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J. Biol. Chem., Vol. 278, Issue 3, 1986-1990, January 17, 2003
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From the Nuclear receptor coactivator PRIP (peroxisome
proliferator-activated receptor (PPAR
Coactivator PRIP, the Peroxisome Proliferator-activated
Receptor-interacting Protein, Is a Modulator of Placental, Cardiac,
Hepatic, and Embryonic Development*
,,,,, and
Departments of Pathology and
§ Pediatrics, Northwestern University, the Feinberg School
of Medicine, Chicago, Illinois 60611-3008 and ¶ The Laboratory of
Metabolism, NCI, National Institutes of Health,
Bethesda, Maryland 20892
)-interacting protein) and
PRIP-interacting protein with methyltransferase activity, designated
PIMT, appear to serve as linkers between cAMP response element-binding
protein-binding protein (CBP)/p300-anchored and PBP (PPAR-binding
protein)-anchored coactivator complexes involved in the transcriptional
activity of nuclear receptors. To assess the biological significance of PRIP, we disrupted the PRIP gene in mice by homologous recombination. Mice nullizygous for PRIP died between embryonic day 11.5 and 12.5 (postcoitum) due in most part to defects in the development of
placenta, heart, liver, nervous system, and retardation of embryonic
growth. Transient transfection assays using fibroblasts isolated from
PRIP
/ embryos revealed a significant decrease in
the capacity for ligand-dependent transcriptional
activation of retinoid X receptor 
and to a lesser effect on
PPAR transcriptional activity. These observations indicate that PRIP
like PBP, CBP, and p300 is an essential and nonredundant coactivator.
*
This work was supported by National Institutes of Health
Grants K08 ES00356 and CA88898 (to Y.-J. Z.), CA64239 (to S. E. C.), CA84472 (to M. S. R.), and GM23750 (to J. K. 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.
To whom correspondence should be addressed: Dept. of
Pathology, Northwestern University, the Feinberg School of Medicine, 303 East Chicago Ave., Chicago, IL 60611-3008. Tel.: 312-503-8144; Fax:
312-503-8249; E-mail: jkreddy@northwestern.edu.
Copyright © 2003 by The American Society for Biochemistry and Molecular Biology, Inc.
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