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Article: The 53BP1-EXPAND1 connection in chromatin structure regulation.
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TitleThe 53BP1-EXPAND1 connection in chromatin structure regulation.
 
AuthorsSy, SM
Chen, J2
Huen, MS1 1 1
 
Keywords53Bp1
Chromatin
Expand1
Mum1
 
Issue Date2010
 
PublisherLandes Bioscience. The Journal's web site is located at http://www.landesbioscience.com/journals/nucleus/
 
CitationNucleus (Austin, Tex.), 2010, v. 1 n. 6, p. 472-474 [How to Cite?]
DOI: http://dx.doi.org/10.4161/nucl.1.6.13059
 
AbstractThe mammalian interphase chromatin responds to DNA damages by altering the compactness of its architecture, thereby permitting local access of DNA repair machineries. Adding to the cellular strategies of chromatin remodeling following DNA damage, our recent work identified the 53BP1-EXPAND1 module in promoting chromatin dynamics in response to DNA double-strand breaks. Endowed with a nucleosome-binding PWWP domain, EXPAND1 tethers to the chromatin where it is involved in maintaining basal chromatin accessibility in unperturbed cells. Interestingly, through its direct interaction with the DNA damage mediator protein 53BP1, EXPAND1 accumulates at the damage-modified chromatin and triggers its further decondensation. These observations, together with the fact that EXPAND 1 promotes cell survival following DNA damage, suggest that the chromatin-bound factor may facilitate DNA repair by regulating the organization of chromatin structure.
 
ISSN1949-1042
 
DOIhttp://dx.doi.org/10.4161/nucl.1.6.13059
 
PubMed Central IDPMC3027048
 
ReferencesReferences in Scopus
 
DC FieldValue
dc.contributor.authorSy, SM
 
dc.contributor.authorChen, J
 
dc.contributor.authorHuen, MS
 
dc.date.accessioned2011-07-27T01:25:49Z
 
dc.date.available2011-07-27T01:25:49Z
 
dc.date.issued2010
 
dc.description.abstractThe mammalian interphase chromatin responds to DNA damages by altering the compactness of its architecture, thereby permitting local access of DNA repair machineries. Adding to the cellular strategies of chromatin remodeling following DNA damage, our recent work identified the 53BP1-EXPAND1 module in promoting chromatin dynamics in response to DNA double-strand breaks. Endowed with a nucleosome-binding PWWP domain, EXPAND1 tethers to the chromatin where it is involved in maintaining basal chromatin accessibility in unperturbed cells. Interestingly, through its direct interaction with the DNA damage mediator protein 53BP1, EXPAND1 accumulates at the damage-modified chromatin and triggers its further decondensation. These observations, together with the fact that EXPAND 1 promotes cell survival following DNA damage, suggest that the chromatin-bound factor may facilitate DNA repair by regulating the organization of chromatin structure.
 
dc.description.naturelink_to_OA_fulltext
 
dc.identifier.citationNucleus (Austin, Tex.), 2010, v. 1 n. 6, p. 472-474 [How to Cite?]
DOI: http://dx.doi.org/10.4161/nucl.1.6.13059
 
dc.identifier.doihttp://dx.doi.org/10.4161/nucl.1.6.13059
 
dc.identifier.epage474
 
dc.identifier.hkuros186733
 
dc.identifier.issn1949-1042
 
dc.identifier.issue6
 
dc.identifier.pmcidPMC3027048
 
dc.identifier.pmid21327088
 
dc.identifier.scopuseid_2-s2.0-78549254849
 
dc.identifier.spage472
 
dc.identifier.urihttp://hdl.handle.net/10722/135013
 
dc.identifier.volume1
 
dc.languageeng
 
dc.publisherLandes Bioscience. The Journal's web site is located at http://www.landesbioscience.com/journals/nucleus/
 
dc.publisher.placeUnited States
 
dc.relation.ispartofNucleus (Austin, Tex.)
 
dc.relation.referencesReferences in Scopus
 
dc.subject.meshChromatin - metabolism
 
dc.subject.meshChromatin Assembly and Disassembly - genetics
 
dc.subject.meshChromosomal Proteins, Non-Histone - metabolism
 
dc.subject.meshDNA Breaks, Double-Stranded
 
dc.subject.meshIntracellular Signaling Peptides and Proteins - metabolism
 
dc.subject53Bp1
 
dc.subjectChromatin
 
dc.subjectExpand1
 
dc.subjectMum1
 
dc.titleThe 53BP1-EXPAND1 connection in chromatin structure regulation.
 
dc.typeArticle
 
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<contributor.author>Chen, J</contributor.author>
<contributor.author>Huen, MS</contributor.author>
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<description.abstract>The mammalian interphase chromatin responds to DNA damages by altering the compactness of its architecture, thereby permitting local access of DNA repair machineries. Adding to the cellular strategies of chromatin remodeling following DNA damage, our recent work identified the 53BP1-EXPAND1 module in promoting chromatin dynamics in response to DNA double-strand breaks. Endowed with a nucleosome-binding PWWP domain, EXPAND1 tethers to the chromatin where it is involved in maintaining basal chromatin accessibility in unperturbed cells. Interestingly, through its direct interaction with the DNA damage mediator protein 53BP1, EXPAND1 accumulates at the damage-modified chromatin and triggers its further decondensation. These observations, together with the fact that EXPAND 1 promotes cell survival following DNA damage, suggest that the chromatin-bound factor may facilitate DNA repair by regulating the organization of chromatin structure.</description.abstract>
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<subject>Chromatin</subject>
<subject>Expand1</subject>
<subject>Mum1</subject>
<subject.mesh>Chromatin - metabolism</subject.mesh>
<subject.mesh>Chromatin Assembly and Disassembly - genetics</subject.mesh>
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<subject.mesh>DNA Breaks, Double-Stranded</subject.mesh>
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Author Affiliations
  1. The University of Hong Kong
  2. University of Texas M. D. Anderson Cancer Center