Parc-ing p53 in the Cytoplasm

Parc-ing p53 in the Cytoplasm

Nikolaev et al. (this issue of Cell) report the identification of a parkin-like protein, Parc, and its role in anchoring the tumor suppressor protein p53 in the cytoplasm reveals yet another level of control of p53 function. Regulation of the subcellular localization of p53 by Parc may serve as a novel target in treatment of certain types of tumors.

Parc A Cytoplasmic Anchor for p53

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...

p53 in the Cytoplasm A Question of Overkill?

The tumor suppressor p53 regulates cellular responses to stress by serving in the nucleus to regulate transcription of genes involved in processes including cell cycle arrest, DNA repair, and apoptosis. Nevertheless, recent papers show that p53 may have a separate cytoplasmic role in directly regulating the Bax-dependent mitochondrial pathway to cell death.

Xerox PARC

J - Parc

An outline is explained for hadron-physics projects at J-PARC, which is considered to be one of the flagship facilities in hadron physics from 2008. The facility provides an intensity frontier with 50 GeV proton beam for nuclear and particle physics. It could cover a wide range of hadron physics from strongly interacting many-body systems with an extended hadronic degree of freedom, strangeness...