. . . "1" . "2003-1-15" . "Nuclear localization of p53 is essential for its tumor suppressor function. Here, we have identified Parc, a Parkin-like ubiquitin ligase, as a cytoplasmic anchor protein in p53-associated protein complexes. Parc directly interacts and forms a approximately 1 MDa complex with p53 in the cytoplasm of unstressed cells. In the absence of stress, inactivation of Parc induces nuclear localization of endogenous p53 and activates p53-dependent apoptosis. Overexpression of Parc promotes cytoplasmic sequestration of ectopic p53. Furthermore, abnormal cytoplasmic localization of p53 was observed in a number of neuroblastoma cell lines; RNAi-mediated reduction of endogenous Parc significantly sensitizes these neuroblastoma cells in the DNA damage response. These results reveal that Parc is a critical regulator in controlling p53 subcellular localization and subsequent function." . . "eng" . . "IM" . . . . . . . . . . . "MEDLINE" . "Jan" . "0092-8674" . . . . . . "Print" . "10" . "112" . "NLM" . "Y" . "29-40" . "2006-11-15" . . . . . . . . . . . . . . . . . . . . . "2003" . "Parc: a cytoplasmic anchor for p53." . "Institute for Cancer Genetics and Department of Pathology, College of Physicians and Surgeons, Columbia University, 1150 St. Nicholas Avenue, New York, NY 10032, USA." . "Journal Article" . "Research Support, Non-U.S. Gov't" . "Research Support, U.S. Gov't, P.H.S." . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . .