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Article: Histone ubiquitination associates with BRCAl-dependent DNA damage response

TitleHistone ubiquitination associates with BRCAl-dependent DNA damage response
Authors
KeywordsChemicals And Cas Registry Numbers
Issue Date2009
PublisherAmerican Society for Microbiology
Citation
Molecular And Cellular Biology, 2009, v. 29 n. 3, p. 849-860 How to Cite?
Abstract
Histone ubiquitination participates in multiple cellular processes, including the DNA damage response. However, the molecular mechanisms involved are not clear. Here, we have identified that RAP80/UIMC1 (ubiquitin interaction motif containing 1), a functional partner of BRCA1, recognizes ubiquitinated histones H2A and H2B. The interaction between RAP80 and ubiquitinated histones H2A and H2B is increased following DNA damage. Since RAP80 facilitates BRCAl's translocation to DNA damage sites, our results indicate that ubiquitinated histones H2A and H2B could be upstream partners of the BRCA1/RAP80 complex in the DNA damage response. Moreover, we have found that RNF8 (ring finger protein 8), an E3 ubiquitin ligase, regulates ubiquitination of both histones H2A and H2B. In RNF8-deficient mouse embryo fibroblasts, ubiquitination of both histones H2A and H2B is dramatically reduced, which abolishes the DNA damage-induced BRCA1 and RAP80 accumulation at damage lesions on the chromatin. Taken together, our results suggest that ubiquitinated histones H2A and H2B may recruit the BRCA1 complex to DNA damage lesions on the chromatin. Copyright © 2009, American Society for Microbiology. All Rights Reserved.
Persistent Identifierhttp://hdl.handle.net/10722/90769
ISSN
2013 Impact Factor: 5.036
PubMed Central ID
ISI Accession Number ID
Funding AgencyGrant Number
Department of DefenseBC050367
P50 CA116201
National Institutes of HealthCA132755
University of Michigan Cancer Center
University of Michigan
AACR
National Cancer InstituteCA89239
CA92312
CA100109
Anna Fuller Fund Fellowship
Funding Information:

This work was supported by the Department of Defense (grant BC050367 to X. Y.), the National Institutes of Health (grant CA132755 to X.Y.), the University of Michigan Cancer Center, and the GI Peptide Research Center of the University of Michigan. X. Y. is a recipient of an AACR-Susan G. Komen for the Cure Career Development Award for Breast Cancer Research. J.C. is a recipient of an Era of Hope Scholar award from the Department of Defense and is a member of the Mayo Clinic Breast SPORE program (grant P50 CA116201). J. C. was also supported by the National Cancer Institute (grants CA89239, CA92312, and CA100109). M. S. Y. H. is supported by an Anna Fuller Fund Fellowship.

References

 

DC FieldValueLanguage
dc.contributor.authorWu, Jen_HK
dc.contributor.authorHuen, MSYen_HK
dc.contributor.authorLu, LYen_HK
dc.contributor.authorYe, Len_HK
dc.contributor.authorDou, Yen_HK
dc.contributor.authorLjungman, Men_HK
dc.contributor.authorChen, Jen_HK
dc.contributor.authorYu, Xen_HK
dc.date.accessioned2010-09-17T10:08:05Z-
dc.date.available2010-09-17T10:08:05Z-
dc.date.issued2009en_HK
dc.identifier.citationMolecular And Cellular Biology, 2009, v. 29 n. 3, p. 849-860en_HK
dc.identifier.issn0270-7306en_HK
dc.identifier.urihttp://hdl.handle.net/10722/90769-
dc.description.abstractHistone ubiquitination participates in multiple cellular processes, including the DNA damage response. However, the molecular mechanisms involved are not clear. Here, we have identified that RAP80/UIMC1 (ubiquitin interaction motif containing 1), a functional partner of BRCA1, recognizes ubiquitinated histones H2A and H2B. The interaction between RAP80 and ubiquitinated histones H2A and H2B is increased following DNA damage. Since RAP80 facilitates BRCAl's translocation to DNA damage sites, our results indicate that ubiquitinated histones H2A and H2B could be upstream partners of the BRCA1/RAP80 complex in the DNA damage response. Moreover, we have found that RNF8 (ring finger protein 8), an E3 ubiquitin ligase, regulates ubiquitination of both histones H2A and H2B. In RNF8-deficient mouse embryo fibroblasts, ubiquitination of both histones H2A and H2B is dramatically reduced, which abolishes the DNA damage-induced BRCA1 and RAP80 accumulation at damage lesions on the chromatin. Taken together, our results suggest that ubiquitinated histones H2A and H2B may recruit the BRCA1 complex to DNA damage lesions on the chromatin. Copyright © 2009, American Society for Microbiology. All Rights Reserved.en_HK
dc.languageengen_HK
dc.publisherAmerican Society for Microbiologyen_HK
dc.relation.ispartofMolecular and Cellular Biologyen_HK
dc.subjectChemicals And Cas Registry Numbersen_HK
dc.titleHistone ubiquitination associates with BRCAl-dependent DNA damage responseen_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.doi10.1128/MCB.01302-08en_HK
dc.identifier.pmid19015238-
dc.identifier.pmcidPMC2630672-
dc.identifier.scopuseid_2-s2.0-59249095962en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-59249095962&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume29en_HK
dc.identifier.issue3en_HK
dc.identifier.spage849en_HK
dc.identifier.epage860en_HK
dc.identifier.isiWOS:000262609100020-
dc.publisher.placeUnited Statesen_HK
dc.identifier.scopusauthoridWu, J=35313196500en_HK
dc.identifier.scopusauthoridHuen, MSY=23004751500en_HK
dc.identifier.scopusauthoridLu, LY=8686996700en_HK
dc.identifier.scopusauthoridYe, L=35504324300en_HK
dc.identifier.scopusauthoridDou, Y=7005659152en_HK
dc.identifier.scopusauthoridLjungman, M=7003372190en_HK
dc.identifier.scopusauthoridChen, J=35261693300en_HK
dc.identifier.scopusauthoridYu, X=35249962700en_HK

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