cell cycle progression and is suggested to be a crucial target of cell adhesion signals. In this study, we demonstrate that beta3-endonexin, a molecule known to associate with the integrin beta3 cytoplasmic domain, specifically binds cyclin A. Deletion of the amino-terminal 52-amino-acid residues ... including the cyclin-binding RxL motif abolishes the ability of beta3-endonexin to interact with cyclin A. In an in vitro kinase assay, beta3-endonexin inhibits pRB kinase activity associated with cyclin A-Cdk2 while leaving its histone H1 kinase activity unaffected. Coexpression of beta3-endonexin in yeast cells overcomes growth suppression caused by an activation of cyclin A-associated kinase. Our results indicate that beta3-endonexin is a novel cyclin A-binding molecule that regulates cyclin A-associated pRB kinase activity.
Mesh Terms:
Animals, COS Cells, Cell Cycle, Cyclin A, Escherichia coli, Kinetics, Nuclear Proteins, Protein Kinase Inhibitors, Protein Kinases, Proteins, Recombinant Fusion Proteins, Recombinant Proteins, Saccharomyces cerevisiae, Sequence Deletion, Transfection, beta-Galactosidase
Animals, COS Cells, Cell Cycle, Cyclin A, Escherichia coli, Kinetics, Nuclear Proteins, Protein Kinase Inhibitors, Protein Kinases, Proteins, Recombinant Fusion Proteins, Recombinant Proteins, Saccharomyces cerevisiae, Sequence Deletion, Transfection, beta-Galactosidase
Biochem. Biophys. Res. Commun.
Date: Jan. 27, 2000
PubMed ID: 10673397
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