Please use this identifier to cite or link to this item: https://doi.org/10.1074/jbc.270.49.29051
Title: A novel serine/threonine kinase binding the ras-related RhoA GTPase which translocates the kinase to peripheral membranes
Authors: Leung, T. 
Manser, E. 
Tan, L.
Lim, L.
Issue Date: 1995
Citation: Leung, T., Manser, E., Tan, L., Lim, L. (1995). A novel serine/threonine kinase binding the ras-related RhoA GTPase which translocates the kinase to peripheral membranes. Journal of Biological Chemistry 270 (49) : 29051-29054. ScholarBank@NUS Repository. https://doi.org/10.1074/jbc.270.49.29051
Abstract: We previously reported the cloning of a serine/threonine kinase, PAK (for p21 (Cdc42/Rac)-activated kinase), which binds to the Ras-related GTPases Cdc42Hs and Rac1 (Manser, E., Leung, T., Salihuddin, H., Zhao, Z-s., and Lim, L. (1994) Nature 367, 40-46). These p21 proteins together with RhoA comprise the Rho subfamily of proteins that are involved in morphological events. We now report the isolation of a rat cDNA encoding a 150-kDa protein, which specifically binds RhoA in its GTP form and contains an N-terminal serine/threonine kinase domain highly related to the human myotonic dystrophy kinase and a cysteine-rich domain toward the C terminus. The RhoA binding domain is unrelated to other p21 binding domains. Antibody raised against the kinase domain of the predicted protein, termed ROKα (for ROKα, RhoA- binding kinase), recognized a ubiquitous 150-kDa protein. The brain p150 purified by affinity chromatography with RhoA exhibited serine/threonine kinase activity. In cultured cells, immunoreactive p150 was recruited to membranes upon transfection with dominant positive RhoA(V14) mutant and was localized with actin microfilaments at the cell periphery. These results are consistent with a role for the kinase ROKα as an effector for RhoA.
Source Title: Journal of Biological Chemistry
URI: http://scholarbank.nus.edu.sg/handle/10635/115564
ISSN: 00219258
DOI: 10.1074/jbc.270.49.29051
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