File Download

There are no files associated with this item.

  Links for fulltext
     (May Require Subscription)
Supplementary

Article: RAD18-BRCTx interaction is required for efficient repair of UV-induced DNA damage

TitleRAD18-BRCTx interaction is required for efficient repair of UV-induced DNA damage
Authors
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
Citation
Dna Repair, 2012, v. 11 n. 2, p. 131-138 How to Cite?
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..
Persistent Identifierhttp://hdl.handle.net/10722/144510
ISSN
2023 Impact Factor: 3.0
2023 SCImago Journal Rankings: 1.906
ISI Accession Number ID
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).

References

 

DC FieldValueLanguage
dc.contributor.authorLiu, Ten_HK
dc.contributor.authorChen, Hen_HK
dc.contributor.authorKim, Hen_HK
dc.contributor.authorHuen, MSYen_HK
dc.contributor.authorChen, Jen_HK
dc.contributor.authorHuang, Jen_HK
dc.date.accessioned2012-02-03T06:11:41Z-
dc.date.available2012-02-03T06:11:41Z-
dc.date.issued2012en_HK
dc.identifier.citationDna Repair, 2012, v. 11 n. 2, p. 131-138en_HK
dc.identifier.issn1568-7864en_HK
dc.identifier.urihttp://hdl.handle.net/10722/144510-
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..en_HK
dc.languageengen_US
dc.publisherElsevier BV. The Journal's web site is located at http://www.elsevier.com/locate/dnarepairen_HK
dc.relation.ispartofDNA Repairen_HK
dc.subjectBRCT domainen_HK
dc.subjectDNA damageen_HK
dc.subjectDNA repairen_HK
dc.subjectRAD18en_HK
dc.titleRAD18-BRCTx interaction is required for efficient repair of UV-induced DNA damageen_HK
dc.typeArticleen_HK
dc.identifier.emailHuen, MSY:huen.michael@hku.hken_HK
dc.identifier.authorityHuen, MSY=rp01336en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1016/j.dnarep.2011.10.012en_HK
dc.identifier.pmid22036607-
dc.identifier.scopuseid_2-s2.0-84855851489en_HK
dc.identifier.hkuros198267en_US
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-84855851489&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume11en_HK
dc.identifier.issue2en_HK
dc.identifier.spage131en_HK
dc.identifier.epage138en_HK
dc.identifier.isiWOS:000301618900005-
dc.publisher.placeNetherlandsen_HK
dc.identifier.scopusauthoridLiu, T=36470537100en_HK
dc.identifier.scopusauthoridChen, H=53877265300en_HK
dc.identifier.scopusauthoridKim, H=53877803200en_HK
dc.identifier.scopusauthoridHuen, MSY=23004751500en_HK
dc.identifier.scopusauthoridChen, J=35261693300en_HK
dc.identifier.scopusauthoridHuang, J=30767499300en_HK
dc.identifier.citeulike10008825-
dc.identifier.issnl1568-7856-

Export via OAI-PMH Interface in XML Formats


OR


Export to Other Non-XML Formats