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Originally published In Press as doi:10.1074/jbc.M001323200 on May 23, 2000

J. Biol. Chem., Vol. 275, Issue 34, 26172-26177, August 25, 2000
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Functional Cloning and Characterization of a Novel Nonhomeodomain Protein That Inhibits the Binding of PBX1-HOX Complexes to DNA*

Carolina AbramovichDagger §, Wei-Feng Shen, Nicolas PineaultDagger , Suzan ImrenDagger , Ben MontpetitDagger , Corey Largman, and R. Keith HumphriesDagger ||**

From Dagger  The Terry Fox Laboratory, British Columbia Cancer Agency, Vancouver, British Columbia V5Z 1L3, Canada, the  Department of Medicine, San Francisco Veterans Affairs Medical Center and University of California, San Francisco, California 94121, and the || Department of Medicine, University of British Columbia, Vancouver, British Columbia V6T 2B5, Canada

PBX1 is a homeodomain protein that functions in complexes with other homeodomain-containing proteins to regulate gene expression during developmental and/or differentiation processes. A yeast two-hybrid screen of a fetal liver-hematopoietic cDNA library using PBX1a as bait led to the discovery of a novel non-homeodomain-containing protein that interacts with PBX1 as well as PBX2 and PBX3. RNA analysis revealed it to be expressed in CD34+ hematopoietic cell populations enriched in primitive progenitors, as is PBX1; search of the expressed sequence tag data base indicated that it is also expressed in other early embryonic as well as adult tissues. The full-length cDNA encodes a 731-amino acid protein that has no significant homology to known proteins. This protein that we have termed hematopoietic PBX-interacting protein (HPIP) is mainly localized in the cytosol and in small amounts in the nucleus. The region of PBX that interacts with HPIP includes both the homeodomain and immediate N-terminal flanking sequences. Strikingly, electrophoretic mobility shift assays revealed that HPIP inhibits the ability of PBX-HOX heterodimers to bind to target sequences. Moreover, HPIP strongly inhibits the transactivation activity of E2A-PBX. Together these findings suggest that HPIP is a new regulator of PBX function.

* This work was supported by the National Cancer Institute of Canada with funds from the Canadian Cancer Society and The Terry Fox Run, the Medical Research Council of Canada (MRC-C), National Institutes of Health Grant DK48642, and the Department of Veterans Affairs (to C. 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.

§ Recipient of fellowships from the Leukemia Research Society of Canada and MRC-C.

** To whom correspondence should be addressed: Terry Fox Laboratory, 601 W. 10th Avenue, Vancouver, BC V5Z 1L3, Canada. Tel.: 604-877-6070 (ext. 3095); Fax: 604-877-0712; E-mail: keith@ terryfox.ubc.ca.

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