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Phosphorylation of PNKP by ATM prevents its proteasomal degradation and enhances resistance to oxidative stress.

Abstract:

We examined the mechanism regulating the cellular levels of PNKP, the major kinase/phosphatase involved in the repair of oxidative DNA damage, and find that it is controlled by ATM phosphorylation and ubiquitylation-dependent proteasomal degradation. We discovered that ATM-dependent phosphorylation of PNKP at serines 114 and 126 in response to oxidative DNA damage inhibits ubiquitylation-dependent proteasomal degradation of PNKP, and consequently increases PNKP stability that is required for ...

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Publication status:
Published
Peer review status:
Peer reviewed

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Publisher copy:
10.1093/nar/gks909

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Institution:
University of Oxford
Division:
MSD
Department:
Oncology
Role:
Author
More by this author
Institution:
University of Oxford
Division:
MSD
Department:
Oncology
Role:
Author
More by this author
Institution:
University of Oxford
Division:
MSD
Department:
Oncology
Role:
Author
More by this author
Institution:
University of Oxford
Division:
MSD
Department:
NDM
Role:
Author
More by this author
Institution:
University of Oxford
Division:
MSD
Department:
NDM
Role:
Author
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Funding agency for:
Dianov, G
Medical Research Council More from this funder
Cancer Research UK More from this funder
Publisher:
Oxford University Press Publisher's website
Journal:
Nucleic acids research Journal website
Volume:
40
Issue:
22
Pages:
11404-11415
Publication date:
2012-12-01
DOI:
EISSN:
1362-4962
ISSN:
0305-1048
Source identifiers:
353916

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