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Stress-dependent nucleolin mobilization mediated by p53-nucleolin complex formation.

We recently discovered that heat shock causes nucleolin to relocalize from the nucleolus to the nucleoplasm, whereupon it binds replication protein A and inhibits DNA replication initiation. We report that nucleolin mobilization also occurs following exposure to ionizing radiation (IR) and treatment with camptothecin. Mobilization was selective in that another nucleolar marker, upstream binding factor, did not relocalize in response to IR. Nucleolin relocalization was dependent on p53 and stress, the latter initially stimulating nucleolin-p53 complex formation. Nucleolin relocalization and complex formation in vivo were independent of p53 transactivation but required the p53 C-terminal regulatory domain. Nucleolin and p53 also interact directly in vitro, with a similar requirement for p53 domains. These data indicate a novel p53-dependent mechanism in which cell stress mobilizes nucleolin for transient replication inhibition and DNA repair.

Pubmed ID: 12138209

Authors

  • Daniely Y
  • Dimitrova DD
  • Borowiec JA

Journal

Molecular and cellular biology

Publication Data

August 24, 2002

Associated Grants

  • Agency: NIAID NIH HHS, Id: AI29963
  • Agency: NCI NIH HHS, Id: P30CA16087

Mesh Terms

  • Active Transport, Cell Nucleus
  • Camptothecin
  • Cell Fractionation
  • Cell Nucleus
  • Enzyme Inhibitors
  • Fibroblasts
  • Humans
  • Lung
  • Microscopy, Fluorescence
  • Nuclear Proteins
  • Phosphoproteins
  • RNA-Binding Proteins
  • Radiation, Ionizing
  • Tumor Cells, Cultured
  • Tumor Suppressor Protein p53