Journal article
Phosphorylation of PNKP by ATM prevents its proteasomal degradation and enhances resistance to oxidative stress.
- Abstract:
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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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(Preview, Version of record, pdf, 2.5MB, Terms of use)
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- Publisher copy:
- 10.1093/nar/gks909
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Bibliographic Details
- Publisher:
- Oxford University Press
- Journal:
- Nucleic acids research More from this journal
- Volume:
- 40
- Issue:
- 22
- Pages:
- 11404-11415
- Publication date:
- 2012-12-01
- DOI:
- EISSN:
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1362-4962
- ISSN:
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0305-1048
Item Description
- Language:
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English
- Keywords:
-
- UUID:
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uuid:d8c2176f-08b9-42ea-bef6-5763f2cb529e
- Local pid:
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pubs:353916
- Source identifiers:
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353916
- Deposit date:
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2013-11-17
Terms of use
- Copyright holder:
- Parsons et al
- Copyright date:
- 2012
- Notes:
- Copyright © 2012 Parsons et al. Published by Oxford University Press. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/3.0/), which permits unrestricted, distribution, and reproduction in any medium, provided the original work is properly cited.
- Licence:
- CC Attribution (CC BY)
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