Abstract
A key issue in studying mammalian DNA base excision repair is how its component proteins respond to a plethora of cell-signaling mediators invoked by DNA damage and stress-inducing agents such as reactive oxygen species, and how the actions of individual BER proteins are attributed to cell survival or apoptotic/necrotic death. This article reviews the past and recent progress on posttranslational modification (PTM) of mammalian apurinic/apyrimidinic (AP) endonuclease 1 (APE1).
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Abbreviations
- AP:
-
Apurinic/apyrimidinic
- APE:
-
AP endonuclease
- APE1:
-
AP endonuclease 1
- BER:
-
Base excision repair
- CKII:
-
Casein kinase II
- FEN1:
-
Flap endonuclease 1
- HAT:
-
Histone acetyltransferase
- HDAC:
-
Histone deacetylase
- MDM2:
-
Mouse double minute 2
- NAM:
-
Nicotinamide
- nCaRE:
-
Negative calcium response element
- NPM1:
-
Nucleophosmin
- PARP1:
-
Poly(ADP-ribose) polymerase 1
- PKC:
-
Protein kinase C
- Pol B:
-
DNA polymerase beta
- Ref-1:
-
Redox factor 1
- ROS:
-
Reactive oxygen species
- SSB:
-
Single-strand break
- PTM:
-
Posttranslational modification
- SNP:
-
Single nucleotide polymorphism
- TF:
-
Transcription factor
- TSA:
-
Trichostatin A
- XRCC1:
-
X-ray repair cross complementation group 1
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Acknowledgments
While we were in the final process of revision, Huang et al. newly reported that APE1 was phosphorylated at Thr 233, resulting in a decrease of the APE activity, particularly in brain tissues from patients with Parkinson’s and Alzheimer’s diseases (Nat Cell Biol 12:563–571, 2010). A significant question in relation to this review is if and how T233 phosphorylation affects the intracellular levels of acetylated and ubiquitinated APE1. This work was supported by NIH CA98664 (TI).
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Busso, C.S., Lake, M.W. & Izumi, T. Posttranslational modification of mammalian AP endonuclease (APE1). Cell. Mol. Life Sci. 67, 3609–3620 (2010). https://doi.org/10.1007/s00018-010-0487-3
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DOI: https://doi.org/10.1007/s00018-010-0487-3