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Published on: November 15, 2013
PRIC295, a Nuclear Receptor Coactivator, Identified from PPARα-Interacting Cofactor Complex
Sean R Pyper1, Navin Viswakarma, Yuzhi Jia
1Department of Pathology, Feinberg School of Medicine, Northwestern University, Chicago, IL 60611, USA.
PPAR Research
|October 2, 2010
Summary
Researchers discovered PRIC295, a novel coactivator protein that interacts with PPARα and Mediator complex subunits. PRIC295 enhances nuclear receptor activity, potentially playing a key role in lipid metabolism and energy combustion regulation.
Area of Science:
- Molecular Biology
- Cellular Biology
- Biochemistry
Background:
- Peroxisome proliferator-activated receptor-α (PPARα) is crucial for lipid metabolism and energy combustion.
- Chronic PPARα activation in rodents is linked to hepatocellular carcinomas.
- PPARα gene expression relies on the Mediator complex, specifically subunit 1 (Med1).
Purpose of the Study:
- To identify and characterize novel coactivator proteins interacting with PPARα.
- To investigate the role of PRIC295 in nuclear receptor-mediated transcription.
Main Methods:
- Protein identification and characterization.
- Co-immunoprecipitation assays to study protein interactions.
- In vitro transactivation assays to assess coactivator function.
Main Results:
- PRIC295, a novel coactivator, was identified and characterized.
- PRIC295 interacts with Med1 and Med24 subunits of the Mediator complex.
- PRIC295 contains 10 LXXLL motifs, binds PPARα and other nuclear receptors ligand-dependently, and enhances their transactivation function.
Conclusions:
- PRIC295 acts as a transcription coactivator for nuclear receptors, including PPARα.
- PRIC295 may be part of the PRIC complex with Med1 and Med24, influencing gene expression in vivo.
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