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J Biol Chem, Vol. 275, Issue 19, 14295-14306, May 12, 2000

Identification and Characterization of CKIP-1, a Novel Pleckstrin Homology Domain-containing Protein That Interacts with Protein Kinase CK2*

Denis G. BoscDagger , Kevin C. Graham§, Ronald B. Saulnier§, Cunjie Zhang§||, David ProberDagger , R. Daniel Gietz**, and David W. Litchfield§Dagger Dagger

From the § Department of Biochemistry, University of Western Ontario, London, Ontario N6A 5C1, the Dagger  Manitoba Institute of Cell Biology, Winnipeg, Manitoba R3E 0V9, and the ** Department of Biochemistry and Medical Genetics, University of Manitoba, Winnipeg, Manitoba R3E 0W3, Canada

The catalytic subunits of protein kinase CK2, CK2alpha and CK2alpha ', are closely related to each other but exhibit functional specialization. To test the hypothesis that specific functions of CK2alpha and CK2alpha ' are mediated by specific interaction partners, we used the yeast two-hybrid system to identify CK2alpha - or CK2alpha '-binding proteins. We report the identification and characterization of a novel CK2-interacting protein, designated CKIP-1, that interacts with CK2alpha , but not CK2alpha ', in the yeast two-hybrid system. CKIP-1 also interacts with CK2alpha in vitro and is co-immunoprecipitated from cell extracts with epitope-tagged CK2alpha and an enhanced green fluorescent protein fusion protein encoding CKIP-1 (i.e. EGFP-CKIP-1) when they are co-expressed. CK2 activity is detected in anti-CKIP-1 immunoprecipitates performed with extracts from non-transfected cells indicating that CKIP-1 and CK2 interact under physiological conditions. The CKIP-1 cDNA is broadly expressed and encodes a protein with a predicted molecular weight of 46,000. EGFP-CKIP-1 is localized within the nucleus and at the plasma membrane. The plasma membrane localization is dependent on the presence of an amino-terminal pleckstrin homology domain. We postulate that CKIP-1 is a non-enzymatic regulator of one isoform of CK2 (i.e. CK2alpha ) with a potential role in targeting CK2alpha to a particular cellular location.

* This work was supported by grants from the National Cancer Institute of Canada with funds from the Canadian Cancer Society and from the Terry Fox Foundation raised through the Terry Fox Run (to D. W. L.).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.

Supported by a fellowship from the Faculty of Medicine at the University of Western Ontario with funds from the Cancer Research Society.

|| Supported by the Premier's Research Excellence Award Program.

Dagger Dagger To whom correspondence should be addressed: Dept. of Biochemistry, Health Sciences Centre, University of Western Ontario, London, Ontario N6A 5C1, Canada. Tel.: 519-661-4186; Fax: 519-661-3175; E-mail: litchfi@julian.uwo.ca.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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