ROCK (Rho-associated kinase), a family of serine/threonine kinases, is an important downstream target of GTPase Rho and plays an important role in Rho-mediated signaling. Two isoforms of ROCK have been identified (ROCK1 and ROCK2). ROCK is composed of N-terminal catalytic, coiled-coil and C-terminal PH (pleckstrin homology) domains. The C-terminus of ROCK negatively regulates its kinase activity (1,2). Caspase-3-induced cleavage of ROCK1 and direct cleavage of ROCK2 by granzyme B (grB) activates ROCK and leads to phosphorylation of myosin light chain and inhibition of myosin phosphatase (3). This phosphorylation may account for the mechanism by which Rho regulates cytokinesis, cell motility, cell membrane blebbing during apoptosis and smooth muscle contraction (4-6).
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