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Originally published In Press as doi:10.1074/jbc.M206427200 on November 20, 2002

J. Biol. Chem., Vol. 278, Issue 7, 5062-5071, February 14, 2003
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The p34cdc2-related Cyclin-dependent kinase 11 Interacts with the p47 Subunit of Eukaryotic Initiation Factor 3 during Apoptosis*

Jiaqi ShiDagger , Yongmei FengDagger , Anne-Christine GouletDagger , Richard R. Vaillancourt§, Nancy A. Sachs§, John W. Hershey, and Mark A. NelsonDagger ||

From the Dagger  Department of Pathology, Arizona Cancer Center, and the § Department of Pharmacology/Toxicology, University of Arizona, Tucson, Arizona 85724 and the  Department of Biological Chemistry, School of Medicine, University of California, Davis, California 95616

Cyclin-dependent kinase 11 (CDK11; also named PITSLRE) is part of the large family of p34cdc2-related kinases whose functions appear to be linked with cell cycle progression, tumorigenesis, and apoptotic signaling. However, substrates of CDK11 during apoptosis have not been identified. We used a yeast two-hybrid screening strategy and identified eukaryotic initiation factor 3 p47 protein (eIF3 p47) as an interacting partner of caspase-processed C-terminal kinase domain of CDK11 (CDK11p46). We demonstrate that the eIF3 p47 can interact with CDK11 in vitro and in vivo, and the interaction can be strengthened by stimulation of apoptosis. EIF3 p47 contains a Mov34/JAB domain and appears to interact with CDK11p46 through this motif. We show in vitro that the caspase-processed CDK11p46 can phosphorylate eIF3 p47 at a specific serine residue (Ser46) and that eIF3 p47 is phosphorylated in vivo during apoptosis. Purified recombinant CDK11p46 inhibited translation of a reporter gene in vitro in a dose-dependent manner. In contrast, a kinase-defective mutant CDK11p46M did not inhibit translation of the reporter gene. Stable expression of CDK11p46 in vivo inhibited the synthesis of a transfected luciferase reporter protein and overall cellular protein synthesis. These data provide insight into the cellular function of CDK11 during apoptosis.

* This work was supported by National Institutes of Health Grants CA70145 (to M. N.) and ES066694 and CA 23074 (to the Arizona Cancer Center).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

|| To whom correspondence should be addressed: Arizona Cancer Center, 1515 N. Campbell Ave., Tucson, AZ 85724. Tel.: 520-626-2619; Fax: 520-626-1027; E-mail: mnelson@azcc.arizona.edu.

Copyright © 2003 by The American Society for Biochemistry and Molecular Biology, Inc.
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