@article{oai:nagoya.repo.nii.ac.jp:00005691,
 author = {Mizuno, Tomoaki and Amano, Mutsuki and Kaibuchi, Kozo and Nishida, Yasuyoshi},
 issue = {2},
 journal = {Gene},
 month = {Oct},
 note = {The Rho family of small GTPases and their associated regulators and targets are essential mediators of diverse morphogenetic events in development. Mammalian Rho‐kinase/ROKα, one of the targets of Rho, has been shown to bind to Rho in GTP－bound form and to phosphorylate the myosin light chain (MLC) and the myosin binding subunit (MBS) of myosin phosphatase, resulting in the activation of myosin. Thus, Rho‐kinase/ROKα has been suggested to play essential roles in the formation of stress fibers and focal adhesions. We have identified the Drosophila homolog of Rho‐kinase/ROKα, DRho‐kinase, which has conserved the basic structural feature of Rho‐kinase/ROKα consisting of the N‐terminal kinase, central coiled-coil and C‐terminal pleckstrin homology (PH) domains. A two‐hybrid analysis demonstrated that DRho‐kinase interacts with the GTP‐bound form of the Drosophila Rho, Drho1, at the conserved Rho-binding site. DRho‐kinase can phosphorylate MLC and MBS, preferable substrates for bovine Rho‐kinase, in vitro. DRho‐kinase is ubiquitously expressed throughout development, in a pattern essentially identical to that of Drho1. These results suggest that DRho‐kinase is an effector of Drho1.},
 pages = {437--444},
 title = {Identification and characterization of Drosophila homolog of Rho-kinase},
 volume = {238},
 year = {1999}
}