The Rho target protein, Rho-associated coiled coil-containing protein kinase (ROCK)-1 has been found to be a new Caspase-3 substrate. ROCK, one of the effectors of the small GTPase Rho, has recently been shown to contribute significantly to myosin light chain (MLC) activation through two pathways: direct phosphorylation of MLC and phosphorylation of MLC phosphatase, leading to its inhibition. The increase in cellular contractility that is necessary for apoptotic membrane blebbing implies sustained augmentation of MLC phosphorylation. ROCK-1 consists of an amino-terminal kinase domain and an inhibitory cysteine/histidine-rich C-terminal domain that is located within a pleckstrin-homology region. They are joined by a variable region that contains the Rho-binding domain. During apoptosis, ROCK-I is cleaved by caspase-3 at a conserved DETD1113/G sequence and its carboxy-terminal inhibitory domain is removed, resulting in deregulated and constitutive kinase activity. The caspase-3-mediated cleavage and activation of ROCK I induces phosphorylation of MLC and membrane blebbing, one of the first events in the execution phase of apoptosis.View more
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