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Mol. Cell. Biol., Oct 1996, 5313-5327, Vol 16, No. 10
Copyright © 1996, American Society for Microbiology

The p160 RhoA-binding kinase ROK alpha is a member of a kinase family and is involved in the reorganization of the cytoskeleton

T Leung, XQ Chen, E Manser and L Lim
Glaxo-IMCB Group, Institute of Molecular & Cell Biology, National University of Singapore, Singapore.

The GTPase RhoA has been implicated in various cellular activities, including the formation of stress fibers, motility, and cytokinesis. We recently reported on a p150 serine/threonine kinase (termed ROK alpha) binding RhoA only in its active GTP-bound state and on its cDNA; introduction of RhoA into HeLa cells resulted in translocation of the cytoplasmic kinase to plasma membranes, consistent with ROK alpha being a target for RhoA (T. Leung, E. Manser, L. Tan, and L. Lim, J. Biol. Chem. 256:29051-29054, 1995). Reanalysis of the cDNA revealed that ROK alpha contains an additional N-terminal region. We also isolated another cDNA which encoded a protein (ROK beta) with 90% identity to ROK alpha in the kinase domain. Both ROK alpha and ROK beta, which had a molecular mass of 160 kDa, contained a highly conserved cysteine/histidine-rich domain located within a putative pleckstrin homology domain. The kinases bound RhoA, RhoB, and RhoC but not Rac1 and Cdc42. The Rho-binding domain comprises about 30 amino acids. Mutations within this domain caused partial or complete loss of Rho binding. The morphological effects of ROK alpha were investigated by microinjecting HeLa cells with DNA constructs encoding various forms of ROK alpha. Full-length ROK alpha promoted formation of stress fibers and focal adhesion complexes, consistent with its being an effector of RhoA. ROK alpha truncated at the C terminus promoted this formation and also extensive condensation of actin microfilaments and nuclear disruption. The proteins exhibited protein kinase activity which was required for stress fiber formation; the kinase-dead ROK alpha K112A and N-terminally truncated mutants showed no such promotion. The latter mutant instead induced disassembly of stress fibers and focal adhesion complexes, accompanied by cell spreading. These effects were mediated by the C-terminal region containing Rho-binding, cysteine/histidine- rich, and pleckstrin homology domains. Thus, the multidomained ROK alpha appears to be involved in reorganization of the cytoskeleton, with the N and C termini acting as positive and negative regulators, respectively, of the kinase domain whose activity is crucial for formation of stress fibers and focal adhesion complexes.


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  • Shiokawa, S., Iwashita, M., Akimoto, Y., Nagamatsu, S., Sakai, K., Hanashi, H., Kabir-Salmani, M., Nakamura, Y., Uehata, M., Yoshimura, Y. (2002). Small Guanosine Triphospatase RhoA and Rho-Associated Kinase as Regulators of Trophoblast Migration. J. Clin. Endocrinol. Metab. 87: 5808-5816 [Abstract] [Full Text]  
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  • Tanaka, H., Yamashita, T., Asada, M., Mizutani, S., Yoshikawa, H., Tohyama, M. (2002). Cytoplasmic p21Cip1/WAF1 regulates neurite remodeling by inhibiting Rho-kinase activity. JCB 158: 321-329 [Abstract] [Full Text]  
  • Pawlak, G., Helfman, D. M. (2002). MEK Mediates v-Src-induced Disruption of the Actin Cytoskeleton via Inactivation of the Rho-ROCK-LIM Kinase Pathway. J. Biol. Chem. 277: 26927-26933 [Abstract] [Full Text]  
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  • Tsuji, T., Ishizaki, T., Okamoto, M., Higashida, C., Kimura, K., Furuyashiki, T., Arakawa, Y., Birge, R. B., Nakamoto, T., Hirai, H., Narumiya, S. (2002). ROCK and mDia1 antagonize in Rho-dependent Rac activation in Swiss 3T3 fibroblasts. JCB 157: 819-830 [Abstract] [Full Text]  
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