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J. Biol. Chem., Vol. 279, Issue 40, 42114-42127, October 1, 2004

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The Pleckstrin Homology Domain of CK2 Interacting Protein-1 Is Required for Interactions and Recruitment of Protein Kinase CK2 to the Plasma Membrane^*

Mary Ellen K. Olsten, David A. Canton¶, Cunjie Zhang||, Paul A. Walton**, and David W. Litchfield

From the Departments of Biochemistry and ^**Anatomy and Cell Biology, University of Western Ontario, London, Ontario N6A 5C1, Canada

CKIP-1 is a recently identified interaction partner of protein kinase CK2 with a number of protein-protein interaction motifs, including an N-terminal pleckstrin homology domain. To test the hypothesis that CKIP-1 has a role in targeting CK2 to specific locations, we examined the effects of CKIP-1 on the localization of CK2. These studies demonstrated that CKIP-1 can recruit CK2 to the plasma membrane. Furthermore, the pleckstrin homology domain of CKIP-1 was found to be required for interactions with CK2 and for the recruitment of CK2 to the plasma membrane. In this regard, point mutations in this domain abolish membrane localization and compromise interactions with CK2. In addition, replacement of the pleckstrin homology domain with a myristoylation signal was insufficient to elicit any interaction with CK2. An investigation of the lipid binding of CKIP-1 reveals that it has broad specificity. A comparison with other pleckstrin homology domains revealed that the pleckstrin homology domain of CKIP-1 is distinct from other defined classes of pleckstrin homology domains. Finally, examination of CK2 for a region that mediates interactions with CKIP-1 revealed a putative HIKE domain, a complex motif found exclusively in proteins that bind pleckstrin homology domains. However, mutations within this motif were not able to abolish CKIP-1-CK2 interactions suggesting that this motif by itself may not be sufficient to mediate interactions. Overall, these results provide novel insights into how CK2, a predominantly nuclear enzyme, is targeted to the plasma membrane, and perhaps more importantly how it may be regulated.

Received for publication, July 7, 2004

^* This work was supported in part by an operating grant from the Canadian Institutes of Health Research (Grant 37854). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Supported by an Ontario Graduate Scholarship in Science and Technology.

^¶ Supported by a Graduate Scholarship from the National Science and Engineering Research Council.

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

To whom correspondence should be addressed: Dept. of Biochemistry, Siebens Drake Research Institute, University of Western Ontario, London, Ontario N6A 5C1, Canada. Tel.: 519-661-4186; Fax: 519-661-3175; E-mail: litchfi{at}uwo.ca.

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