PARC (p53 associated parkin like cytoplasmic protein) antibody directly interacted and formed an approximately 1MD 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. Furthermore, 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.
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