{"@context":{"@vocab":"https://cir.nii.ac.jp/schema/1.0/","rdfs":"http://www.w3.org/2000/01/rdf-schema#","dc":"http://purl.org/dc/elements/1.1/","dcterms":"http://purl.org/dc/terms/","foaf":"http://xmlns.com/foaf/0.1/","prism":"http://prismstandard.org/namespaces/basic/2.0/","cinii":"http://ci.nii.ac.jp/ns/1.0/","datacite":"https://schema.datacite.org/meta/kernel-4/","ndl":"http://ndl.go.jp/dcndl/terms/","jpcoar":"https://github.com/JPCOAR/schema/blob/master/2.0/"},"@id":"https://cir.nii.ac.jp/crid/1361699993538872576.json","@type":"Article","productIdentifier":[{"identifier":{"@type":"DOI","@value":"10.1139/o10-113"}},{"identifier":{"@type":"URI","@value":"https://cdnsciencepub.com/doi/full-xml/10.1139/O10-113"}},{"identifier":{"@type":"URI","@value":"https://cdnsciencepub.com/doi/pdf/10.1139/O10-113"}}],"dc:title":[{"@value":"Heterochromatin and the DNA damage response: the need to relaxThis paper is one of a selection of papers in a Special Issue entitled 31st Annual International Asilomar Chromatin and Chromosomes Conference, and has undergone the Journal’s usual peer review process."}],"description":[{"type":"abstract","notation":[{"@value":"<jats:p> Higher order chromatin structure has an impact on all nuclear functions, including the DNA damage response. Over the past several years, it has become increasingly clear that heterochromatin and euchromatin represent separate entities with respect to both damage sensitivity and repair. The chromatin compaction present in heterochromatin helps to protect this DNA from damage; however, when lesions do occur, the compaction restricts the ability of DNA damage response proteins to access the site, as evidenced by its ability to block the expansion of H2AX phosphorylation. As such, DNA damage in heterochromatin is refractory to repair, which requires the surrounding chromatin structure to be decondensed. In the case of DNA double-strand breaks, this relaxation is at least partially mediated by the ATM kinase phosphorylating and inhibiting the function of the transcriptional repressor KAP1. This review will focus on the functions of KAP1 and other proteins involved in the maintenance or restriction of heterochromatin, including HP1 and TIP60, in the DNA damage response. As heterochromatin is important for maintaining genomic stability, cells must maintain a delicate balance between allowing repair factors access to these regions and ensuring that these regions retain their organization to prevent increased DNA damage and chromosomal mutations. </jats:p>"}]}],"creator":[{"@id":"https://cir.nii.ac.jp/crid/1381699993538872576","@type":"Researcher","foaf:name":[{"@value":"Kendra L. Cann"}],"jpcoar:affiliationName":[{"@value":"Departments of Pathology and Biochemistry & Molecular Biology, Dalhousie University, Halifax, NS, Canada."},{"@value":"Beatrice Hunter Cancer Research Institute, Halifax, NS, Canada."}]},{"@id":"https://cir.nii.ac.jp/crid/1381699993538872577","@type":"Researcher","foaf:name":[{"@value":"Graham Dellaire"}],"jpcoar:affiliationName":[{"@value":"Departments of Pathology and Biochemistry & Molecular Biology, Dalhousie University, Halifax, NS, Canada."},{"@value":"Beatrice Hunter Cancer Research Institute, Halifax, NS, Canada."}]}],"publication":{"publicationIdentifier":[{"@type":"PISSN","@value":"08298211"},{"@type":"EISSN","@value":"12086002"}],"prism:publicationName":[{"@value":"Biochemistry and Cell Biology"}],"dc:publisher":[{"@value":"Canadian Science Publishing"}],"prism:publicationDate":"2011-02","prism:volume":"89","prism:number":"1","prism:startingPage":"45","prism:endingPage":"60"},"reviewed":"false","dc:rights":["http://www.nrcresearchpress.com/page/about/CorporateTextAndDataMining"],"url":[{"@id":"https://cdnsciencepub.com/doi/full-xml/10.1139/O10-113"},{"@id":"https://cdnsciencepub.com/doi/pdf/10.1139/O10-113"}],"createdAt":"2011-02-15","modifiedAt":"2025-07-02","relatedProduct":[{"@id":"https://cir.nii.ac.jp/crid/1360004232044958336","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"Decreased KAT5 Expression Impairs DNA Repair and Induces Altered DNA Methylation in Kidney Podocytes"}]},{"@id":"https://cir.nii.ac.jp/crid/1360282589083168640","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"Homeodomain-interacting protein kinase 2 regulates DNA damage response through interacting with heterochromatin protein 1γ"}]},{"@id":"https://cir.nii.ac.jp/crid/1360283692109034752","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"Methylation of SUV39H1 by SET7/9 results in heterochromatin relaxation and genome instability"}]},{"@id":"https://cir.nii.ac.jp/crid/1360565167491298176","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"Transient bursts of Zscan4 expression are accompanied by the rapid derepression of heterochromatin in mouse embryonic stem cells"}]},{"@id":"https://cir.nii.ac.jp/crid/1360576118761896064","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"DNA repair factor KAT5 prevents ischemic acute kidney injury through glomerular filtration regulation"}]},{"@id":"https://cir.nii.ac.jp/crid/1360848657310678144","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"New mechanism of γ-H2AX generation: Surfactant-induced actin disruption causes deoxyribonuclease I translocation to the nucleus and forms DNA double-strand breaks"}]},{"@id":"https://cir.nii.ac.jp/crid/2051151842060125824","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"Altered DNA methylation in kidney disease : useful markers and therapeutic targets"}]}],"dataSourceIdentifier":[{"@type":"CROSSREF","@value":"10.1139/o10-113"},{"@type":"CROSSREF","@value":"10.1038/onc.2014.278_references_DOI_K5hSFbrUYgTCTRvkMhCSWciDWPr"},{"@type":"CROSSREF","@value":"10.1073/pnas.1216596110_references_DOI_K5hSFbrUYgTCTRvkMhCSWciDWPr"},{"@type":"CROSSREF","@value":"10.1016/j.celrep.2019.01.005_references_DOI_K5hSFbrUYgTCTRvkMhCSWciDWPr"},{"@type":"CROSSREF","@value":"10.1007/s10157-022-02181-5_references_DOI_K5hSFbrUYgTCTRvkMhCSWciDWPr"},{"@type":"CROSSREF","@value":"10.1093/dnares/dsv013_references_DOI_K5hSFbrUYgTCTRvkMhCSWciDWPr"},{"@type":"CROSSREF","@value":"10.1016/j.isci.2021.103436_references_DOI_K5hSFbrUYgTCTRvkMhCSWciDWPr"},{"@type":"CROSSREF","@value":"10.1016/j.mrgentox.2015.09.006_references_DOI_K5hSFbrUYgTCTRvkMhCSWciDWPr"}]}