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Article: Ring finger protein RNF169 antagonizes the ubiquitin-dependent signaling cascade at sites of DNA damage

TitleRing finger protein RNF169 antagonizes the ubiquitin-dependent signaling cascade at sites of DNA damage
Authors
Issue Date2012
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, 2012, v. 287 n. 33, p. 27715-27722 How to Cite?
AbstractUbiquitin signals emanating from DNA double-strand breaks (DSBs) trigger the ordered assembly of DNA damage mediator and repair proteins. This highly orchestrated process is accomplished, in part, through the concerted action of the RNF8 and RNF168 E3 ligases, which have emerged as core signaling intermediates that promote DSB-associated ubiquitylation events. In this study, we report the identification of RNF169 as a negative regulator of the DNA damage signaling cascade. We found that RNF169 interacted with ubiquitin structures and relocalized to DSBs in an RNF8/RNF168-dependent manner. Moreover, ectopic expression of RNF169 attenuated ubiquitin signaling and compromised 53BP1 accumulation at DNA damage sites, suggesting that RNF169 antagonizes RNF168 functions at DSBs. Our study unveils RNF169 as a component in DNA damage signal transduction and adds to the complexity of regulatory ubiquitylation in genome stability maintenance.
Persistent Identifierhttp://hdl.handle.net/10722/152621
ISSN
2014 Impact Factor: 4.573
2014 SCImago Journal Rankings: 2.734
PubMed Central ID
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorChen, Jen_US
dc.contributor.authorFeng, Wen_US
dc.contributor.authorJiang, Jen_US
dc.contributor.authorDeng, Yen_US
dc.contributor.authorHuen, MSYen_US
dc.date.accessioned2012-07-16T09:44:13Z-
dc.date.available2012-07-16T09:44:13Z-
dc.date.issued2012en_US
dc.identifier.citationJournal of Biological Chemistry, 2012, v. 287 n. 33, p. 27715-27722en_US
dc.identifier.issn0021-9258-
dc.identifier.urihttp://hdl.handle.net/10722/152621-
dc.description.abstractUbiquitin signals emanating from DNA double-strand breaks (DSBs) trigger the ordered assembly of DNA damage mediator and repair proteins. This highly orchestrated process is accomplished, in part, through the concerted action of the RNF8 and RNF168 E3 ligases, which have emerged as core signaling intermediates that promote DSB-associated ubiquitylation events. In this study, we report the identification of RNF169 as a negative regulator of the DNA damage signaling cascade. We found that RNF169 interacted with ubiquitin structures and relocalized to DSBs in an RNF8/RNF168-dependent manner. Moreover, ectopic expression of RNF169 attenuated ubiquitin signaling and compromised 53BP1 accumulation at DNA damage sites, suggesting that RNF169 antagonizes RNF168 functions at DSBs. Our study unveils RNF169 as a component in DNA damage signal transduction and adds to the complexity of regulatory ubiquitylation in genome stability maintenance.-
dc.languageengen_US
dc.publisherAmerican Society for Biochemistry and Molecular Biology, Inc. The Journal's web site is located at http://www.jbc.org/-
dc.relation.ispartofJournal of Biological Chemistryen_US
dc.rightsJournal of Biological Chemistry. Copyright © American Society for Biochemistry and Molecular Biology, Inc.-
dc.subject.meshDNA Breaks, Double-Stranded-
dc.subject.meshDNA-Binding Proteins - genetics - metabolism-
dc.subject.meshSignal Transduction-
dc.subject.meshUbiquitin - genetics - metabolism-
dc.subject.meshUbiquitin-Protein Ligases - genetics - metabolism-
dc.titleRing finger protein RNF169 antagonizes the ubiquitin-dependent signaling cascade at sites of DNA damageen_US
dc.typeArticleen_US
dc.identifier.emailFeng, W: fengwj83@hku.hken_US
dc.identifier.emailDeng, Y: yqdeng@scau.edu.cnen_US
dc.identifier.emailHuen, MSY: huen.michael@hku.hk-
dc.identifier.authorityHuen, MSY=rp01336en_US
dc.description.naturelink_to_OA_fulltext-
dc.identifier.doi10.1074/jbc.M112.373530-
dc.identifier.pmid22733822-
dc.identifier.pmcidPMC3431699-
dc.identifier.scopuseid_2-s2.0-84864977706-
dc.identifier.hkuros201054en_US
dc.identifier.volume287-
dc.identifier.issue33-
dc.identifier.spage27715en_US
dc.identifier.epage27722en_US
dc.identifier.isiWOS:000307840700045-
dc.publisher.placeUnited States-

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