The nuclear oncogene SET controls DNA repair by KAP1 and HP1 retention to chromatin.
Identifieur interne : 002D65 ( PubMed/Curation ); précédent : 002D64; suivant : 002D66The nuclear oncogene SET controls DNA repair by KAP1 and HP1 retention to chromatin.
Auteurs : Alkmini Kalousi [France] ; Anne-Sophie Hoffbeck [France] ; Platonas N. Selemenakis [Grèce] ; Jordan Pinder [Canada] ; Kienan I. Savage [Australie] ; Kum Kum Khanna [Australie] ; Laurent Brino [France] ; Graham Dellaire [Canada] ; Vassilis G. Gorgoulis [Grèce] ; Evi Soutoglou [France]Source :
- Cell reports [ 2211-1247 ] ; 2015.
Descripteurs français
- KwdFr :
- Altération de l'ADN (génétique), Cassures double-brin de l'ADN (), Chaperons d'histones (antagonistes et inhibiteurs), Chaperons d'histones (génétique), Chaperons d'histones (métabolisme), Chromatine (génétique), Facteurs de transcription (antagonistes et inhibiteurs), Facteurs de transcription (génétique), Facteurs de transcription (métabolisme), Humains, Hétérochromatine (génétique), Protéines chromosomiques nonhistones (biosynthèse), Protéines chromosomiques nonhistones (génétique), Protéines de liaison à l'ADN (génétique), Protéines de répression (biosynthèse), Protéines de répression (génétique), Réparation de l'ADN par recombinaison (génétique).
- MESH :
- antagonistes et inhibiteurs : Chaperons d'histones, Facteurs de transcription.
- biosynthèse : Protéines chromosomiques nonhistones, Protéines de répression.
- génétique : Altération de l'ADN, Chaperons d'histones, Chromatine, Facteurs de transcription, Hétérochromatine, Protéines chromosomiques nonhistones, Protéines de liaison à l'ADN, Protéines de répression, Réparation de l'ADN par recombinaison.
- métabolisme : Chaperons d'histones, Facteurs de transcription.
- Cassures double-brin de l'ADN, Humains.
English descriptors
- KwdEn :
- Chromatin (genetics), Chromosomal Proteins, Non-Histone (biosynthesis), Chromosomal Proteins, Non-Histone (genetics), DNA Breaks, Double-Stranded (drug effects), DNA Damage (genetics), DNA-Binding Proteins (genetics), Heterochromatin (genetics), Histone Chaperones (antagonists & inhibitors), Histone Chaperones (genetics), Histone Chaperones (metabolism), Humans, Recombinational DNA Repair (genetics), Repressor Proteins (biosynthesis), Repressor Proteins (genetics), Transcription Factors (antagonists & inhibitors), Transcription Factors (genetics), Transcription Factors (metabolism).
- MESH :
- chemical , antagonists & inhibitors : Histone Chaperones, Transcription Factors.
- chemical , biosynthesis : Chromosomal Proteins, Non-Histone, Repressor Proteins.
- chemical , genetics : Chromatin, Chromosomal Proteins, Non-Histone, DNA-Binding Proteins, Heterochromatin, Histone Chaperones, Repressor Proteins, Transcription Factors.
- drug effects : DNA Breaks, Double-Stranded.
- genetics : DNA Damage, Recombinational DNA Repair.
- chemical , metabolism : Histone Chaperones, Transcription Factors.
- Humans.
Abstract
Cells experience damage from exogenous and endogenous sources that endanger genome stability. Several cellular pathways have evolved to detect DNA damage and mediate its repair. Although many proteins have been implicated in these processes, only recent studies have revealed how they operate in the context of high-ordered chromatin structure. Here, we identify the nuclear oncogene SET (I2PP2A) as a modulator of DNA damage response (DDR) and repair in chromatin surrounding double-strand breaks (DSBs). We demonstrate that depletion of SET increases DDR and survival in the presence of radiomimetic drugs, while overexpression of SET impairs DDR and homologous recombination (HR)-mediated DNA repair. SET interacts with the Kruppel-associated box (KRAB)-associated co-repressor KAP1, and its overexpression results in the sustained retention of KAP1 and Heterochromatin protein 1 (HP1) on chromatin. Our results are consistent with a model in which SET-mediated chromatin compaction triggers an inhibition of DNA end resection and HR.
DOI: 10.1016/j.celrep.2015.03.005
PubMed: 25818296
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<term>Chromosomal Proteins, Non-Histone (genetics)</term>
<term>DNA Breaks, Double-Stranded (drug effects)</term>
<term>DNA Damage (genetics)</term>
<term>DNA-Binding Proteins (genetics)</term>
<term>Heterochromatin (genetics)</term>
<term>Histone Chaperones (antagonists & inhibitors)</term>
<term>Histone Chaperones (genetics)</term>
<term>Histone Chaperones (metabolism)</term>
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<term>Repressor Proteins (genetics)</term>
<term>Transcription Factors (antagonists & inhibitors)</term>
<term>Transcription Factors (genetics)</term>
<term>Transcription Factors (metabolism)</term>
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<keywords scheme="KwdFr" xml:lang="fr"><term>Altération de l'ADN (génétique)</term>
<term>Cassures double-brin de l'ADN ()</term>
<term>Chaperons d'histones (antagonistes et inhibiteurs)</term>
<term>Chaperons d'histones (génétique)</term>
<term>Chaperons d'histones (métabolisme)</term>
<term>Chromatine (génétique)</term>
<term>Facteurs de transcription (antagonistes et inhibiteurs)</term>
<term>Facteurs de transcription (génétique)</term>
<term>Facteurs de transcription (métabolisme)</term>
<term>Humains</term>
<term>Hétérochromatine (génétique)</term>
<term>Protéines chromosomiques nonhistones (biosynthèse)</term>
<term>Protéines chromosomiques nonhistones (génétique)</term>
<term>Protéines de liaison à l'ADN (génétique)</term>
<term>Protéines de répression (biosynthèse)</term>
<term>Protéines de répression (génétique)</term>
<term>Réparation de l'ADN par recombinaison (génétique)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="antagonists & inhibitors" xml:lang="en"><term>Histone Chaperones</term>
<term>Transcription Factors</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="biosynthesis" xml:lang="en"><term>Chromosomal Proteins, Non-Histone</term>
<term>Repressor Proteins</term>
</keywords>
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<term>Chromosomal Proteins, Non-Histone</term>
<term>DNA-Binding Proteins</term>
<term>Heterochromatin</term>
<term>Histone Chaperones</term>
<term>Repressor Proteins</term>
<term>Transcription Factors</term>
</keywords>
<keywords scheme="MESH" qualifier="antagonistes et inhibiteurs" xml:lang="fr"><term>Chaperons d'histones</term>
<term>Facteurs de transcription</term>
</keywords>
<keywords scheme="MESH" qualifier="biosynthèse" xml:lang="fr"><term>Protéines chromosomiques nonhistones</term>
<term>Protéines de répression</term>
</keywords>
<keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>DNA Breaks, Double-Stranded</term>
</keywords>
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<term>Chromatine</term>
<term>Facteurs de transcription</term>
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<term>Protéines chromosomiques nonhistones</term>
<term>Protéines de liaison à l'ADN</term>
<term>Protéines de répression</term>
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<front><div type="abstract" xml:lang="en">Cells experience damage from exogenous and endogenous sources that endanger genome stability. Several cellular pathways have evolved to detect DNA damage and mediate its repair. Although many proteins have been implicated in these processes, only recent studies have revealed how they operate in the context of high-ordered chromatin structure. Here, we identify the nuclear oncogene SET (I2PP2A) as a modulator of DNA damage response (DDR) and repair in chromatin surrounding double-strand breaks (DSBs). We demonstrate that depletion of SET increases DDR and survival in the presence of radiomimetic drugs, while overexpression of SET impairs DDR and homologous recombination (HR)-mediated DNA repair. SET interacts with the Kruppel-associated box (KRAB)-associated co-repressor KAP1, and its overexpression results in the sustained retention of KAP1 and Heterochromatin protein 1 (HP1) on chromatin. Our results are consistent with a model in which SET-mediated chromatin compaction triggers an inhibition of DNA end resection and HR.</div>
</front>
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<ELocationID EIdType="doi" ValidYN="Y">10.1016/j.celrep.2015.03.005</ELocationID>
<ELocationID EIdType="pii" ValidYN="Y">S2211-1247(15)00257-0</ELocationID>
<Abstract><AbstractText>Cells experience damage from exogenous and endogenous sources that endanger genome stability. Several cellular pathways have evolved to detect DNA damage and mediate its repair. Although many proteins have been implicated in these processes, only recent studies have revealed how they operate in the context of high-ordered chromatin structure. Here, we identify the nuclear oncogene SET (I2PP2A) as a modulator of DNA damage response (DDR) and repair in chromatin surrounding double-strand breaks (DSBs). We demonstrate that depletion of SET increases DDR and survival in the presence of radiomimetic drugs, while overexpression of SET impairs DDR and homologous recombination (HR)-mediated DNA repair. SET interacts with the Kruppel-associated box (KRAB)-associated co-repressor KAP1, and its overexpression results in the sustained retention of KAP1 and Heterochromatin protein 1 (HP1) on chromatin. Our results are consistent with a model in which SET-mediated chromatin compaction triggers an inhibition of DNA end resection and HR.</AbstractText>
<CopyrightInformation>Copyright © 2015 The Authors. Published by Elsevier Inc. All rights reserved.</CopyrightInformation>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Kalousi</LastName>
<ForeName>Alkmini</ForeName>
<Initials>A</Initials>
<AffiliationInfo><Affiliation>Institut de Génétique et de Biologie Moléculaire et Cellulaire (IGBMC), UMR 7104 Centre National de la Recherche Scientifique (CNRS), UdS, INSERM U964, BP 10142, 67404 Illkirch Cedex, Strasbourg, France.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Hoffbeck</LastName>
<ForeName>Anne-Sophie</ForeName>
<Initials>AS</Initials>
<AffiliationInfo><Affiliation>Institut de Génétique et de Biologie Moléculaire et Cellulaire (IGBMC), UMR 7104 Centre National de la Recherche Scientifique (CNRS), UdS, INSERM U964, BP 10142, 67404 Illkirch Cedex, Strasbourg, France.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Selemenakis</LastName>
<ForeName>Platonas N</ForeName>
<Initials>PN</Initials>
<AffiliationInfo><Affiliation>Molecular Carcinogenesis Group, Department of Histology and Embryology, School of Medicine, University of Athens, 11527 Athens, Greece.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Pinder</LastName>
<ForeName>Jordan</ForeName>
<Initials>J</Initials>
<AffiliationInfo><Affiliation>Departments of Pathology and Biochemistry & Molecular Biology, Dalhousie University, B3H 4R2 Halifax, NS, Canada; Beatrice Hunter Cancer Research Institute, B3H 4R2 Halifax, NS, Canada.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Savage</LastName>
<ForeName>Kienan I</ForeName>
<Initials>KI</Initials>
<AffiliationInfo><Affiliation>QIMR Berghofer Medical Research Institute, QLD 4006 Herston, Australia.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Khanna</LastName>
<ForeName>Kum Kum</ForeName>
<Initials>KK</Initials>
<AffiliationInfo><Affiliation>QIMR Berghofer Medical Research Institute, QLD 4006 Herston, Australia.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Brino</LastName>
<ForeName>Laurent</ForeName>
<Initials>L</Initials>
<AffiliationInfo><Affiliation>Institut de Génétique et de Biologie Moléculaire et Cellulaire (IGBMC), UMR 7104 Centre National de la Recherche Scientifique (CNRS), UdS, INSERM U964, BP 10142, 67404 Illkirch Cedex, Strasbourg, France.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Dellaire</LastName>
<ForeName>Graham</ForeName>
<Initials>G</Initials>
<AffiliationInfo><Affiliation>Departments of Pathology and Biochemistry & Molecular Biology, Dalhousie University, B3H 4R2 Halifax, NS, Canada; Beatrice Hunter Cancer Research Institute, B3H 4R2 Halifax, NS, Canada.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Gorgoulis</LastName>
<ForeName>Vassilis G</ForeName>
<Initials>VG</Initials>
<AffiliationInfo><Affiliation>Molecular Carcinogenesis Group, Department of Histology and Embryology, School of Medicine, University of Athens, 11527 Athens, Greece; Faculty Institute of Cancer Sciences, University of Manchester, Manchester Academic Health Science Centre, M13 9PL Manchester, UK; Biomedical Research Foundation, Academy of Athens, 11527 Athens, Greece.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Soutoglou</LastName>
<ForeName>Evi</ForeName>
<Initials>E</Initials>
<AffiliationInfo><Affiliation>Institut de Génétique et de Biologie Moléculaire et Cellulaire (IGBMC), UMR 7104 Centre National de la Recherche Scientifique (CNRS), UdS, INSERM U964, BP 10142, 67404 Illkirch Cedex, Strasbourg, France. Electronic address: evisou@igbmc.fr.</Affiliation>
</AffiliationInfo>
</Author>
</AuthorList>
<Language>eng</Language>
<GrantList CompleteYN="Y"><Grant><GrantID>MR/K018965/1</GrantID>
<Agency>Medical Research Council</Agency>
<Country>United Kingdom</Country>
</Grant>
</GrantList>
<PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType>
<PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType>
</PublicationTypeList>
<ArticleDate DateType="Electronic"><Year>2015</Year>
<Month>03</Month>
<Day>26</Day>
</ArticleDate>
</Article>
<MedlineJournalInfo><Country>United States</Country>
<MedlineTA>Cell Rep</MedlineTA>
<NlmUniqueID>101573691</NlmUniqueID>
</MedlineJournalInfo>
<ChemicalList><Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D002843">Chromatin</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D002868">Chromosomal Proteins, Non-Histone</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D004268">DNA-Binding Proteins</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D006570">Heterochromatin</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D056488">Histone Chaperones</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D012097">Repressor Proteins</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="C513473">SET protein, human</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="C101116">TRIM28 protein, human</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D014157">Transcription Factors</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>107283-02-3</RegistryNumber>
<NameOfSubstance UI="C066725">heterochromatin-specific nonhistone chromosomal protein HP-1</NameOfSubstance>
</Chemical>
</ChemicalList>
<CitationSubset>IM</CitationSubset>
<MeshHeadingList><MeshHeading><DescriptorName UI="D002843" MajorTopicYN="N">Chromatin</DescriptorName>
<QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D002868" MajorTopicYN="N">Chromosomal Proteins, Non-Histone</DescriptorName>
<QualifierName UI="Q000096" MajorTopicYN="N">biosynthesis</QualifierName>
<QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D053903" MajorTopicYN="N">DNA Breaks, Double-Stranded</DescriptorName>
<QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D004249" MajorTopicYN="N">DNA Damage</DescriptorName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D004268" MajorTopicYN="N">DNA-Binding Proteins</DescriptorName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D006570" MajorTopicYN="N">Heterochromatin</DescriptorName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D056488" MajorTopicYN="N">Histone Chaperones</DescriptorName>
<QualifierName UI="Q000037" MajorTopicYN="N">antagonists & inhibitors</QualifierName>
<QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D059767" MajorTopicYN="N">Recombinational DNA Repair</DescriptorName>
<QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D012097" MajorTopicYN="N">Repressor Proteins</DescriptorName>
<QualifierName UI="Q000096" MajorTopicYN="N">biosynthesis</QualifierName>
<QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D014157" MajorTopicYN="N">Transcription Factors</DescriptorName>
<QualifierName UI="Q000037" MajorTopicYN="N">antagonists & inhibitors</QualifierName>
<QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
</MeshHeadingList>
</MedlineCitation>
<PubmedData><History><PubMedPubDate PubStatus="received"><Year>2014</Year>
<Month>09</Month>
<Day>12</Day>
</PubMedPubDate>
<PubMedPubDate PubStatus="revised"><Year>2015</Year>
<Month>01</Month>
<Day>15</Day>
</PubMedPubDate>
<PubMedPubDate PubStatus="accepted"><Year>2015</Year>
<Month>02</Month>
<Day>27</Day>
</PubMedPubDate>
<PubMedPubDate PubStatus="entrez"><Year>2015</Year>
<Month>3</Month>
<Day>31</Day>
<Hour>6</Hour>
<Minute>0</Minute>
</PubMedPubDate>
<PubMedPubDate PubStatus="pubmed"><Year>2015</Year>
<Month>3</Month>
<Day>31</Day>
<Hour>6</Hour>
<Minute>0</Minute>
</PubMedPubDate>
<PubMedPubDate PubStatus="medline"><Year>2016</Year>
<Month>1</Month>
<Day>5</Day>
<Hour>6</Hour>
<Minute>0</Minute>
</PubMedPubDate>
</History>
<PublicationStatus>ppublish</PublicationStatus>
<ArticleIdList><ArticleId IdType="pubmed">25818296</ArticleId>
<ArticleId IdType="pii">S2211-1247(15)00257-0</ArticleId>
<ArticleId IdType="doi">10.1016/j.celrep.2015.03.005</ArticleId>
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