Actin-myosin-based contraction is responsible for apoptotic nuclear disintegration.

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Publication Date
2005-01ICR Author
Author
Croft, DR
Coleman, ML
Li, S
Robertson, D
Sullivan, T
Stewart, CL
Olson, MF
Type
Journal Article
Metadata
Show full item recordAbstract
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.
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Licenseref URL
https://creativecommons.org/licenses/by-nc-sa/4.0Version of record
Subject
NIH 3T3 Cells
Nuclear Lamina
Cell Nucleus
Cytoskeleton
Microtubules
Fibroblasts
Animals
Mice
Amides
Cycloheximide
Pyridines
Nocodazole
Cytochalasin D
Actins
Myosins
Myosin-Light-Chain Phosphatase
Caspases
Protein Kinases
Protein-Serine-Threonine Kinases
Tumor Necrosis Factor-alpha
Intracellular Signaling Peptides and Proteins
Myosin Light Chains
Cytoskeletal Proteins
Nuclear Proteins
Lamins
Phosphoproteins
Enzyme Inhibitors
Microscopy, Electron, Transmission
Transfection
Apoptosis
Phosphorylation
Mutation
rho-Associated Kinases
Lim Kinases
Caspase Inhibitors
Research team
Genetic Susceptibility
Language
eng
License start date
2005-01
Citation
The Journal of cell biology, 2005, 168 (2), pp. 245 - 255
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