Posttranslational modification of mammalian AP endonuclease (APE1)

Carlos S. Busso, Michael W. Lake, Tadahide Izumi

Research output: Contribution to journalReview articlepeer-review

50 Scopus citations


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).

Original languageEnglish
Pages (from-to)3609-3620
Number of pages12
JournalCellular and Molecular Life Sciences
Issue number21
StatePublished - Nov 2010

Bibliographical note

Funding Information:
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).


  • APE1
  • Acetylation
  • DNA base excision repair
  • Phosphorylation
  • Ubiquitination

ASJC Scopus subject areas

  • Molecular Medicine
  • Molecular Biology
  • Pharmacology
  • Cellular and Molecular Neuroscience
  • Cell Biology


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