dc.contributor.author | Croft, DR | |
dc.contributor.author | Coleman, ML | |
dc.contributor.author | Li, S | |
dc.contributor.author | Robertson, D | |
dc.contributor.author | Sullivan, T | |
dc.contributor.author | Stewart, CL | |
dc.contributor.author | Olson, MF | |
dc.date.accessioned | 2018-06-11T13:38:48Z | |
dc.date.issued | 2005-01 | |
dc.identifier.citation | The Journal of cell biology, 2005, 168 (2), pp. 245 - 255 | |
dc.identifier.issn | 0021-9525 | |
dc.identifier.uri | https://repository.icr.ac.uk/handle/internal/1825 | |
dc.identifier.eissn | 1540-8140 | |
dc.identifier.doi | 10.1083/jcb.200409049 | |
dc.description.abstract | Membrane 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. | |
dc.format | Print | |
dc.format.extent | 245 - 255 | |
dc.language | eng | |
dc.language.iso | eng | |
dc.rights.uri | https://creativecommons.org/licenses/by-nc-sa/4.0 | |
dc.subject | NIH 3T3 Cells | |
dc.subject | Nuclear Lamina | |
dc.subject | Cell Nucleus | |
dc.subject | Cytoskeleton | |
dc.subject | Microtubules | |
dc.subject | Fibroblasts | |
dc.subject | Animals | |
dc.subject | Mice | |
dc.subject | Amides | |
dc.subject | Cycloheximide | |
dc.subject | Pyridines | |
dc.subject | Nocodazole | |
dc.subject | Cytochalasin D | |
dc.subject | Actins | |
dc.subject | Myosins | |
dc.subject | Myosin-Light-Chain Phosphatase | |
dc.subject | Caspases | |
dc.subject | Protein Kinases | |
dc.subject | Protein-Serine-Threonine Kinases | |
dc.subject | Tumor Necrosis Factor-alpha | |
dc.subject | Intracellular Signaling Peptides and Proteins | |
dc.subject | Myosin Light Chains | |
dc.subject | Cytoskeletal Proteins | |
dc.subject | Nuclear Proteins | |
dc.subject | Lamins | |
dc.subject | Phosphoproteins | |
dc.subject | Enzyme Inhibitors | |
dc.subject | Microscopy, Electron, Transmission | |
dc.subject | Transfection | |
dc.subject | Apoptosis | |
dc.subject | Phosphorylation | |
dc.subject | Mutation | |
dc.subject | rho-Associated Kinases | |
dc.subject | Lim Kinases | |
dc.subject | Caspase Inhibitors | |
dc.title | Actin-myosin-based contraction is responsible for apoptotic nuclear disintegration. | |
dc.type | Journal Article | |
rioxxterms.versionofrecord | 10.1083/jcb.200409049 | |
rioxxterms.licenseref.uri | https://creativecommons.org/licenses/by-nc-sa/4.0 | |
rioxxterms.licenseref.startdate | 2005-01 | |
rioxxterms.type | Journal Article/Review | |
dc.relation.isPartOf | The Journal of cell biology | |
pubs.issue | 2 | |
pubs.notes | Not known | |
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.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-status | Published | |
pubs.volume | 168 | |
pubs.embargo.terms | Not known | |
icr.researchteam | Genetic Susceptibility | en_US |
dc.contributor.icrauthor | Stratton, Michael | |