Please use this identifier to cite or link to this item:
|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.|
|Appears in Collections:||Staff Publications|
Show simple item record
Files in This Item:
There are no files associated with this item.
checked on Dec 4, 2019
WEB OF SCIENCETM
checked on Dec 4, 2019
checked on Dec 2, 2019
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.