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Originally published In Press as doi:10.1074/jbc.M100768200 on February 20, 2001

J. Biol. Chem., Vol. 276, Issue 20, 16848-16856, May 18, 2001
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The Binding of Ku Antigen to Homeodomain Proteins Promotes Their Phosphorylation by DNA-dependent Protein Kinase*

Caroline Schild-PoulterDagger §, Louise PopeDagger , Ward GiffinDagger , Jeff C. KochanDagger , Johnny K. NgseeDagger , Maya Traykova-AndonovaDagger , and Robert J. G. HachéDagger ||**

From the Departments of Dagger  Medicine,  Cellular and Molecular Medicine, and || Biochemistry, Microbiology and Immunology, The Loeb Health Research Institute at the Ottawa Hospital, University of Ottawa, Ottawa, Ontario K1Y 4E9, Canada

The Ku antigen (70- and 80-kDa subunits) is a regulatory subunit of DNA-dependent protein kinase (DNA-PK) that promotes the recruitment of the catalytic subunit of DNA-PK (DNA-PKcs) to DNA ends and to specific DNA sequences from which the kinase is activated. Ku and DNA-PKcs plays essential roles in double-stranded DNA break repair and V(D)J recombination and have been implicated in the regulation of specific gene transcription. In a yeast two-hybrid screen of a Jurkat T cell cDNA library, we have identified a specific interaction between the 70-kDa subunit of Ku heterodimer and the homeodomain of HOXC4, a homeodomain protein expressed in the hematopoietic system. Unexpectedly, a similar interaction with Ku was observed for several additional homeodomain proteins including octamer transcription factors 1 and 2 and Dlx2, suggesting that specific binding to Ku may be a property shared by many homeodomain proteins. Ku-homeodomain binding was mediated through the extreme C terminus of Ku70 and was abrogated by amino acid substitutions at Lys595/Lys596. Ku binding allowed the recruitment of the homeodomain to DNA ends and dramatically enhanced the phosphorylation of homeodomain-containing proteins by DNA-PK. These results suggest that Ku functions as a substrate docking protein for signaling by DNA-PK to homeodomain proteins from DNA ends.

* This work was supported by an operating grant from the Arthritis Society of Canada (to R. J. G. H.).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.

§ Recipient of a Postdoctoral Fellowship from the Canadian Institutes of Health Research and the Arthritis Society of Canada.

** An investigator of the Canadian Institutes of Health Research. To whom correspondence should be addressed: The Loeb Health Research Institute at the Ottawa Hospital, 725 Parkdale Ave., Ottawa, Ontario, Canada K1Y 4K9. Tel.: 613-798-5555 (ext. 16283); Fax: 613-761-5036; E-mail: rhache@lri.ca.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.


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