Work

Stress-Dependent Nucleolin Mobilization Mediated by p53-Nucleolin Complex Formation

Year: 2002

Type: article

Abstract: 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.

Source: Molecular and Cellular Biology

DOI: 10.1128/mcb.22.16.6014-6022.2002

Authors: Yaron Daniely, Diana D. Dimitrova, James A. Borowiec

Institutions: NYU Langone Health, Weizmann Institute of Science, New York University

Language: English

Topic: Cancer-related Molecular Pathways

Subfield: Oncology

Field: Medicine

Domain: Health Sciences

SDG: Good health and well-being

Open Access status: green

Funders: American Cancer Society, National Institutes of Health, National Cancer Institute, National Institute of Allergy and Infectious Diseases