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GartnerAnton

Gartner, Anton
DNA Damage Response and Genetic Toxicology
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E4 ligase-specific ubiquitination hubs coordinate DNA double-strand-break repair and apoptosis

Author(s)
Ackermann, LeenaSchell, MichaelPokrzywa, WojciechKevei, EvaGartner, AntonSchumacher, BjoernHoppe, Thorsten
Issued Date
2016-09
DOI
10.1038/nsmb.3296
URI
https://scholarworks.unist.ac.kr/handle/201301/27445
Fulltext
https://www.nature.com/articles/nsmb.3296
Citation
NATURE STRUCTURAL & MOLECULAR BIOLOGY, v.23, no.11, pp.995 - 1002
Abstract
Multiple protein ubiquitination events at DNA double-strand breaks (DSBs) regulate damage recognition, signaling and repair. It has remained poorly understood how the repair process of DSBs is coordinated with the apoptotic response. Here, we identified the E4 ubiquitin ligase UFD-2 as a mediator of DNA-damage-induced apoptosis in a genetic screen in Caenorhabditis elegans. We found that, after initiation of homologous recombination by RAD-51, UFD-2 forms foci that contain substrate-processivity factors including the ubiquitin-selective segregase CDC-48 (p97), the deubiquitination enzyme ATX-3 (Ataxin-3) and the proteasome. In the absence of UFD-2, RAD-51 foci persist, and DNA damage-induced apoptosis is prevented. In contrast, UFD-2 foci are retained until recombination intermediates are removed by the Holliday-junction-processing enzymes GEN-1, MUS-81 or XPF-1. Formation of UFD-2 foci also requires proapoptotic CEP-1 (p53) signaling. Our findings establish a central role of UFD-2 in the coordination between the DNA-repair process and the apoptotic response.
Publisher
NATURE PUBLISHING GROUP
ISSN
1545-9993
Keyword
DAMAGE-INDUCED APOPTOSISNEMATODE CAENORHABDITIS-ELEGANSC. ELEGANSSELECTIVE CHAPERONEPROTEASOME SYSTEMTUMOR-SUPPRESSORPROTEINCDC48/P97P53MULTIUBIQUITYLATION

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