Chronic oxidative stress promotes H2AX protein degradation and enhances chemosensitivity in breast cancer patients

Abstract Anti‐cancer drugs often increase reactive oxygen species (ROS) and cause DNA damage. Here, we highlight a new cross talk between chronic oxidative stress and the histone variant H2AX, a key player in DNA repair. We observe that persistent accumulation of ROS, due to a deficient JunD‐/Nrf2‐a...

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Main Authors: Tina Gruosso, Virginie Mieulet, Melissa Cardon, Brigitte Bourachot, Yann Kieffer, Flavien Devun, Thierry Dubois, Marie Dutreix, Anne Vincent‐Salomon, Kyle Malcolm Miller, Fatima Mechta‐Grigoriou
Format: Article
Language:English
Published: Springer Nature 2016-03-01
Series:EMBO Molecular Medicine
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Online Access:https://doi.org/10.15252/emmm.201505891
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author Tina Gruosso
Virginie Mieulet
Melissa Cardon
Brigitte Bourachot
Yann Kieffer
Flavien Devun
Thierry Dubois
Marie Dutreix
Anne Vincent‐Salomon
Kyle Malcolm Miller
Fatima Mechta‐Grigoriou
author_facet Tina Gruosso
Virginie Mieulet
Melissa Cardon
Brigitte Bourachot
Yann Kieffer
Flavien Devun
Thierry Dubois
Marie Dutreix
Anne Vincent‐Salomon
Kyle Malcolm Miller
Fatima Mechta‐Grigoriou
author_sort Tina Gruosso
collection DOAJ
description Abstract Anti‐cancer drugs often increase reactive oxygen species (ROS) and cause DNA damage. Here, we highlight a new cross talk between chronic oxidative stress and the histone variant H2AX, a key player in DNA repair. We observe that persistent accumulation of ROS, due to a deficient JunD‐/Nrf2‐antioxidant response, reduces H2AX protein levels. This effect is mediated by an enhanced interaction of H2AX with the E3 ubiquitin ligase RNF168, which is associated with H2AX poly‐ubiquitination and promotes its degradation by the proteasome. ROS‐mediated H2AX decrease plays a crucial role in chemosensitivity. Indeed, cycles of chemotherapy that sustainably increase ROS reduce H2AX protein levels in Triple‐Negative breast cancer (TNBC) patients. H2AX decrease by such treatment is associated with an impaired NRF2‐antioxidant response and is indicative of the therapeutic efficiency and survival of TNBC patients. Thus, our data describe a novel ROS‐mediated regulation of H2AX turnover, which provides new insights into genetic instability and treatment efficacy in TNBC patients.
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spelling doaj-art-6de217d98be14d7bb17cccccd1b794cc2025-08-20T03:05:55ZengSpringer NatureEMBO Molecular Medicine1757-46761757-46842016-03-018552754910.15252/emmm.201505891Chronic oxidative stress promotes H2AX protein degradation and enhances chemosensitivity in breast cancer patientsTina Gruosso0Virginie Mieulet1Melissa Cardon2Brigitte Bourachot3Yann Kieffer4Flavien Devun5Thierry Dubois6Marie Dutreix7Anne Vincent‐Salomon8Kyle Malcolm Miller9Fatima Mechta‐Grigoriou10Stress and Cancer Laboratory, Equipe Labelisée LNCC, Institut CurieStress and Cancer Laboratory, Equipe Labelisée LNCC, Institut CurieStress and Cancer Laboratory, Equipe Labelisée LNCC, Institut CurieStress and Cancer Laboratory, Equipe Labelisée LNCC, Institut CurieStress and Cancer Laboratory, Equipe Labelisée LNCC, Institut CurieInstitut Curie, CNRS UMR3347, INSERM U1021, University Paris‐Sud 11Department of Translational Research, Institut CurieInstitut Curie, CNRS UMR3347, INSERM U1021, University Paris‐Sud 11Department of Tumour Biology, Institut CurieDepartment of Molecular Biosciences, Institute for Cellular and Molecular Biology, University of Texas at AustinStress and Cancer Laboratory, Equipe Labelisée LNCC, Institut CurieAbstract Anti‐cancer drugs often increase reactive oxygen species (ROS) and cause DNA damage. Here, we highlight a new cross talk between chronic oxidative stress and the histone variant H2AX, a key player in DNA repair. We observe that persistent accumulation of ROS, due to a deficient JunD‐/Nrf2‐antioxidant response, reduces H2AX protein levels. This effect is mediated by an enhanced interaction of H2AX with the E3 ubiquitin ligase RNF168, which is associated with H2AX poly‐ubiquitination and promotes its degradation by the proteasome. ROS‐mediated H2AX decrease plays a crucial role in chemosensitivity. Indeed, cycles of chemotherapy that sustainably increase ROS reduce H2AX protein levels in Triple‐Negative breast cancer (TNBC) patients. H2AX decrease by such treatment is associated with an impaired NRF2‐antioxidant response and is indicative of the therapeutic efficiency and survival of TNBC patients. Thus, our data describe a novel ROS‐mediated regulation of H2AX turnover, which provides new insights into genetic instability and treatment efficacy in TNBC patients.https://doi.org/10.15252/emmm.201505891JUNDNRF2RNF168Triple‐Negative breast cancerubiquitination
spellingShingle Tina Gruosso
Virginie Mieulet
Melissa Cardon
Brigitte Bourachot
Yann Kieffer
Flavien Devun
Thierry Dubois
Marie Dutreix
Anne Vincent‐Salomon
Kyle Malcolm Miller
Fatima Mechta‐Grigoriou
Chronic oxidative stress promotes H2AX protein degradation and enhances chemosensitivity in breast cancer patients
EMBO Molecular Medicine
JUND
NRF2
RNF168
Triple‐Negative breast cancer
ubiquitination
title Chronic oxidative stress promotes H2AX protein degradation and enhances chemosensitivity in breast cancer patients
title_full Chronic oxidative stress promotes H2AX protein degradation and enhances chemosensitivity in breast cancer patients
title_fullStr Chronic oxidative stress promotes H2AX protein degradation and enhances chemosensitivity in breast cancer patients
title_full_unstemmed Chronic oxidative stress promotes H2AX protein degradation and enhances chemosensitivity in breast cancer patients
title_short Chronic oxidative stress promotes H2AX protein degradation and enhances chemosensitivity in breast cancer patients
title_sort chronic oxidative stress promotes h2ax protein degradation and enhances chemosensitivity in breast cancer patients
topic JUND
NRF2
RNF168
Triple‐Negative breast cancer
ubiquitination
url https://doi.org/10.15252/emmm.201505891
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