[A new view on p53 protein cytoplasmic sequestration]

Bull Cancer. 2003 May;90(5):380-2.
[Article in French]

Abstract

In human tumors, p53 inactivation occurs frequently by mutation, and possibly also by nuclear exclusion of wt p53. First reported by Uta Moll in 1992, p53 "cytoplasmic sequestration" has been thoroughly studied to elucidate molecular mechanism of this process, using neuroblastoma cell lines as model. An American team at the Columbia University has just isolated the cytoplasmic protein Parc [Nikolaev, Cell] which specifically binds to p53 and anchors it, so that the "guardian of the genome" cannot play its role in the nucleus. AntiParc siRNA-manipulation relocates p53 into the nucleus, restitutes a function to p and chemo-radiosensitivity to malignant neuroblasts.

Publication types

  • English Abstract
  • Review

MeSH terms

  • Cytoplasm / chemistry*
  • DNA Topoisomerase IV / pharmacology*
  • Humans
  • Neoplasms / physiopathology
  • Neuroblastoma
  • Tumor Cells, Cultured
  • Tumor Suppressor Protein p53 / metabolism
  • Tumor Suppressor Protein p53 / pharmacokinetics*
  • Tumor Suppressor Protein p53 / pharmacology*

Substances

  • Tumor Suppressor Protein p53
  • DNA Topoisomerase IV