Posttranslational modification of mammalian AP endonuclease (APE1)

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

doi:10.1007/s00018-010-0487-3

Posttranslational modification of mammalian AP endonuclease (APE1)

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

Toxicology and Cancer Biology

Research output: Contribution to journal › Review article › peer-review

51 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 language	English
Pages (from-to)	3609-3620
Number of pages	12
Journal	Cellular and Molecular Life Sciences
Volume	67
Issue number	21
DOIs	https://doi.org/10.1007/s00018-010-0487-3
State	Published - 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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10.1007/s00018-010-0487-3

Cite this

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title = "Posttranslational modification of mammalian AP endonuclease (APE1)",

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).",

keywords = "APE1, Acetylation, DNA base excision repair, Phosphorylation, Ubiquitination",

author = "Busso, {Carlos S.} and Lake, {Michael W.} and Tadahide Izumi",

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{\textquoteright}s and Alzheimer{\textquoteright}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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AU - Lake, Michael W.

AU - Izumi, Tadahide

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N2 - 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).

AB - 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).

KW - APE1

KW - Acetylation

KW - DNA base excision repair

KW - Phosphorylation

KW - Ubiquitination

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Posttranslational modification of mammalian AP endonuclease (APE1)

Abstract

Bibliographical note

Keywords

ASJC Scopus subject areas

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