β3-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 β3-endonexin, a molecule known to associate with the integrin β3 cytoplasmic domain, specifically binds cyclin A. Deletion of the amino-te...
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Published in | Biochemical and biophysical research communications Vol. 267; no. 3; pp. 947 - 952 |
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Main Authors | , , , , , |
Format | Journal Article |
Language | English |
Published |
Elsevier Inc
27.01.2000
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Subjects | |
Online Access | Get full text |
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Summary: | 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 β3-endonexin, a molecule known to associate with the integrin β3 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 β3-endonexin to interact with cyclin A. In an in vitro kinase assay, β3-endonexin inhibits pRB kinase activity associated with cyclin A-Cdk2 while leaving its histone H1 kinase activity unaffected. Coexpression of β3-endonexin in yeast cells overcomes growth suppression caused by an activation of cyclin A-associated kinase. Our results indicate that β3-endonexin is a novel cyclin A-binding molecule that regulates cyclin A-associated pRB kinase activity. |
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ISSN: | 0006-291X 1090-2104 |
DOI: | 10.1006/bbrc.1999.2007 |