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Article: Critical roles of ring finger protein RNF8 in replication stress responses

TitleCritical roles of ring finger protein RNF8 in replication stress responses
Authors
Issue Date2011
PublisherAmerican Society for Biochemistry and Molecular Biology, Inc. The Journal's web site is located at http://www.jbc.org/
Citation
Journal Of Biological Chemistry, 2011, v. 286 n. 25, p. 22355-22361 How to Cite?
AbstractHistone ubiquitylation is emerging as an important protective component in cellular responses to DNA damage. The ubiquitin ligases RNF8 and RNF168 assemble ubiquitin chains onto histone molecules surrounding DNA breaks and facilitate retention of DNA repair proteins. Although RNF8 and RNF168 play important roles in repair of DNA double strand breaks, their requirement for cell protection from replication stress is largely unknown. In this study, we uncovered RNF168-independent roles of RNF8 in repair of replication inhibition-induced DNA damage. We showed that RNF8 depletion, but not RNF168 depletion, hyper-sensitized cells to hydroxyurea and aphidicolin treatment. Consistently, hydroxyurea induced persistent single strand DNA lesions and sustained CHK1 activation in RNF8-depleted cells. In line with strict requirement for RAD51-dependent repair of hydroxyurea-stalled replication forks, RNF8 depletion compromised RAD51 accumulation onto single strand DNA lesions, suggesting that impaired replication fork repair may underlie the enhanced cellular sensitivity to replication arrest observed in RNF8-depleted cells. In total, our study highlights the differential requirement for the ubiquitin ligase RNF8 in facilitating repair of replication stress-associated DNA damage. © 2011 by The American Society for Biochemistry and Molecular Biology, Inc.
Persistent Identifierhttp://hdl.handle.net/10722/135012
ISSN
2015 Impact Factor: 4.258
2015 SCImago Journal Rankings: 3.151
PubMed Central ID
ISI Accession Number ID
Funding AgencyGrant Number
Faculty Development Fund and Seed Funding Programme for Applied Research201007160001
National Basic Research Program of China (973 Program)2009CB118802
Guangdong Province Universities and Colleges Pearl River Scholar Funded Scheme
Funding Information:

This work was supported by the Faculty Development Fund and Seed Funding Programme for Applied Research (Project Code 201007160001, to M. S. Y. H.), by grants from the National Basic Research Program of China (973 Program, Grant 2009CB118802, to M. S. Y. H. and Y. D.), and by Guangdong Province Universities and Colleges Pearl River Scholar Funded Scheme (2009, to Y. D.).

References

 

DC FieldValueLanguage
dc.contributor.authorSy, SMHen_HK
dc.contributor.authorJiang, Jen_HK
dc.contributor.authorDong, SSen_HK
dc.contributor.authorLok, GTMen_HK
dc.contributor.authorWu, Jen_HK
dc.contributor.authorCai, Hen_HK
dc.contributor.authorYeung, ESLen_HK
dc.contributor.authorHuang, Jen_HK
dc.contributor.authorChen, Jen_HK
dc.contributor.authorDeng, Yen_HK
dc.contributor.authorHuen, MSYen_HK
dc.date.accessioned2011-07-27T01:25:48Z-
dc.date.available2011-07-27T01:25:48Z-
dc.date.issued2011en_HK
dc.identifier.citationJournal Of Biological Chemistry, 2011, v. 286 n. 25, p. 22355-22361en_HK
dc.identifier.issn0021-9258en_HK
dc.identifier.urihttp://hdl.handle.net/10722/135012-
dc.description.abstractHistone ubiquitylation is emerging as an important protective component in cellular responses to DNA damage. The ubiquitin ligases RNF8 and RNF168 assemble ubiquitin chains onto histone molecules surrounding DNA breaks and facilitate retention of DNA repair proteins. Although RNF8 and RNF168 play important roles in repair of DNA double strand breaks, their requirement for cell protection from replication stress is largely unknown. In this study, we uncovered RNF168-independent roles of RNF8 in repair of replication inhibition-induced DNA damage. We showed that RNF8 depletion, but not RNF168 depletion, hyper-sensitized cells to hydroxyurea and aphidicolin treatment. Consistently, hydroxyurea induced persistent single strand DNA lesions and sustained CHK1 activation in RNF8-depleted cells. In line with strict requirement for RAD51-dependent repair of hydroxyurea-stalled replication forks, RNF8 depletion compromised RAD51 accumulation onto single strand DNA lesions, suggesting that impaired replication fork repair may underlie the enhanced cellular sensitivity to replication arrest observed in RNF8-depleted cells. In total, our study highlights the differential requirement for the ubiquitin ligase RNF8 in facilitating repair of replication stress-associated DNA damage. © 2011 by The American Society for Biochemistry and Molecular Biology, Inc.en_HK
dc.languageengen_US
dc.publisherAmerican Society for Biochemistry and Molecular Biology, Inc. The Journal's web site is located at http://www.jbc.org/en_HK
dc.relation.ispartofJournal of Biological Chemistryen_HK
dc.rightsJournal of Biological Chemistry. Copyright © American Society for Biochemistry and Molecular Biology, Inc.-
dc.subject.meshCell Line-
dc.subject.meshCell Survival - drug effects-
dc.subject.meshDNA Damage-
dc.subject.meshDNA Replication - drug effects - genetics-
dc.subject.meshDNA-Binding Proteins - deficiency - metabolism-
dc.titleCritical roles of ring finger protein RNF8 in replication stress responsesen_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=0021-9258&volume=286&spage=22355&epage=22361&date=2011&atitle=Critical+roles+of+ring+finger+protein+RNF8+in+replication+stress+responses-
dc.identifier.emailHuen, MSY:huen.michael@hku.hken_HK
dc.identifier.authorityHuen, MSY=rp01336en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1074/jbc.M111.232041en_HK
dc.identifier.pmid21558560-
dc.identifier.pmcidPMC3121383-
dc.identifier.scopuseid_2-s2.0-79959326643en_HK
dc.identifier.hkuros186731en_US
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-79959326643&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume286en_HK
dc.identifier.issue25en_HK
dc.identifier.spage22355en_HK
dc.identifier.epage22361en_HK
dc.identifier.eissn1083-351X-
dc.identifier.isiWOS:000291719900045-
dc.publisher.placeUnited Statesen_HK
dc.identifier.scopusauthoridSy, SMH=54901413200en_HK
dc.identifier.scopusauthoridJiang, J=24776301400en_HK
dc.identifier.scopusauthoridDong, SS=35788109500en_HK
dc.identifier.scopusauthoridLok, GTM=44161157700en_HK
dc.identifier.scopusauthoridWu, J=40762461200en_HK
dc.identifier.scopusauthoridCai, H=7202853215en_HK
dc.identifier.scopusauthoridYeung, ESL=54409746400en_HK
dc.identifier.scopusauthoridHuang, J=30767499300en_HK
dc.identifier.scopusauthoridChen, J=35261693300en_HK
dc.identifier.scopusauthoridDeng, Y=7401531432en_HK
dc.identifier.scopusauthoridHuen, MSY=23004751500en_HK

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