The last five amino acid residues at the C-terminus of PRK1 /KKN is essential for full lipid responsiveness

Lim, Wee Guan, Zhu, Yimin, Wang, Chern-Hoe, Tan, Bee Jen, Armstrong, Jeffrey S., Dockland, Terje, Yang, Hongyuan, Zhu, Yi-Zhun, Teo, Tian Seng and Duan, Wei 2005, The last five amino acid residues at the C-terminus of PRK1 /KKN is essential for full lipid responsiveness, Cellular signalling, vol. 17, no. 9, pp. 1084-1097.

Attached Files
Name Description MIMEType Size Downloads

Title The last five amino acid residues at the C-terminus of PRK1 /KKN is essential for full lipid responsiveness
Author(s) Lim, Wee Guan
Zhu, Yimin
Wang, Chern-Hoe
Tan, Bee Jen
Armstrong, Jeffrey S.
Dockland, Terje
Yang, Hongyuan
Zhu, Yi-Zhun
Teo, Tian Seng
Duan, Wei
Journal name Cellular signalling
Volume number 17
Issue number 9
Start page 1084
End page 1097
Publisher Elsevier Inc.
Place of publication New York, N.Y.
Publication date 2005-09
ISSN 0898-6568
1873-3913
Summary 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.
Language eng
Field of Research 060199 Biochemistry and Cell Biology not elsewhere classified
HERDC Research category C1.1 Refereed article in a scholarly journal
Copyright notice ©2004, Elsevier Inc.
Persistent URL http://hdl.handle.net/10536/DRO/DU:30009151

Document type: Journal Article
Collection: School of Medicine
Connect to link resolver
 
Unless expressly stated otherwise, the copyright for items in DRO is owned by the author, with all rights reserved.

Versions
Version Filter Type
Citation counts: TR Web of Science Citation Count  Cited 7 times in TR Web of Science
Scopus Citation Count Cited 2 times in Scopus
Google Scholar Search Google Scholar
Access Statistics: 460 Abstract Views, 0 File Downloads  -  Detailed Statistics
Created: Mon, 13 Oct 2008, 15:52:38 EST

Every reasonable effort has been made to ensure that permission has been obtained for items included in DRO. If you believe that your rights have been infringed by this repository, please contact drosupport@deakin.edu.au.