Abstract
The execution phase of apoptosis is characterized by marked changes in cell morphology that include contraction and membrane blebbing. The actin-myosin system has been proposed to be the source of contractile force that drives bleb formation, although the biochemical pathway that promotes actin-myosin contractility during apoptosis has not been identified. Here we show that the Rho effector protein ROCK I, which contributes to phosphorylation of myosin light-chains, myosin ATPase activity and coupling of actin-myosin filaments to the plasma membrane, is cleaved during apoptosis to generate a truncated active form. The activity of ROCK proteins is both necessary and sufficient for formation of membrane blebs and for re-localization of fragmented DNA into blebs and apoptotic bodies.
Original language | English |
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Pages (from-to) | 339-45 |
Number of pages | 7 |
Journal | Nature Cell Biology |
Volume | 3 |
Issue number | 4 |
DOIs | |
Publication status | Published - Apr 2001 |
Keywords
- 3T3 Cells
- Animals
- Apoptosis
- Caspase Inhibitors
- Caspases
- Cell Membrane
- DNA
- DNA Fragmentation
- Enzyme Activation
- Humans
- Intracellular Signaling Peptides and Proteins
- Mice
- Protein-Serine-Threonine Kinases
- Recombinant Fusion Proteins
- Tumor Cells, Cultured
- rho-Associated Kinases