Article: Histone ubiquitination associates with BRCAl-dependent DNA damage response
| Title | Histone ubiquitination associates with BRCAl-dependent DNA damage response | ||||||||||||||||
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| Authors | Wu, J3 Huen, MSY2 Lu, LY3 Ye, L3 Dou, Y1 Ljungman, M3 Chen, J2 Yu, X3 | ||||||||||||||||
| Keywords | Chemicals And Cas Registry Numbers | ||||||||||||||||
| Issue Date | 2009 | ||||||||||||||||
| Publisher | American Society for Microbiology | ||||||||||||||||
| Citation | Molecular And Cellular Biology, 2009, v. 29 n. 3, p. 849-860 [How to Cite?] DOI: http://dx.doi.org/10.1128/MCB.01302-08 | ||||||||||||||||
| 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. | ||||||||||||||||
| ISSN | 0270-7306 2011 Impact Factor: 5.527 2011 SCImago Journal Rankings: 1.368 | ||||||||||||||||
| DOI | http://dx.doi.org/10.1128/MCB.01302-08 | ||||||||||||||||
| ISI Accession Number ID | WOS:000262609100020
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. | ||||||||||||||||
| PubMed Central ID | PMC2630672 | ||||||||||||||||
| References | References in Scopus |
| dc.contributor.author | Wu, J | ||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| dc.contributor.author | Huen, MSY | ||||||||||||||||
| dc.contributor.author | Lu, LY | ||||||||||||||||
| dc.contributor.author | Ye, L | ||||||||||||||||
| dc.contributor.author | Dou, Y | ||||||||||||||||
| dc.contributor.author | Ljungman, M | ||||||||||||||||
| dc.contributor.author | Chen, J | ||||||||||||||||
| dc.contributor.author | Yu, X | ||||||||||||||||
| dc.date.accessioned | 2010-09-17T10:08:05Z | ||||||||||||||||
| dc.date.available | 2010-09-17T10:08:05Z | ||||||||||||||||
| dc.date.issued | 2009 | ||||||||||||||||
| dc.description.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. | ||||||||||||||||
| dc.description.nature | Link_to_subscribed_fulltext | ||||||||||||||||
| dc.identifier.citation | Molecular 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.doi | http://dx.doi.org/10.1128/MCB.01302-08 | ||||||||||||||||
| dc.identifier.epage | 860 | ||||||||||||||||
| dc.identifier.isi | WOS:000262609100020
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.issn | 0270-7306 2011 Impact Factor: 5.527 2011 SCImago Journal Rankings: 1.368 | ||||||||||||||||
| dc.identifier.issue | 3 | ||||||||||||||||
| dc.identifier.pmcid | PMC2630672 | ||||||||||||||||
| dc.identifier.pmid | 19015238 | ||||||||||||||||
| dc.identifier.scopus | eid_2-s2.0-59249095962 | ||||||||||||||||
| dc.identifier.spage | 849 | ||||||||||||||||
| dc.identifier.uri | http://hdl.handle.net/10722/90769 | ||||||||||||||||
| dc.identifier.volume | 29 | ||||||||||||||||
| dc.language | eng | ||||||||||||||||
| dc.publisher | American Society for Microbiology | ||||||||||||||||
| dc.publisher.place | United States | ||||||||||||||||
| dc.relation.ispartof | Molecular and Cellular Biology | ||||||||||||||||
| dc.relation.references | References in Scopus | ||||||||||||||||
| dc.subject | Chemicals And Cas Registry Numbers | ||||||||||||||||
| dc.title | Histone ubiquitination associates with BRCAl-dependent DNA damage response | ||||||||||||||||
| dc.type | Article |
- University Michigan Ann Arbor
- Yale University
- University of Michigan Medical School