Ubiquitin-Specific Protease 5 Is Required for the Efficient Repair of DNA Double-Strand Breaks
Identifieur interne : 000A36 ( Main/Exploration ); précédent : 000A35; suivant : 000A37Ubiquitin-Specific Protease 5 Is Required for the Efficient Repair of DNA Double-Strand Breaks
Auteurs : Satoshi Nakajima [États-Unis] ; Li Lan [États-Unis] ; Leizhen Wei [États-Unis] ; Ching-Lung Hsieh [États-Unis] ; Vesna Rapi Otrin [États-Unis] ; Akira Yasui [Japon] ; Arthur S. Levine [États-Unis]Source :
- PLoS ONE [ 1932-6203 ] ; 2014.
Descripteurs français
- KwdFr :
- Cassures double-brin de l'ADN (effets des radiations), Cinétique, Endopeptidases (déficit), Endopeptidases (génétique), Endopeptidases (métabolisme), Histone (métabolisme), Humains, Lignée cellulaire, Protéines de liaison à l'ADN (métabolisme), Rayons X (effets indésirables), Recombinaison homologue (effets des radiations), Réparation de l'ADN (effets des radiations), Survie cellulaire (effets des radiations), Techniques de knock-down de gènes, Ubiquitin-protein ligases, Ubiquitine (métabolisme).
- MESH :
- déficit : Endopeptidases.
- effets des radiations : Cassures double-brin de l'ADN, Recombinaison homologue, Réparation de l'ADN, Survie cellulaire.
- effets indésirables : Rayons X.
- génétique : Endopeptidases.
- métabolisme : Endopeptidases, Histone, Protéines de liaison à l'ADN, Ubiquitine.
- Cinétique, Humains, Lignée cellulaire, Techniques de knock-down de gènes, Ubiquitin-protein ligases.
English descriptors
- KwdEn :
- Cell Line, Cell Survival (radiation effects), DNA Breaks, Double-Stranded (radiation effects), DNA Repair (radiation effects), DNA-Binding Proteins (metabolism), Endopeptidases (deficiency), Endopeptidases (genetics), Endopeptidases (metabolism), Gene Knockdown Techniques, Histones (metabolism), Homologous Recombination (radiation effects), Humans, Kinetics, Ubiquitin (metabolism), Ubiquitin-Protein Ligases, X-Rays (adverse effects).
- MESH :
- chemical , deficiency : Endopeptidases.
- chemical , genetics : Endopeptidases.
- chemical , metabolism : DNA-Binding Proteins, Endopeptidases, Histones, Ubiquitin.
- adverse effects : X-Rays.
- radiation effects : Cell Survival, DNA Breaks, Double-Stranded, DNA Repair, Homologous Recombination.
- Cell Line, Gene Knockdown Techniques, Humans, Kinetics, Ubiquitin-Protein Ligases.
Abstract
During the DNA damage response (DDR), ubiquitination plays an important role in the recruitment and regulation of repair proteins. However, little is known about elimination of the ubiquitination signal after repair is completed. Here we show that the ubiquitin-specific protease 5 (USP5), a deubiquitinating enzyme, is involved in the elimination of the ubiquitin signal from damaged sites and is required for efficient DNA double-strand break (DSB) repair. Depletion of USP5 sensitizes cells to DNA damaging agents, produces DSBs, causes delayed disappearance of γH2AX foci after Bleocin treatment, and influences DSB repair efficiency in the homologous recombination pathway but not in the non-homologous end joining pathway. USP5 co-localizes to DSBs induced by laser micro-irradiation in a RAD18-dependent manner. Importantly, polyubiquitin chains at sites of DNA damage remained for longer periods in USP5-depleted cells. Our results show that disassembly of polyubiquitin chains by USP5 at sites of damage is important for efficient DSB repair.
Url:
DOI: 10.1371/journal.pone.0084899
PubMed: 24454762
PubMed Central: 3891734
Affiliations:
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id="aff1"><addr-line>Department of Microbiology and Molecular Genetics and University of Pittsburgh Cancer Institute, University of Pittsburgh School of Medicine, Pittsburgh, Pennsylvania, United States of America</addr-line></nlm:aff><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Microbiology and Molecular Genetics and University of Pittsburgh Cancer Institute, University of Pittsburgh School of Medicine, Pittsburgh, Pennsylvania</wicri:regionArea><placeName><region type="state">Pennsylvanie</region></placeName></affiliation></author><author><name sortKey="Hsieh, Ching Lung" sort="Hsieh, Ching Lung" uniqKey="Hsieh C" first="Ching-Lung" last="Hsieh">Ching-Lung Hsieh</name><affiliation wicri:level="2"><nlm:aff id="aff1"><addr-line>Department of Microbiology and Molecular Genetics and University of Pittsburgh Cancer Institute, University of Pittsburgh School of Medicine, Pittsburgh, Pennsylvania, United States of America</addr-line></nlm:aff><country 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Pennsylvania</wicri:regionArea><placeName><region type="state">Pennsylvanie</region></placeName></affiliation></author><author><name sortKey="Yasui, Akira" sort="Yasui, Akira" uniqKey="Yasui A" first="Akira" last="Yasui">Akira Yasui</name><affiliation wicri:level="4"><nlm:aff id="aff2"><addr-line>Division of the Dynamic Proteome, Institute of Development, Aging, and Cancer, Tohoku University, Sendai, Japan</addr-line></nlm:aff><country xml:lang="fr">Japon</country><wicri:regionArea>Division of the Dynamic Proteome, Institute of Development, Aging, and Cancer, Tohoku University, Sendai</wicri:regionArea><orgName type="university">Université du Tōhoku</orgName><placeName><settlement type="city">Sendai</settlement><region type="province">Région de Tōhoku</region></placeName></affiliation></author><author><name sortKey="Levine, Arthur S" sort="Levine, Arthur S" uniqKey="Levine A" first="Arthur S." last="Levine">Arthur S. Levine</name><affiliation wicri:level="2"><nlm:aff id="aff1"><addr-line>Department of Microbiology and Molecular Genetics and University of Pittsburgh Cancer Institute, University of Pittsburgh School of Medicine, Pittsburgh, Pennsylvania, United States of America</addr-line></nlm:aff><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Microbiology and Molecular Genetics and University of Pittsburgh Cancer Institute, University of Pittsburgh School of Medicine, Pittsburgh, Pennsylvania</wicri:regionArea><placeName><region type="state">Pennsylvanie</region></placeName></affiliation></author></analytic><series><title level="j">PLoS ONE</title><idno type="eISSN">1932-6203</idno><imprint><date when="2014">2014</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Cell Line</term><term>Cell Survival (radiation effects)</term><term>DNA Breaks, Double-Stranded (radiation effects)</term><term>DNA Repair (radiation effects)</term><term>DNA-Binding Proteins (metabolism)</term><term>Endopeptidases (deficiency)</term><term>Endopeptidases (genetics)</term><term>Endopeptidases (metabolism)</term><term>Gene Knockdown Techniques</term><term>Histones (metabolism)</term><term>Homologous Recombination (radiation effects)</term><term>Humans</term><term>Kinetics</term><term>Ubiquitin (metabolism)</term><term>Ubiquitin-Protein Ligases</term><term>X-Rays (adverse effects)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Cassures double-brin de l'ADN (effets des radiations)</term><term>Cinétique</term><term>Endopeptidases (déficit)</term><term>Endopeptidases (génétique)</term><term>Endopeptidases (métabolisme)</term><term>Histone (métabolisme)</term><term>Humains</term><term>Lignée cellulaire</term><term>Protéines de liaison à l'ADN (métabolisme)</term><term>Rayons X (effets indésirables)</term><term>Recombinaison homologue (effets des radiations)</term><term>Réparation de l'ADN (effets des radiations)</term><term>Survie cellulaire (effets des radiations)</term><term>Techniques de knock-down de gènes</term><term>Ubiquitin-protein ligases</term><term>Ubiquitine (métabolisme)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="deficiency" xml:lang="en"><term>Endopeptidases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Endopeptidases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>DNA-Binding Proteins</term><term>Endopeptidases</term><term>Histones</term><term>Ubiquitin</term></keywords><keywords scheme="MESH" qualifier="adverse effects" xml:lang="en"><term>X-Rays</term></keywords><keywords scheme="MESH" qualifier="déficit" xml:lang="fr"><term>Endopeptidases</term></keywords><keywords scheme="MESH" qualifier="effets des radiations" xml:lang="fr"><term>Cassures double-brin de l'ADN</term><term>Recombinaison homologue</term><term>Réparation de l'ADN</term><term>Survie cellulaire</term></keywords><keywords scheme="MESH" qualifier="effets indésirables" xml:lang="fr"><term>Rayons X</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Endopeptidases</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Endopeptidases</term><term>Histone</term><term>Protéines de liaison à l'ADN</term><term>Ubiquitine</term></keywords><keywords scheme="MESH" qualifier="radiation effects" xml:lang="en"><term>Cell Survival</term><term>DNA Breaks, Double-Stranded</term><term>DNA Repair</term><term>Homologous Recombination</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Cell Line</term><term>Gene Knockdown Techniques</term><term>Humans</term><term>Kinetics</term><term>Ubiquitin-Protein Ligases</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Cinétique</term><term>Humains</term><term>Lignée cellulaire</term><term>Techniques de knock-down de gènes</term><term>Ubiquitin-protein ligases</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p>During the DNA damage response (DDR), ubiquitination plays an important role in the recruitment and regulation of repair proteins. However, little is known about elimination of the ubiquitination signal after repair is completed. Here we show that the ubiquitin-specific protease 5 (USP5), a deubiquitinating enzyme, is involved in the elimination of the ubiquitin signal from damaged sites and is required for efficient DNA double-strand break (DSB) repair. Depletion of USP5 sensitizes cells to DNA damaging agents, produces DSBs, causes delayed disappearance of γH2AX foci after Bleocin treatment, and influences DSB repair efficiency in the homologous recombination pathway but not in the non-homologous end joining pathway. USP5 co-localizes to DSBs induced by laser micro-irradiation in a RAD18-dependent manner. Importantly, polyubiquitin chains at sites of DNA damage remained for longer periods in USP5-depleted cells. Our results show that disassembly of polyubiquitin chains by USP5 at sites of damage is important for efficient DSB repair.</p></div></front><back><div1 type="bibliography"><listBibl><biblStruct><analytic><author><name sortKey="Ciccia, A" uniqKey="Ciccia A">A Ciccia</name></author><author><name sortKey="Elledge, Sj" uniqKey="Elledge S">SJ Elledge</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Jackson, Sp" uniqKey="Jackson S">SP Jackson</name></author><author><name sortKey="Bartek, J" uniqKey="Bartek J">J Bartek</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Polo, Se" uniqKey="Polo S">SE Polo</name></author><author><name sortKey="Jackson, Sp" uniqKey="Jackson S">SP Jackson</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Van Attikum, H" uniqKey="Van Attikum H">H van Attikum</name></author><author><name sortKey="Gasser, Sm" uniqKey="Gasser S">SM 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Ulbrich</name></author><author><name sortKey="Matsuda, A" uniqKey="Matsuda A">A Matsuda</name></author><author><name sortKey="Reddy, Va" uniqKey="Reddy V">VA Reddy</name></author></analytic></biblStruct></listBibl></div1></back></TEI><affiliations><list><country><li>Japon</li><li>États-Unis</li></country><region><li>Pennsylvanie</li><li>Région de Tōhoku</li></region><settlement><li>Sendai</li></settlement><orgName><li>Université du Tōhoku</li></orgName></list><tree><country name="États-Unis"><region name="Pennsylvanie"><name sortKey="Nakajima, Satoshi" sort="Nakajima, Satoshi" uniqKey="Nakajima S" first="Satoshi" last="Nakajima">Satoshi Nakajima</name></region><name sortKey="Hsieh, Ching Lung" sort="Hsieh, Ching Lung" uniqKey="Hsieh C" first="Ching-Lung" last="Hsieh">Ching-Lung Hsieh</name><name sortKey="Lan, Li" sort="Lan, Li" uniqKey="Lan L" first="Li" last="Lan">Li Lan</name><name sortKey="Levine, Arthur S" sort="Levine, Arthur S" uniqKey="Levine A" first="Arthur S." last="Levine">Arthur S. Levine</name><name sortKey="Rapi Otrin, Vesna" sort="Rapi Otrin, Vesna" uniqKey="Rapi Otrin V" first="Vesna" last="Rapi Otrin">Vesna Rapi Otrin</name><name sortKey="Wei, Leizhen" sort="Wei, Leizhen" uniqKey="Wei L" first="Leizhen" last="Wei">Leizhen Wei</name></country><country name="Japon"><region name="Région de Tōhoku"><name sortKey="Yasui, Akira" sort="Yasui, Akira" uniqKey="Yasui A" first="Akira" last="Yasui">Akira Yasui</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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