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Originally published In Press as doi:10.1074/jbc.C000121200 on March 15, 2000
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J Biol Chem, Vol. 275, Issue 20, 14779-14782, May 19, 2000

ACCELERATED PUBLICATION
Deletion of PBP/PPARBP, the Gene for Nuclear Receptor Coactivator Peroxisome Proliferator-activated Receptor-binding Protein, Results in Embryonic Lethality*

Yijun Zhu, Chao Qi, Yuzhi Jia, Jeffrey S. Nye, M. Sambasiva Rao, and Janardan K. ReddyDagger

From the Department of Pathology, Northwestern University Medical School, Chicago, Illinois 60611

We previously isolated and identified peroxisome proliferator-activated receptor (PPAR)-binding Protein (PBP) as a coactivator for PPARgamma . PBP has recently been identified as a component of the multiprotein complexes such as TRAP, DRIP, and ARC that appear to play an important role in the transcriptional activation by several transcriptional factors including nuclear receptors. To assess the biological significance of PBP, we disrupted the PBP gene (PBP/PPARBP) in mice by homologous recombination. PBP+/- mice are healthy, fertile, and do not differ significantly from PBP+/+ control littermates. PBP null mutation (PBP-/-) is embryonically lethal at embryonic day 11.5, suggesting that PBP is an essential gene for mouse embryogenesis. The embryonic lethality is attributed, in part, to defects in the development of placental vasculature similar to those encountered in PPARgamma mutants. Transient transfection assays using fibroblasts isolated from PBP mutant embryos revealed a decreased capacity for ligand-dependent transcriptional activation of PPARgamma as compared with fibroblasts derived form the wild type embryos. These observations suggest that there is no functional redundancy between PBP and other coactivators such as steroid receptor coactivator-1 and that PBP plays a critical role in the signaling of PPARgamma and other nuclear receptors.

* This work was supported by National Institutes of Health Grant R37 GM23750 (to J. K. R.), a Department of Veterans Affairs merit review grant (to M. S. R.), and by the Joseph L. Mayberry, Sr. Endowment Fund.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.

Dagger To whom correspondence should be addressed: Dept. of Pathology, Northwestern University Medical School, 303 East Chicago Ave., Chicago, IL 60611. Tel.: 312-503-7948; Fax: 312-503-8249; E-mail: jkreddy@nwu.edu.

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