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|dc.title||The last five amino acid residues at the C-terminus of PRK1/PKN is essential for full lipid responsiveness|
|dc.identifier.citation||Wee, G.L., Zhu, Y., Bee, J.T., Armstrong, J.S., Yang, H., Tian, S.T., Duan, W., Wang, C.-H., Dokland, T., Zhu, Y.-Z. (2005). The last five amino acid residues at the C-terminus of PRK1/PKN is essential for full lipid responsiveness. Cellular Signalling 17 (9) : 1084-1097. ScholarBank@NUS Repository. https://doi.org/10.1016/j.cellsig.2004.12.003|
|dc.description.abstract||PRK1/PKN is a member of the protein kinase C (PKC) superfamily of serine/threonine protein kinases. Despite its important role as a RhoA effector, limited information is available regarding how this kinase is regulated. We show here that the last seven amino acid residues at the C-terminus is dispensable for the catalytic activity of PRK1 but is critical for the in vivo stability of this kinase. Surprisingly, the intact hydrophobic motif in PRK1 is dispensable for 3-phosphoinositide-dependent kinase-1 (PDK-1) binding and phosphorylation of the activation loop, as the PRK1-Δ940 mutant lacking the last two residues of the hydrophobic motif and the last 5 residues at the C-terminus interacts with PDK-1 in vivo and has a similar specific activity as the wild-type protein. We also found that the last four amino acid residues at the C-terminus of PRK1 is critical for the full lipid responsiveness as the PRK1-Δ942 deletion mutant is no longer activated by arachidonic acid. Our data suggest that the very C-terminus in PRK1 is critically involved in the control of the catalytic activity and activation by lipids. Since this very C-terminal segment is the least conserved among members of the PKC superfamily, it would be a promising target for isozyme-specific pharmaceutical interventions. © 2004 Elsevier Inc. All rights reserved.|
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