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Reorganization of the nuclear architecture in the Drosophila melanogaster Lamin B mutant lacking the CaaX box

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dc.contributor.authorBondarenko, Semen M.en
dc.contributor.authorSharakhov, Igor V.en
dc.contributor.departmentEntomologyen
dc.date.accessioned2021-09-01T12:36:28Zen
dc.date.available2021-09-01T12:36:28Zen
dc.date.issued2020-01-01en
dc.date.updated2021-09-01T12:36:22Zen
dc.description.abstractLamins interact with the nuclear membrane and chromatin but the precise players and mechanisms of these interactions are unknown. Here, we tested whether the removal of the CaaX motif from Lamin B disrupts its attachment to the nuclear membrane and affects chromatin distribution. We used Drosophila melanogaster LamA25  homozygous mutants that lack the CaaX box. We found that the mutant Lamin B was not confined to the nuclear periphery but was distributed throughout the nuclear interior, colocalizing with chromosomes in salivary gland and proventriculus. The peripheral position of Lamin C, nuclear pore complex (NPC), heterochromatin protein 1a (HP1a), H3K9me2- and H3K27me3-associated chromatin remained intact. The fluorescence intensity of the DAPI-stained peripheral chromatin significantly decreased and that of the central chromatin significantly increased in the proventriculus nuclei of the mutantflies compared to wild-type. However, the mutation had little effect on chromatin radial distribution inside highly polytenized salivary gland nuclei.en
dc.description.versionPublished versionen
dc.format.extentPages 283-298en
dc.format.extent16 page(s)en
dc.format.mimetypeapplication/pdfen
dc.identifier.doihttps://doi.org/10.1080/19491034.2020.1819704en
dc.identifier.eissn1949-1042en
dc.identifier.issn1949-1034en
dc.identifier.issue1en
dc.identifier.orcidSharakhov, Igor [0000-0003-0752-3747]en
dc.identifier.pmid32960740en
dc.identifier.urihttp://hdl.handle.net/10919/104889en
dc.identifier.volume11en
dc.language.isoenen
dc.publisherTaylor & Francisen
dc.relation.urihttp://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcApp=PARTNER_APP&SrcAuth=LinksAMR&KeyUT=WOS:000571869300001&DestLinkType=FullRecord&DestApp=ALL_WOS&UsrCustomerID=930d57c9ac61a043676db62af60056c1en
dc.rightsCreative Commons Attribution 4.0 Internationalen
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/en
dc.subjectLife Sciences & Biomedicineen
dc.subjectCell Biologyen
dc.subjectNuclear laminaen
dc.subjectLamin Ben
dc.subjectDm(0)en
dc.subjectB-type laminen
dc.subjectLam(a25)mutanten
dc.subjectDrosophilaen
dc.subjectchromatinen
dc.subjectnuclear envelopeen
dc.subjectproventriculus nucleien
dc.subjectsalivary gland nucleien
dc.subjectconfocal microscopyen
dc.subjectMATRIX ATTACHMENT REGIONSen
dc.subjectLAMIN DM(0)en
dc.subjectDROSOPHILAen
dc.subjectORGANIZATIONen
dc.subjectCHROMATINen
dc.subjectHETEROCHROMATINen
dc.subjectNEURODEGENERATIONen
dc.subjectCHROMOSOMESen
dc.subjectPLATFORMen
dc.subjectBINDINGen
dc.subject.meshChromatinen
dc.subject.meshNuclear Poreen
dc.subject.meshAnimalsen
dc.subject.meshDrosophila melanogasteren
dc.subject.meshDrosophila Proteinsen
dc.subject.meshChromosomal Proteins, Non-Histoneen
dc.subject.meshHistonesen
dc.subject.meshLaminsen
dc.subject.meshLamin Type Ben
dc.subject.meshHomozygoteen
dc.subject.meshMutationen
dc.titleReorganization of the nuclear architecture in the Drosophila melanogaster Lamin B mutant lacking the CaaX boxen
dc.title.serialNucleusen
dc.typeArticle - Refereeden
dc.type.dcmitypeTexten
dc.type.otherArticleen
dc.type.otherJournalen
pubs.organisational-group/Virginia Techen
pubs.organisational-group/Virginia Tech/Agriculture & Life Sciencesen
pubs.organisational-group/Virginia Tech/Agriculture & Life Sciences/Entomologyen
pubs.organisational-group/Virginia Tech/University Research Institutesen
pubs.organisational-group/Virginia Tech/University Research Institutes/Fralin Life Sciencesen
pubs.organisational-group/Virginia Tech/Faculty of Health Sciencesen
pubs.organisational-group/Virginia Tech/All T&R Facultyen
pubs.organisational-group/Virginia Tech/Agriculture & Life Sciences/CALS T&R Facultyen
pubs.organisational-group/Virginia Tech/University Research Institutes/Fralin Life Sciences/Durelle Scotten

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