Actin-myosin-based contraction is responsible for apoptotic nuclear disintegration.
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ICR Authors
Authors
Croft, DR
Coleman, ML
Li, S
Robertson, D
Sullivan, T
Stewart, CL
Olson, MF
Coleman, ML
Li, S
Robertson, D
Sullivan, T
Stewart, CL
Olson, MF
Document Type
Journal Article
Date
2005-01
Date Accepted
Date Available
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.
Citation
The Journal of cell biology, 2005, 168 (2), pp. 245 - 255
Source Title
Publisher
ISSN
0021-9525
eISSN
1540-8140
Research Team
Genetic Susceptibility