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

Hasan Seker, Carlos Rubbi, Steven P. Linke, Elise D. Bowman, Susan Garfield, Laura A. Hansen, Katherine L B Borden, Jo Milner, Curtis C. Harris

Research output: Contribution to journalArticle

40 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)1620-1628
Number of pages9
JournalOncogene
Volume22
Issue number11
DOIs
StatePublished - Mar 20 2003

Fingerprint

DNA Damage
Promyelocytic Leukemia Protein
HCT116 Cells
Phosphoproteins
Ultraviolet Rays
Confocal Microscopy
DNA Repair
Cell Line

All Science Journal Classification (ASJC) codes

  • Molecular Biology
  • Cancer Research
  • Genetics

Cite this

Seker, H., Rubbi, C., Linke, S. P., Bowman, E. D., Garfield, S., Hansen, L. A., ... Harris, C. C. (2003). UV-C-induced DNA damage leads to p53-dependent nuclear trafficking of PML. Oncogene, 22(11), 1620-1628. https://doi.org/10.1038/sj.onc.1206140

UV-C-induced DNA damage leads to p53-dependent nuclear trafficking of PML. / Seker, Hasan; Rubbi, Carlos; Linke, Steven P.; Bowman, Elise D.; Garfield, Susan; Hansen, Laura A.; Borden, Katherine L B; Milner, Jo; Harris, Curtis C.

In: Oncogene, Vol. 22, No. 11, 20.03.2003, p. 1620-1628.

Research output: Contribution to journalArticle

Seker, H, Rubbi, C, Linke, SP, Bowman, ED, Garfield, S, Hansen, LA, Borden, KLB, Milner, J & Harris, CC 2003, 'UV-C-induced DNA damage leads to p53-dependent nuclear trafficking of PML', Oncogene, vol. 22, no. 11, pp. 1620-1628. https://doi.org/10.1038/sj.onc.1206140
Seker H, Rubbi C, Linke SP, Bowman ED, Garfield S, Hansen LA et al. UV-C-induced DNA damage leads to p53-dependent nuclear trafficking of PML. Oncogene. 2003 Mar 20;22(11):1620-1628. https://doi.org/10.1038/sj.onc.1206140
Seker, Hasan ; Rubbi, Carlos ; Linke, Steven P. ; Bowman, Elise D. ; Garfield, Susan ; Hansen, Laura A. ; Borden, Katherine L B ; Milner, Jo ; Harris, Curtis C. / UV-C-induced DNA damage leads to p53-dependent nuclear trafficking of PML. In: Oncogene. 2003 ; Vol. 22, No. 11. pp. 1620-1628.
@article{fbad1f19428d41b4afb358edb84e1245,
title = "UV-C-induced DNA damage leads to p53-dependent nuclear trafficking of PML",
abstract = "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.",
author = "Hasan Seker and Carlos Rubbi and Linke, {Steven P.} and Bowman, {Elise D.} and Susan Garfield and Hansen, {Laura A.} and Borden, {Katherine L B} and Jo Milner and Harris, {Curtis C.}",
year = "2003",
month = "3",
day = "20",
doi = "10.1038/sj.onc.1206140",
language = "English",
volume = "22",
pages = "1620--1628",
journal = "Oncogene",
issn = "0950-9232",
publisher = "Nature Publishing Group",
number = "11",

}

TY - JOUR

T1 - UV-C-induced DNA damage leads to p53-dependent nuclear trafficking of PML

AU - Seker, Hasan

AU - Rubbi, Carlos

AU - Linke, Steven P.

AU - Bowman, Elise D.

AU - Garfield, Susan

AU - Hansen, Laura A.

AU - Borden, Katherine L B

AU - Milner, Jo

AU - Harris, Curtis C.

PY - 2003/3/20

Y1 - 2003/3/20

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=0037457077&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0037457077&partnerID=8YFLogxK

U2 - 10.1038/sj.onc.1206140

DO - 10.1038/sj.onc.1206140

M3 - Article

VL - 22

SP - 1620

EP - 1628

JO - Oncogene

JF - Oncogene

SN - 0950-9232

IS - 11

ER -