Cullin 9 (CUL9)

PARC directly interacted and formed an approximately 1-MD complex with p53 in the cytoplasm of unstressed cells. In the absence of stress, inactivation of PARC induced nuclear localization of endogenous p53 and activated p53-dependent apoptosis. Overexpression of PARC promoted cytoplasmic sequestration of ectopic p53.abnormal cytoplasmic localization of p53 was observed in a number of neuroblastoma cell lines; RNA interference-mediated reduction of endogenous PARC significantly sensitized these neuroblastoma cells in the DNA damage response. These results revealed that PARC is a critical regulator in controlling p53 subcellular localization and subsequent function.PARC also has a unique motif that is highly homologous to the C terminus of cullin proteins that the authors referred to as the C-terminal cullin homology domain.