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

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TitleRing finger protein RNF169 antagonizes the ubiquitin-dependent signaling cascade at sites of DNA damage
AuthorsChen, J1
Feng, W1 2
Jiang, J2
Deng, Y2
Huen, MSY1
Issue Date2012
PublisherAmerican Society for Biochemistry and Molecular Biology, Inc. The Journal's web site is located at http://www.jbc.org/
CitationJournal of Biological Chemistry, 2012, v. 287 n. 33, p. 27715-27722 [How to Cite?]
DOI: http://dx.doi.org/10.1074/jbc.M112.373530
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.
ISSN0021-9258
2011 Impact Factor: 4.773
2011 SCImago Journal Rankings: 0.793
DOIhttp://dx.doi.org/10.1074/jbc.M112.373530
PubMed Central IDPMC3431699
DC Field
Value
dc.contributor.authorChen, J
dc.contributor.authorFeng, W
dc.contributor.authorJiang, J
dc.contributor.authorDeng, Y
dc.contributor.authorHuen, MSY
dc.date.accessioned2012-07-16T09:44:13Z
dc.date.available2012-07-16T09:44:13Z
dc.date.issued2012
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.description.natureLink_to_subscribed_fulltext
dc.identifier.citationJournal of Biological Chemistry, 2012, v. 287 n. 33, p. 27715-27722 [How to Cite?]
DOI: http://dx.doi.org/10.1074/jbc.M112.373530
dc.identifier.doihttp://dx.doi.org/10.1074/jbc.M112.373530
dc.identifier.epage27722
dc.identifier.hkuros201054
dc.identifier.issn0021-9258
2011 Impact Factor: 4.773
2011 SCImago Journal Rankings: 0.793
dc.identifier.issue33
dc.identifier.pmcidPMC3431699
dc.identifier.pmid22733822
dc.identifier.scopuseid_2-s2.0-84864977706
dc.identifier.spage27715
dc.identifier.urihttp://hdl.handle.net/10722/152621
dc.identifier.volume287
dc.languageeng
dc.publisherAmerican Society for Biochemistry and Molecular Biology, Inc. The Journal's web site is located at http://www.jbc.org/
dc.publisher.placeUnited States
dc.relation.ispartofJournal of Biological Chemistry
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 damage
dc.typeArticle
Author Affiliations
  1. The University of Hong Kong
  2. South China Agricultural University