Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 278, Issue 3, Pages 1986-1990Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.C200634200
Keywords
-
Categories
Funding
- NCI NIH HHS [CA84472, CA88898, CA64239] Funding Source: Medline
- NIEHS NIH HHS [K08 ES00356] Funding Source: Medline
- NIGMS NIH HHS [GM23750] Funding Source: Medline
Ask authors/readers for more resources
Nuclear receptor coactivator PRIP (peroxisome proliferator-activated receptor (PPARgamma)-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 (PPARgamma-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 a and to a lesser effect on PPARgamma transcriptional activity. These observations indicate that PRIP like PBP, CBP, and p300 is an essential and nonredundant coactivator.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available