Coactivator PRIP, the peroxisome proliferator-activated receptor-interacting protein, is a modulator of placental, cardiac, hepatic, and embryonic development

Yi Jun Zhu, Susan E. Crawford, Veronica Stellmach, Rama S. Dwivedi, M. Sambasiva Rao, Frank J. Gonzalez, Chao Qi, Janardan K. Reddy*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

61 Scopus citations

Abstract

Nuclear receptor coactivator PRIP (peroxisome proliferator-activated receptor (PPARγ)-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 (PPARγ-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 α and to a lesser effect on PPARγ transcriptional activity. These observations indicate that PRIP like PBP, CBP, and p300 is an essential and nonredundant coactivator.

Original languageEnglish (US)
Pages (from-to)1986-1990
Number of pages5
JournalJournal of Biological Chemistry
Volume278
Issue number3
DOIs
StatePublished - Jan 17 2003

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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