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Article: RAD18-BRCTx interaction is required for efficient repair of UV-induced DNA damage
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TitleRAD18-BRCTx interaction is required for efficient repair of UV-induced DNA damage
 
AuthorsLiu, T2
Chen, H2
Kim, H4
Huen, MSY1
Chen, J3
Huang, J2
 
KeywordsBRCT domain
DNA damage
DNA repair
RAD18
 
Issue Date2012
 
PublisherElsevier BV. The Journal's web site is located at http://www.elsevier.com/locate/dnarepair
 
CitationDna Repair, 2012, v. 11 n. 2, p. 131-138 [How to Cite?]
DOI: http://dx.doi.org/10.1016/j.dnarep.2011.10.012
 
AbstractBRCA1 carboxyl-terminal (BRCT) motifs are present in a number of proteins involved in DNA repair and/or DNA damage signaling pathways. The BRCT domain-containing protein BRCTx has been shown to interact physically with RAD18, an E3 ligase involved in postreplication repair and homologous recombination repair. However, the physiological relevance of the interaction between RAD18 and BRCTx is largely unknown. In this study, we showed that RAD18 interacts with BRCTx in a phosphorylation-dependent manner and that this interaction, mediated via highly conserved serine residues on the RAD18 C terminus, is required for BRCTx accumulation at DNA damage sites. Furthermore, we uncovered critical roles of the RAD18-BRCTx module in UV-induced DNA damage repair but not PCNA mono-ubiquitination or homologous recombination. Thus, our results suggest that RAD18 has an additional function in the surveillance of the UV-induced DNA damage response signal. © 2011 Elsevier B.V..
 
ISSN1568-7864
2013 Impact Factor: 3.362
2013 SCImago Journal Rankings: 2.917
 
DOIhttp://dx.doi.org/10.1016/j.dnarep.2011.10.012
 
ISI Accession Number IDWOS:000301618900005
Funding AgencyGrant Number
National Natural Science Foundation of China31071243
Natural Science Foundation of Zhejiang ProvinceR2110569
China's Fundamental Research Funds for the Central Universities
Department of DefenseW81XWH-05-1-0470
Funding Information:

We would like to thank Dr. M. Yamaizumi for providing RAD18-/- MEFs and all our colleagues in the Huang laboratory for insightful discussions and technical assistance. This work was supported in part by grants from the National Natural Science Foundation of China (grant 31071243), the Natural Science Foundation of Zhejiang Province (grant R2110569) and the China's Fundamental Research Funds for the Central Universities. J.C. is a recipient of an Era of Hope Scholar award from the Department of Defense (W81XWH-05-1-0470) and a member of MD Anderson Cancer Center (CA016672).

 
ReferencesReferences in Scopus
 
DC FieldValue
dc.contributor.authorLiu, T
 
dc.contributor.authorChen, H
 
dc.contributor.authorKim, H
 
dc.contributor.authorHuen, MSY
 
dc.contributor.authorChen, J
 
dc.contributor.authorHuang, J
 
dc.date.accessioned2012-02-03T06:11:41Z
 
dc.date.available2012-02-03T06:11:41Z
 
dc.date.issued2012
 
dc.description.abstractBRCA1 carboxyl-terminal (BRCT) motifs are present in a number of proteins involved in DNA repair and/or DNA damage signaling pathways. The BRCT domain-containing protein BRCTx has been shown to interact physically with RAD18, an E3 ligase involved in postreplication repair and homologous recombination repair. However, the physiological relevance of the interaction between RAD18 and BRCTx is largely unknown. In this study, we showed that RAD18 interacts with BRCTx in a phosphorylation-dependent manner and that this interaction, mediated via highly conserved serine residues on the RAD18 C terminus, is required for BRCTx accumulation at DNA damage sites. Furthermore, we uncovered critical roles of the RAD18-BRCTx module in UV-induced DNA damage repair but not PCNA mono-ubiquitination or homologous recombination. Thus, our results suggest that RAD18 has an additional function in the surveillance of the UV-induced DNA damage response signal. © 2011 Elsevier B.V..
 
dc.description.naturelink_to_subscribed_fulltext
 
dc.identifier.citationDna Repair, 2012, v. 11 n. 2, p. 131-138 [How to Cite?]
DOI: http://dx.doi.org/10.1016/j.dnarep.2011.10.012
 
dc.identifier.citeulike10008825
 
dc.identifier.doihttp://dx.doi.org/10.1016/j.dnarep.2011.10.012
 
dc.identifier.epage138
 
dc.identifier.hkuros198267
 
dc.identifier.isiWOS:000301618900005
Funding AgencyGrant Number
National Natural Science Foundation of China31071243
Natural Science Foundation of Zhejiang ProvinceR2110569
China's Fundamental Research Funds for the Central Universities
Department of DefenseW81XWH-05-1-0470
Funding Information:

We would like to thank Dr. M. Yamaizumi for providing RAD18-/- MEFs and all our colleagues in the Huang laboratory for insightful discussions and technical assistance. This work was supported in part by grants from the National Natural Science Foundation of China (grant 31071243), the Natural Science Foundation of Zhejiang Province (grant R2110569) and the China's Fundamental Research Funds for the Central Universities. J.C. is a recipient of an Era of Hope Scholar award from the Department of Defense (W81XWH-05-1-0470) and a member of MD Anderson Cancer Center (CA016672).

 
dc.identifier.issn1568-7864
2013 Impact Factor: 3.362
2013 SCImago Journal Rankings: 2.917
 
dc.identifier.issue2
 
dc.identifier.pmid22036607
 
dc.identifier.scopuseid_2-s2.0-84855851489
 
dc.identifier.spage131
 
dc.identifier.urihttp://hdl.handle.net/10722/144510
 
dc.identifier.volume11
 
dc.languageeng
 
dc.publisherElsevier BV. The Journal's web site is located at http://www.elsevier.com/locate/dnarepair
 
dc.publisher.placeNetherlands
 
dc.relation.ispartofDNA Repair
 
dc.relation.referencesReferences in Scopus
 
dc.subjectBRCT domain
 
dc.subjectDNA damage
 
dc.subjectDNA repair
 
dc.subjectRAD18
 
dc.titleRAD18-BRCTx interaction is required for efficient repair of UV-induced DNA damage
 
dc.typeArticle
 
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Author Affiliations
  1. The University of Hong Kong
  2. Zhejiang University
  3. University of Texas M. D. Anderson Cancer Center
  4. Sungkyunkwan University