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Article: Histone ubiquitination associates with BRCAl-dependent DNA damage response
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TitleHistone ubiquitination associates with BRCAl-dependent DNA damage response
 
AuthorsWu, J3
Huen, MSY2
Lu, LY3
Ye, L3
Dou, Y1
Ljungman, M3
Chen, J2
Yu, X3
 
KeywordsChemicals And Cas Registry Numbers
 
Issue Date2009
 
PublisherAmerican Society for Microbiology
 
CitationMolecular And Cellular Biology, 2009, v. 29 n. 3, p. 849-860 [How to Cite?]
DOI: http://dx.doi.org/10.1128/MCB.01302-08
 
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.
 
ISSN0270-7306
2012 Impact Factor: 5.372
2012 SCImago Journal Rankings: 3.821
 
DOIhttp://dx.doi.org/10.1128/MCB.01302-08
 
PubMed Central IDPMC2630672
 
ISI Accession Number IDWOS:000262609100020
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.

 
ReferencesReferences in Scopus
 
DC FieldValue
dc.contributor.authorWu, J
 
dc.contributor.authorHuen, MSY
 
dc.contributor.authorLu, LY
 
dc.contributor.authorYe, L
 
dc.contributor.authorDou, Y
 
dc.contributor.authorLjungman, M
 
dc.contributor.authorChen, J
 
dc.contributor.authorYu, X
 
dc.date.accessioned2010-09-17T10:08:05Z
 
dc.date.available2010-09-17T10:08:05Z
 
dc.date.issued2009
 
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.
 
dc.description.natureLink_to_subscribed_fulltext
 
dc.identifier.citationMolecular And Cellular Biology, 2009, v. 29 n. 3, p. 849-860 [How to Cite?]
DOI: http://dx.doi.org/10.1128/MCB.01302-08
 
dc.identifier.doihttp://dx.doi.org/10.1128/MCB.01302-08
 
dc.identifier.epage860
 
dc.identifier.isiWOS:000262609100020
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.

 
dc.identifier.issn0270-7306
2012 Impact Factor: 5.372
2012 SCImago Journal Rankings: 3.821
 
dc.identifier.issue3
 
dc.identifier.pmcidPMC2630672
 
dc.identifier.pmid19015238
 
dc.identifier.scopuseid_2-s2.0-59249095962
 
dc.identifier.spage849
 
dc.identifier.urihttp://hdl.handle.net/10722/90769
 
dc.identifier.volume29
 
dc.languageeng
 
dc.publisherAmerican Society for Microbiology
 
dc.publisher.placeUnited States
 
dc.relation.ispartofMolecular and Cellular Biology
 
dc.relation.referencesReferences in Scopus
 
dc.subjectChemicals And Cas Registry Numbers
 
dc.titleHistone ubiquitination associates with BRCAl-dependent DNA damage response
 
dc.typeArticle
 
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<contributor.author>Ye, L</contributor.author>
<contributor.author>Dou, Y</contributor.author>
<contributor.author>Ljungman, M</contributor.author>
<contributor.author>Chen, J</contributor.author>
<contributor.author>Yu, X</contributor.author>
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Author Affiliations
  1. University Michigan Ann Arbor
  2. Yale University
  3. University of Michigan Medical School