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Papers In Press, published online ahead of print May 16, 2003
Pathology, Northwestern University , The Feinberg School of Medicine, Chicago, Illinois 60611
Corresponding Author: jkreddy{at}northwestern.edu
Nuclear receptor coactivator PRIP (peroxisome proliferators-activated receptor (PPARg)-interacting protein) appears to serve as a linker between cAMP response element-binding protein-binding protein (CBP/p300)-anchored and PBP (PPARg-binding protein)-anchored coactivator complexes involved in the transcriptional activity of nuclear receptors. Disruption of PRIP and PBP genes results in embryonic lethality between embryonic day 11.5 and 12.5 (postcoitum) indicating that PRIP and PBP are essential and nonredundant coactivators. Both PRIP and PBP were initially identified as PPARg coactivators suggesting a role for these molecules in PPARg-induced adipogenesis. PBP-/- mouse embryonic fibroblasts fail to exhibit PPAR1-stimulated adipogenesis indicating that PBP is a downstream regulator of PPARg-mediated adipogenesis. We now show that PRIP-/- mouse embryonic fibroblasts are also refractory to PPARg- stimulated adipogenesis and fail to express adipogenic marker aP2, a PPARg responsive gene. Chromatin immunoprecipitation assays reveal reduced association in PRIP-/- cells of PIMT (PRIP-binding protein) and PBP with aP2 gene promoter, suggesting that PRIP is required for the linking of CBP/p300-anchored cofactor complex with PBP-anchored mediator complex. These data indicate that PRIP, like PBP, is a downstream regulator of PPARg-mediated adipogenesis and that both these coactivators are required for the successful completion of adipogenic program.
J. Biol. Chem, 10.1074/jbc.C300175200
Submitted on April 23, 2003
Revised on May 16, 2003
Accepted on May 16, 2003
Transcriptional coactivator PRIP, the peroxisome proliferator-activated receptor g (PPARg)-interacting protein, is required for PPARg-mediated adipogenesis
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