Peroxisome Proliferator-Activated Receptor Gamma and Regulations by the Ubiquitin-Proteasome System in Pancreatic Cancer

Figure 1

A schematic representation of the PPARγ molecule and its domains with their function. The molecule of PPARγ consists of an aminoterminal domain (also called A/B domain), which is responsible for ligand-independent transcriptional regulation. The following domain (also called domain C) contains two zinc finger-like and α-helical DNA-binding motifs typical of transcription factors. The C domain interacts with DNA through a PPRE (Peroxisome Proliferator Response Element) sequence. More carboxy terminal is the hinge domain (or D domain) which allows independent movement of the next and last domain of PPARγ molecule, domain E/F. This is the ligand-binding domain and potentiates the ability of PPARγ to dimerize with RXRα and recruit coactivators for transcription. Several post-translational modifications such as phosphorylation, ubiquitination, and SUMOylation modulate PPARγ activity.