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P53

Parc keeper

Nature Reviews Molecular Cell Biology volume 4, page 174 (2003)Cite this article

Now, in Cell, Gu and colleagues report the purification and characterization of a crucial factor in this process called Parc (p53 associated, parkin-like cytoplasmic protein). Parc exists as part of a large complex (∼1 MDa) in the cytoplasm, and tightly associates with p53, with its amino terminus appearing to interact directly with the carboxyl terminus of p53. Sequence analysis showed that Parc contains several domains, including Ring–IBR–Ring and CCH (C-terminal Cullen homology domain) signature motifs, which are found in proteins associated with ubiquitin-ligase activity. But despite having an intrinsic ubiquitin-ligase activity, the authors found no direct evidence to suggest that Parc regulates p53 stability through ubiquitylation.

Gu and co-workers found that overexpression of Parc promoted the cytoplasmic sequestration of ectopic p53. Neuroblastoma cells were also found to express abnormally high cytoplasmic levels of Parc, and RNA-interference-mediated downregulation of Parc in these cells induced nuclear localization of p53 and p53-mediated apoptosis.

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References

ORIGINAL RESEARCH PAPERS

  1. Kastan, M. B. & Zambetti, G. P. Parc-ing p53 in the cytoplasm. Cell 112, 29–40 (2003)

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FURTHER READING

  1. Nikolaev, A. Y., Li, M., Puskas, N., Qin, J. & Gu, W. Parc: a cytoplasmic anchor for p53. Cell 112, 1–5 (2003)

    Article  Google Scholar 

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Authors and Affiliations

  1. Associate Editor, Nature Reviews Drug Discovery,

    Simon Frantz

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  1. Simon Frantz
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Frantz, S. Parc keeper. Nat Rev Mol Cell Biol 4, 174 (2003). https://doi.org/10.1038/nrm1065

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  • DOI: https://doi.org/10.1038/nrm1065

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