dc.contributor.author | Baldock, RA | |
dc.contributor.author | Day, M | |
dc.contributor.author | Wilkinson, OJ | |
dc.contributor.author | Cloney, R | |
dc.contributor.author | Jeggo, PA | |
dc.contributor.author | Oliver, AW | |
dc.contributor.author | Watts, FZ | |
dc.contributor.author | Pearl, LH | |
dc.date.accessioned | 2020-07-23T15:02:08Z | |
dc.date.issued | 2015-12-15 | |
dc.identifier.citation | Cell reports, 2015, 13 (10), pp. 2081 - 2089 | |
dc.identifier.issn | 2211-1247 | |
dc.identifier.uri | https://repository.icr.ac.uk/handle/internal/3854 | |
dc.identifier.eissn | 2211-1247 | |
dc.identifier.doi | 10.1016/j.celrep.2015.10.074 | |
dc.description.abstract | 53BP1 plays multiple roles in mammalian DNA damage repair, mediating pathway choice and facilitating DNA double-strand break repair in heterochromatin. Although it possesses a C-terminal BRCT2 domain, commonly involved in phospho-peptide binding in other proteins, initial recruitment of 53BP1 to sites of DNA damage depends on interaction with histone post-translational modifications--H4K20me2 and H2AK13/K15ub--downstream of the early γH2AX phosphorylation mark of DNA damage. We now show that, contrary to current models, the 53BP1-BRCT2 domain binds γH2AX directly, providing a third post-translational mark regulating 53BP1 function. We find that the interaction of 53BP1 with γH2AX is required for sustaining the 53BP1-dependent focal concentration of activated ATM that facilitates repair of DNA double-strand breaks in heterochromatin in G1. | |
dc.format | Print-Electronic | |
dc.format.extent | 2081 - 2089 | |
dc.language | eng | |
dc.language.iso | eng | |
dc.publisher | CELL PRESS | |
dc.rights.uri | https://creativecommons.org/licenses/by/4.0 | |
dc.subject | Heterochromatin | |
dc.subject | Animals | |
dc.subject | Humans | |
dc.subject | Mice | |
dc.subject | Intracellular Signaling Peptides and Proteins | |
dc.subject | DNA-Binding Proteins | |
dc.subject | Chromosomal Proteins, Non-Histone | |
dc.subject | Histones | |
dc.subject | RNA, Small Interfering | |
dc.subject | Fluorescent Antibody Technique | |
dc.subject | Crystallography, X-Ray | |
dc.subject | Transfection | |
dc.subject | DNA Repair | |
dc.subject | Protein Processing, Post-Translational | |
dc.subject | Protein Structure, Quaternary | |
dc.subject | DNA Breaks, Double-Stranded | |
dc.subject | Gene Knockdown Techniques | |
dc.subject | Ataxia Telangiectasia Mutated Proteins | |
dc.subject | Tumor Suppressor p53-Binding Protein 1 | |
dc.title | ATM Localization and Heterochromatin Repair Depend on Direct Interaction of the 53BP1-BRCT2 Domain with γH2AX. | |
dc.type | Journal Article | |
dcterms.dateAccepted | 2015-10-26 | |
rioxxterms.versionofrecord | 10.1016/j.celrep.2015.10.074 | |
rioxxterms.licenseref.uri | https://creativecommons.org/licenses/by-nc-nd/4.0 | |
rioxxterms.licenseref.startdate | 2015-12 | |
rioxxterms.type | Journal Article/Review | |
dc.relation.isPartOf | Cell reports | |
pubs.issue | 10 | |
pubs.notes | Not known | |
pubs.organisational-group | /ICR | |
pubs.organisational-group | /ICR | |
pubs.publication-status | Published | |
pubs.volume | 13 | |
pubs.embargo.terms | Not known | |
dc.contributor.icrauthor | Pearl, Laurence | |