PPAR-gamma AF-2 domain functions as a component of a ubiquitin-dependent degradation signal.

ABSTRACT: The nuclear hormone receptor peroxisome proliferator-activated receptor-gamma (PPAR-gamma) functions as the "master switch" in adipocyte development and is important in regulating glucose metabolism. PPAR-gamma is rapidly degraded in adipocytes by the ubiquitin proteasome pathway under basal and ligand-activated conditions. Proteasome inhibition increases PPAR-gamma activity, indicating disposal of PPAR-gamma by the ubiquitin proteasome system regulates PPAR-gamma activity. However, the signals and factors required for recognition of PPAR-gamma by the ubiquitin proteasome pathway are unknown. To begin understanding how the ubiquitin-proteasome pathway interacts with PPAR-gamma, we designed a series of constructs containing each PPAR-gamma domain expressed as a fusion protein with the GAL4

SUBMITTER: Kilroy GE 

PROVIDER: S-EPMC2750041 | biostudies-literature | 2009 Apr

REPOSITORIES: biostudies-literature