Show simple item record

dc.contributor.authorBaldock, RA
dc.contributor.authorDay, M
dc.contributor.authorWilkinson, OJ
dc.contributor.authorCloney, R
dc.contributor.authorJeggo, PA
dc.contributor.authorOliver, AW
dc.contributor.authorWatts, FZ
dc.contributor.authorPearl, LH
dc.date.accessioned2020-07-23T15:02:08Z
dc.date.issued2015-12
dc.identifier.citationCell reports, 2015, 13 (10), pp. 2081 - 2089
dc.identifier.issn2211-1247
dc.identifier.urihttps://repository.icr.ac.uk/handle/internal/3854
dc.identifier.eissn2211-1247
dc.identifier.doi10.1016/j.celrep.2015.10.074
dc.description.abstract53BP1 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.formatPrint-Electronic
dc.format.extent2081 - 2089
dc.languageeng
dc.language.isoeng
dc.rights.urihttps://creativecommons.org/licenses/by/4.0
dc.subjectHeterochromatin
dc.subjectAnimals
dc.subjectHumans
dc.subjectMice
dc.subjectIntracellular Signaling Peptides and Proteins
dc.subjectDNA-Binding Proteins
dc.subjectChromosomal Proteins, Non-Histone
dc.subjectHistones
dc.subjectRNA, Small Interfering
dc.subjectFluorescent Antibody Technique
dc.subjectCrystallography, X-Ray
dc.subjectTransfection
dc.subjectDNA Repair
dc.subjectProtein Processing, Post-Translational
dc.subjectProtein Structure, Quaternary
dc.subjectDNA Breaks, Double-Stranded
dc.subjectGene Knockdown Techniques
dc.subjectAtaxia Telangiectasia Mutated Proteins
dc.subjectTumor Suppressor p53-Binding Protein 1
dc.titleATM Localization and Heterochromatin Repair Depend on Direct Interaction of the 53BP1-BRCT2 Domain with γH2AX.
dc.typeJournal Article
dcterms.dateAccepted2015-10-26
rioxxterms.versionofrecord10.1016/j.celrep.2015.10.074
rioxxterms.licenseref.urihttps://creativecommons.org/licenses/by-nc-nd/4.0
rioxxterms.licenseref.startdate2015-12
rioxxterms.typeJournal Article/Review
dc.relation.isPartOfCell reports
pubs.issue10
pubs.notesNot known
pubs.organisational-group/ICR
pubs.organisational-group/ICR
pubs.publication-statusPublished
pubs.volume13
pubs.embargo.termsNot known
dc.contributor.icrauthorPearl, Laurenceen


Files in this item

Thumbnail

This item appears in the following collection(s)

Show simple item record

https://creativecommons.org/licenses/by/4.0
Except where otherwise noted, this item's license is described as https://creativecommons.org/licenses/by/4.0