Please use this identifier to cite or link to this item: https://doi.org/10.1016/j.abb.2008.09.008
Title: The C-terminus of PRK2/PKNγ is required for optimal activation by RhoA in a GTP-dependent manner
Authors: Lim, W.G.
Chen, X.
Liu, J.-p.
Tan, B.J. 
Zhou, S.
Smith, A.
Lees, N.
Hou, L.
Gu, F.
Yu, X.Y.
Du, Y.
Smith, D.
Verma, C.
Liu, K.
Duan, W.
Keywords: PDK-1
PKC
PRK2
Rho
Signal transduction
Issue Date: 15-Nov-2008
Citation: Lim, W.G., Chen, X., Liu, J.-p., Tan, B.J., Zhou, S., Smith, A., Lees, N., Hou, L., Gu, F., Yu, X.Y., Du, Y., Smith, D., Verma, C., Liu, K., Duan, W. (2008-11-15). The C-terminus of PRK2/PKNγ is required for optimal activation by RhoA in a GTP-dependent manner. Archives of Biochemistry and Biophysics 479 (2) : 170-178. ScholarBank@NUS Repository. https://doi.org/10.1016/j.abb.2008.09.008
Abstract: PRK2/PKNγ is a Rho effector and a member of the protein kinase C superfamily of serine/threonine kinases. Here, we explore the structure-function relationship between various motifs in the C-terminal half of PRK2 and its kinase activity and regulation. We report that two threonine residues at conserved phosphoacceptor position in the activation loop and the turn motif are essential for the catalytic activity of PRK2, but the phosphomimetic Asp-978 at hydrophobic motif is dispensable for kinase catalytic competence. Moreover, the PRK2-Δ958 mutant with the turn motif truncated still interacts with 3-phosphoinositide-dependent kinase-1 (PDK-1). Thus, both the intact hydrophobic motif and the turn motif in PRK2 are dispensable for the binding of PDK-1. We also found that while the last seven amino acid residues at the C-terminus of PRK2 are not required for the activation of the kinase by RhoA in vitro, however, the extreme C-terminal segment is critical for the full activation of PRK2 by RhoA in cells in a GTP-dependent manner. Our data suggest that the extreme C-terminus of PRK2 may represent a potential drug target for effector-specific pharmacological intervention of Rho-medicated biological processes. © 2008 Elsevier Inc. All rights reserved.
Source Title: Archives of Biochemistry and Biophysics
URI: http://scholarbank.nus.edu.sg/handle/10635/106426
ISSN: 00039861
DOI: 10.1016/j.abb.2008.09.008
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