RAD50 phosphorylation promotes ATR downstream signaling and DNA restart following replication stress.
Identifieur interne : 003258 ( PubMed/Checkpoint ); précédent : 003257; suivant : 003259RAD50 phosphorylation promotes ATR downstream signaling and DNA restart following replication stress.
Auteurs : Magtouf Gatei [Australie] ; Amanda W. Kijas [Australie] ; Denis Biard [France] ; Thilo Dörk ; Martin F. Lavin [Australie]Source :
- Human molecular genetics [ 1460-2083 ] ; 2014.
Descripteurs français
- KwdFr :
- Ataxie-télangiectasie (anatomopathologie), Cassures double-brin de l'ADN, Checkpoint kinase 1, Enzymes de réparation de l'ADN (métabolisme), Fibroblastes, Humains, Lignée cellulaire, Phosphorylation, Protein kinases (métabolisme), Protéines de liaison à l'ADN (métabolisme), Réplication de l'ADN, Stress physiologique, Sérine (métabolisme), Transduction du signal.
- MESH :
- anatomopathologie : Ataxie-télangiectasie.
- métabolisme : Enzymes de réparation de l'ADN, Protein kinases, Protéines de liaison à l'ADN, Sérine.
- Cassures double-brin de l'ADN, Checkpoint kinase 1, Fibroblastes, Humains, Lignée cellulaire, Phosphorylation, Réplication de l'ADN, Stress physiologique, Transduction du signal.
English descriptors
- KwdEn :
- Ataxia Telangiectasia (pathology), Cell Line, Checkpoint Kinase 1, DNA Breaks, Double-Stranded, DNA Repair Enzymes (metabolism), DNA Replication, DNA-Binding Proteins (metabolism), Fibroblasts, Humans, Phosphorylation, Protein Kinases (metabolism), Serine (metabolism), Signal Transduction, Stress, Physiological.
- MESH :
- chemical , metabolism : DNA Repair Enzymes, DNA-Binding Proteins, Protein Kinases, Serine.
- chemical : Checkpoint Kinase 1.
- pathology : Ataxia Telangiectasia.
- Cell Line, DNA Breaks, Double-Stranded, DNA Replication, Fibroblasts, Humans, Phosphorylation, Signal Transduction, Stress, Physiological.
Abstract
The MRE11/RAD50/NBN (MRN) complex plays a key role in detecting DNA double-strand breaks, recruiting and activating ataxia-telangiectasia mutated and in processing the breaks. Members of this complex also act as adaptor molecules for downstream signaling to the cell cycle and other cellular processes. Somewhat more controversial are the results to support a role for MRN in the ataxia-telangiectasia and Rad3-related (ATR) activation and signaling. We provide evidence that RAD50 is required for ATR activation in mammalian cells in response to DNA replication stress. It is in turn phosphorylated at a specific site (S635) by ATR, which is required for ATR signaling through Chk1 and other downstream substrates. We find that RAD50 phosphorylation is essential for DNA replication restart by promoting loading of cohesin at these sites. We also demonstrate that replication stress-induced RAD50 phosphorylation is functionally significant for cell survival and cell cycle checkpoint activation. These results highlight the importance of the adaptor role for a member of the MRN complex in all aspects of the response to DNA replication stress.
DOI: 10.1093/hmg/ddu141
PubMed: 24694934
Affiliations:
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Kijas</name><affiliation wicri:level="1"><nlm:affiliation>Radiation Biology and Oncology, QIMR Berghofer Medical Research Institute, Brisbane, QLD 4029, Australia.</nlm:affiliation><country xml:lang="fr">Australie</country><wicri:regionArea>Radiation Biology and Oncology, QIMR Berghofer Medical Research Institute, Brisbane, QLD 4029</wicri:regionArea><wicri:noRegion>QLD 4029</wicri:noRegion></affiliation></author><author><name sortKey="Biard, Denis" sort="Biard, Denis" uniqKey="Biard D" first="Denis" last="Biard">Denis Biard</name><affiliation wicri:level="1"><nlm:affiliation>CEA, DSV/iMETI/SEPIA; BP6, 92265 Fontenay-aux-Roses Cedex, France.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>CEA, DSV/iMETI/SEPIA; BP6, 92265 Fontenay-aux-Roses Cedex</wicri:regionArea><wicri:noRegion>92265 Fontenay-aux-Roses Cedex</wicri:noRegion><wicri:noRegion>92265 Fontenay-aux-Roses Cedex</wicri:noRegion></affiliation></author><author><name sortKey="Dork, Thilo" sort="Dork, Thilo" uniqKey="Dork T" first="Thilo" last="Dörk">Thilo Dörk</name><affiliation><nlm:affiliation>Clinics of Obstetrics and Gynaecology, Hannover Medical School, Gynaecology Research Unit, Carl-Neuberg-Str. 1, D-30625 Hannover, Germany and.</nlm:affiliation><wicri:noCountry code="subField">Germany and</wicri:noCountry></affiliation></author><author><name sortKey="Lavin, Martin F" sort="Lavin, Martin F" uniqKey="Lavin M" first="Martin F" last="Lavin">Martin F. Lavin</name><affiliation wicri:level="1"><nlm:affiliation>Radiation Biology and Oncology, QIMR Berghofer Medical Research Institute, Brisbane, QLD 4029, Australia Centre for Clinical Research, University of Queensland, Building 71/918, Royal Brisbane & Women's Hospital Campus, Herston, QLD 4029, Australia martin.lavin@qimrberghofer.edu.au m.lavin@uq.edu.au.</nlm:affiliation><country wicri:rule="url">Australie</country><wicri:regionArea>Radiation Biology and Oncology, QIMR Berghofer Medical Research Institute, Brisbane, QLD 4029, Australia Centre for Clinical Research, University of Queensland, Building 71/918, Royal Brisbane & Women's Hospital Campus, Herston, QLD 4029</wicri:regionArea><wicri:noRegion>QLD 4029</wicri:noRegion></affiliation></author></analytic><series><title level="j">Human molecular genetics</title><idno type="eISSN">1460-2083</idno><imprint><date when="2014" type="published">2014</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Ataxia Telangiectasia (pathology)</term><term>Cell Line</term><term>Checkpoint Kinase 1</term><term>DNA Breaks, Double-Stranded</term><term>DNA Repair Enzymes (metabolism)</term><term>DNA Replication</term><term>DNA-Binding Proteins (metabolism)</term><term>Fibroblasts</term><term>Humans</term><term>Phosphorylation</term><term>Protein Kinases (metabolism)</term><term>Serine (metabolism)</term><term>Signal Transduction</term><term>Stress, Physiological</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Ataxie-télangiectasie (anatomopathologie)</term><term>Cassures double-brin de l'ADN</term><term>Checkpoint kinase 1</term><term>Enzymes de réparation de l'ADN (métabolisme)</term><term>Fibroblastes</term><term>Humains</term><term>Lignée cellulaire</term><term>Phosphorylation</term><term>Protein kinases (métabolisme)</term><term>Protéines de liaison à l'ADN (métabolisme)</term><term>Réplication de l'ADN</term><term>Stress physiologique</term><term>Sérine (métabolisme)</term><term>Transduction du signal</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>DNA Repair Enzymes</term><term>DNA-Binding Proteins</term><term>Protein Kinases</term><term>Serine</term></keywords><keywords scheme="MESH" type="chemical" xml:lang="en"><term>Checkpoint Kinase 1</term></keywords><keywords scheme="MESH" qualifier="anatomopathologie" xml:lang="fr"><term>Ataxie-télangiectasie</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Enzymes de réparation de l'ADN</term><term>Protein kinases</term><term>Protéines de liaison à l'ADN</term><term>Sérine</term></keywords><keywords scheme="MESH" qualifier="pathology" xml:lang="en"><term>Ataxia Telangiectasia</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Cell Line</term><term>DNA Breaks, Double-Stranded</term><term>DNA Replication</term><term>Fibroblasts</term><term>Humans</term><term>Phosphorylation</term><term>Signal Transduction</term><term>Stress, Physiological</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Cassures double-brin de l'ADN</term><term>Checkpoint kinase 1</term><term>Fibroblastes</term><term>Humains</term><term>Lignée cellulaire</term><term>Phosphorylation</term><term>Réplication de l'ADN</term><term>Stress physiologique</term><term>Transduction du signal</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The MRE11/RAD50/NBN (MRN) complex plays a key role in detecting DNA double-strand breaks, recruiting and activating ataxia-telangiectasia mutated and in processing the breaks. Members of this complex also act as adaptor molecules for downstream signaling to the cell cycle and other cellular processes. Somewhat more controversial are the results to support a role for MRN in the ataxia-telangiectasia and Rad3-related (ATR) activation and signaling. We provide evidence that RAD50 is required for ATR activation in mammalian cells in response to DNA replication stress. It is in turn phosphorylated at a specific site (S635) by ATR, which is required for ATR signaling through Chk1 and other downstream substrates. We find that RAD50 phosphorylation is essential for DNA replication restart by promoting loading of cohesin at these sites. We also demonstrate that replication stress-induced RAD50 phosphorylation is functionally significant for cell survival and cell cycle checkpoint activation. These results highlight the importance of the adaptor role for a member of the MRN complex in all aspects of the response to DNA replication stress.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">24694934</PMID><DateCreated><Year>2014</Year><Month>07</Month><Day>19</Day></DateCreated><DateCompleted><Year>2016</Year><Month>03</Month><Day>22</Day></DateCompleted><DateRevised><Year>2016</Year><Month>11</Month><Day>25</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1460-2083</ISSN><JournalIssue CitedMedium="Internet"><Volume>23</Volume><Issue>16</Issue><PubDate><Year>2014</Year><Month>Aug</Month><Day>15</Day></PubDate></JournalIssue><Title>Human molecular genetics</Title><ISOAbbreviation>Hum. Mol. Genet.</ISOAbbreviation></Journal><ArticleTitle>RAD50 phosphorylation promotes ATR downstream signaling and DNA restart following replication stress.</ArticleTitle><Pagination><MedlinePgn>4232-48</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1093/hmg/ddu141</ELocationID><Abstract><AbstractText>The MRE11/RAD50/NBN (MRN) complex plays a key role in detecting DNA double-strand breaks, recruiting and activating ataxia-telangiectasia mutated and in processing the breaks. Members of this complex also act as adaptor molecules for downstream signaling to the cell cycle and other cellular processes. Somewhat more controversial are the results to support a role for MRN in the ataxia-telangiectasia and Rad3-related (ATR) activation and signaling. We provide evidence that RAD50 is required for ATR activation in mammalian cells in response to DNA replication stress. It is in turn phosphorylated at a specific site (S635) by ATR, which is required for ATR signaling through Chk1 and other downstream substrates. We find that RAD50 phosphorylation is essential for DNA replication restart by promoting loading of cohesin at these sites. We also demonstrate that replication stress-induced RAD50 phosphorylation is functionally significant for cell survival and cell cycle checkpoint activation. These results highlight the importance of the adaptor role for a member of the MRN complex in all aspects of the response to DNA replication stress.</AbstractText><CopyrightInformation>© The Author 2014. Published by Oxford University Press. All rights reserved. For Permissions, please email: journals.permissions@oup.com.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Gatei</LastName><ForeName>Magtouf</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Radiation Biology and Oncology, QIMR Berghofer Medical Research Institute, Brisbane, QLD 4029, Australia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Kijas</LastName><ForeName>Amanda W</ForeName><Initials>AW</Initials><AffiliationInfo><Affiliation>Radiation Biology and Oncology, QIMR Berghofer Medical Research Institute, Brisbane, QLD 4029, Australia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Biard</LastName><ForeName>Denis</ForeName><Initials>D</Initials><AffiliationInfo><Affiliation>CEA, DSV/iMETI/SEPIA; BP6, 92265 Fontenay-aux-Roses Cedex, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Dörk</LastName><ForeName>Thilo</ForeName><Initials>T</Initials><AffiliationInfo><Affiliation>Clinics of Obstetrics and Gynaecology, Hannover Medical School, Gynaecology Research Unit, Carl-Neuberg-Str. 1, D-30625 Hannover, Germany and.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Lavin</LastName><ForeName>Martin F</ForeName><Initials>MF</Initials><AffiliationInfo><Affiliation>Radiation Biology and Oncology, QIMR Berghofer Medical Research Institute, Brisbane, QLD 4029, Australia Centre for Clinical Research, University of Queensland, Building 71/918, Royal Brisbane & Women's Hospital Campus, Herston, QLD 4029, Australia martin.lavin@qimrberghofer.edu.au m.lavin@uq.edu.au.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2014</Year><Month>04</Month><Day>02</Day></ArticleDate></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>Hum Mol Genet</MedlineTA><NlmUniqueID>9208958</NlmUniqueID><ISSNLinking>0964-6906</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D004268">DNA-Binding Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C112158">Rad50 protein, human</NameOfSubstance></Chemical><Chemical><RegistryNumber>452VLY9402</RegistryNumber><NameOfSubstance UI="D012694">Serine</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.-</RegistryNumber><NameOfSubstance UI="D011494">Protein Kinases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.11.1</RegistryNumber><NameOfSubstance UI="C000605867">CHEK1 protein, human</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.11.1</RegistryNumber><NameOfSubstance UI="D000071877">Checkpoint Kinase 1</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 6.5.1.-</RegistryNumber><NameOfSubstance UI="D045643">DNA Repair Enzymes</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D001260" MajorTopicYN="N">Ataxia Telangiectasia</DescriptorName><QualifierName UI="Q000473" MajorTopicYN="Y">pathology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D002460" MajorTopicYN="N">Cell Line</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000071877" MajorTopicYN="N">Checkpoint Kinase 1</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D053903" MajorTopicYN="Y">DNA Breaks, Double-Stranded</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D045643" MajorTopicYN="N">DNA Repair Enzymes</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004261" MajorTopicYN="Y">DNA Replication</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004268" MajorTopicYN="N">DNA-Binding Proteins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005347" MajorTopicYN="N">Fibroblasts</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010766" MajorTopicYN="N">Phosphorylation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011494" MajorTopicYN="N">Protein Kinases</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D012694" MajorTopicYN="N">Serine</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D015398" MajorTopicYN="Y">Signal Transduction</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013312" MajorTopicYN="N">Stress, Physiological</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="entrez"><Year>2014</Year><Month>4</Month><Day>4</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2014</Year><Month>4</Month><Day>4</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2016</Year><Month>3</Month><Day>24</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">24694934</ArticleId><ArticleId IdType="pii">ddu141</ArticleId><ArticleId IdType="doi">10.1093/hmg/ddu141</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Australie</li><li>France</li></country></list><tree><noCountry><name sortKey="Dork, Thilo" sort="Dork, Thilo" uniqKey="Dork T" first="Thilo" last="Dörk">Thilo Dörk</name></noCountry><country name="Australie"><noRegion><name sortKey="Gatei, Magtouf" sort="Gatei, Magtouf" uniqKey="Gatei M" first="Magtouf" last="Gatei">Magtouf Gatei</name></noRegion><name sortKey="Kijas, Amanda W" sort="Kijas, Amanda W" uniqKey="Kijas A" first="Amanda W" last="Kijas">Amanda W. Kijas</name><name sortKey="Lavin, Martin F" sort="Lavin, Martin F" uniqKey="Lavin M" first="Martin F" last="Lavin">Martin F. Lavin</name></country><country name="France"><noRegion><name sortKey="Biard, Denis" sort="Biard, Denis" uniqKey="Biard D" first="Denis" last="Biard">Denis Biard</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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