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 language | English |
|---|---|
| Pages (from-to) | 1620-1628 |
| Number of pages | 9 |
| Journal | Oncogene |
| Volume | 22 |
| Issue number | 11 |
| DOIs | |
| State | Published - Mar 20 2003 |
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All Science Journal Classification (ASJC) codes
- Molecular Biology
- Cancer Research
- Genetics
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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 journal › Article
}
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.
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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 -