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

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).

Original languageEnglish
Pages (from-to)3609-3620
Number of pages12
JournalCellular and Molecular Life Sciences
Volume67
Issue number21
DOIs
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).

Keywords

  • 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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