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ROCK-I is a Rho-associated serine/threonine kinase isozyme that mediates RhoA-induced assembly of focal adhesions and actin stress fibers. It contains an N-terminal kinase domain, a central 600 amino acid long coiled-coil region, a C-terminal pleckstrin homology region (PH) and a Cys-rich zinc finger motif. The ROCK-I kinase domain is approximately 90% identical to that of ROCK-II. ROCK-I binds GTP-bound Rho through a Rho-binding domain (RBD). As a result, the kinase activity of ROCK-I is moderately stimulated. The ROCK isozymes regulate cell contractility through phosphorylation of the myosin light chain. This effect results from either the inhibition of the myosin phosphatase or by direct phosphorylation of the myosin light chain, thus bypassing the myosin light chain kinase. In addition, ROCK-I activates the ubiquitously expressed Na-H exchanger (NHE1) via a number of mechanisms including RhoA. NHE1 may mediate ROCK-I-induced changes in the actin cytoskeleton. Therefore, ROCK-I plays an important role in the regulation of focal adhesion and stress fiber formation.Host Species: MouseClone: 46Isotype: IgG1Species Reactivity: MouseImmunogen: Mouse ROCK-I aa. 906-1012Formula Weight [Chemical]: 160kDaImmunofluorescence, Western Blotting
