UV-C-induced DNA damage leads to p53-dependent nuclear trafficking of PML

Oncogene. 2003 Mar 20;22(11):1620-8. doi: 10.1038/sj.onc.1206140.


The promyelocytic leukemia protein (PML) is a nuclear phosphoprotein that localizes to distinct domains in the nucleus, described as PML nuclear bodies (PML-NBs). Recent findings indicate that PML regulates the p53 response to oncogenic signals. Here, we define a p53-dependent role for PML in response to DNA damage. We exposed cells to ultraviolet light (UV-C) and imaged the nuclear distribution of PML, p53, and the BLM helicase by confocal microscopy. After DNA damage, PML partially relocated out of the PML-NBs, and colocalized with BLM and p53 at sites of DNA repair. In addition, using the isogenic HCT116 cell lines (p53+/+ and -/-), we show that the redistribution of PML was dependent on functional p53. Western analysis revealed that the level of PML protein remained unaltered after UV-C treatment. These results are consistent with the hypothesis that PML, in conjunction with p53 and BLM, contributes to the cellular response to UV-C-induced DNA damage and its repair.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Cell Line
  • DNA / radiation effects*
  • DNA Damage*
  • Microscopy, Confocal
  • Neoplasm Proteins / metabolism*
  • Nuclear Proteins*
  • Protein Transport / physiology*
  • Reverse Transcriptase Polymerase Chain Reaction
  • Transcription Factors / metabolism*
  • Tumor Suppressor Protein p53 / physiology*
  • Tumor Suppressor Proteins
  • Ultraviolet Rays*


  • Neoplasm Proteins
  • Nuclear Proteins
  • Transcription Factors
  • Tumor Suppressor Protein p53
  • Tumor Suppressor Proteins
  • DNA