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dc.contributor.authorCroft, DRen_US
dc.contributor.authorColeman, MLen_US
dc.contributor.authorLi, Sen_US
dc.contributor.authorRobertson, Den_US
dc.contributor.authorSullivan, Ten_US
dc.contributor.authorStewart, CLen_US
dc.contributor.authorOlson, MFen_US
dc.date.accessioned2018-06-11T13:38:48Z
dc.date.issued2005-01en_US
dc.identifier.citationThe Journal of cell biology, 2005, 168 (2), pp. 245 - 255en_US
dc.identifier.issn0021-9525en_US
dc.identifier.urihttps://repository.icr.ac.uk/handle/internal/1825
dc.identifier.eissn1540-8140en_US
dc.identifier.doi10.1083/jcb.200409049en_US
dc.description.abstractMembrane blebbing during the apoptotic execution phase results from caspase-mediated cleavage and activation of ROCK I. Here, we show that ROCK activity, myosin light chain (MLC) phosphorylation, MLC ATPase activity, and an intact actin cytoskeleton, but not microtubular cytoskeleton, are required for disruption of nuclear integrity during apoptosis. Inhibition of ROCK or MLC ATPase activity, which protect apoptotic nuclear integrity, does not affect caspase-mediated degradation of nuclear proteins such as lamins A, B1, or C. The conditional activation of ROCK I was sufficient to tear apart nuclei in lamin A/C null fibroblasts, but not in wild-type fibroblasts. Thus, apoptotic nuclear disintegration requires actin-myosin contractile force and lamin proteolysis, making apoptosis analogous to, but distinct from, mitosis where nuclear disintegration results from microtubule-based forces and from lamin phosphorylation and depolymerization.en_US
dc.formatPrinten_US
dc.format.extent245 - 255en_US
dc.languageengen_US
dc.language.isoengen_US
dc.subjectNIH 3T3 Cellsen_US
dc.subjectNuclear Laminaen_US
dc.subjectCell Nucleusen_US
dc.subjectCytoskeletonen_US
dc.subjectMicrotubulesen_US
dc.subjectFibroblastsen_US
dc.subjectAnimalsen_US
dc.subjectMiceen_US
dc.subjectAmidesen_US
dc.subjectCycloheximideen_US
dc.subjectPyridinesen_US
dc.subjectNocodazoleen_US
dc.subjectCytochalasin Den_US
dc.subjectActinsen_US
dc.subjectMyosinsen_US
dc.subjectMyosin-Light-Chain Phosphataseen_US
dc.subjectCaspasesen_US
dc.subjectProtein Kinasesen_US
dc.subjectProtein-Serine-Threonine Kinasesen_US
dc.subjectTumor Necrosis Factor-alphaen_US
dc.subjectIntracellular Signaling Peptides and Proteinsen_US
dc.subjectMyosin Light Chainsen_US
dc.subjectCytoskeletal Proteinsen_US
dc.subjectNuclear Proteinsen_US
dc.subjectLaminsen_US
dc.subjectPhosphoproteinsen_US
dc.subjectEnzyme Inhibitorsen_US
dc.subjectMicroscopy, Electron, Transmissionen_US
dc.subjectTransfectionen_US
dc.subjectApoptosisen_US
dc.subjectPhosphorylationen_US
dc.subjectMutationen_US
dc.subjectrho-Associated Kinasesen_US
dc.subjectLim Kinasesen_US
dc.subjectCaspase Inhibitorsen_US
dc.titleActin-myosin-based contraction is responsible for apoptotic nuclear disintegration.en_US
dc.typeJournal Article
rioxxterms.versionofrecord10.1083/jcb.200409049en_US
rioxxterms.licenseref.urihttps://creativecommons.org/licenses/by-nc-sa/4.0en_US
rioxxterms.licenseref.startdate2005-01en_US
rioxxterms.typeJournal Article/Reviewen_US
dc.relation.isPartOfThe Journal of cell biologyen_US
pubs.issue2en_US
pubs.notesNot knownen_US
pubs.organisational-group/ICR
pubs.organisational-group/ICR/Primary Group
pubs.organisational-group/ICR/Primary Group/ICR Divisions
pubs.organisational-group/ICR/Primary Group/ICR Divisions/Breast Cancer Research
pubs.organisational-group/ICR/Primary Group/ICR Divisions/Breast Cancer Research/Genetic Susceptibility
pubs.organisational-group/ICR/Primary Group/ICR Divisions/Genetics and Epidemiology
pubs.organisational-group/ICR/Primary Group/ICR Divisions/Genetics and Epidemiology/Genetic Susceptibility
pubs.publication-statusPublisheden_US
pubs.volume168en_US
pubs.embargo.termsNot knownen_US
icr.researchteamGenetic Susceptibilityen_US
dc.contributor.icrauthorStratton, Michaelen_US


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