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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.

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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
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
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