Please use this identifier to cite or link to this item: https://doi.org/10.1016/j.cellsig.2004.12.003
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dc.titleThe last five amino acid residues at the C-terminus of PRK1/PKN is essential for full lipid responsiveness
dc.contributor.authorWee, G.L.
dc.contributor.authorZhu, Y.
dc.contributor.authorBee, J.T.
dc.contributor.authorArmstrong, J.S.
dc.contributor.authorYang, H.
dc.contributor.authorTian, S.T.
dc.contributor.authorDuan, W.
dc.contributor.authorWang, C.-H.
dc.contributor.authorDokland, T.
dc.contributor.authorZhu, Y.-Z.
dc.date.accessioned2011-11-29T06:11:15Z
dc.date.available2011-11-29T06:11:15Z
dc.date.issued2005
dc.identifier.citationWee, 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.identifier.issn08986568
dc.identifier.urihttp://scholarbank.nus.edu.sg/handle/10635/28939
dc.description.abstractPRK1/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.
dc.description.urihttp://libproxy1.nus.edu.sg/login?url=http://dx.doi.org/10.1016/j.cellsig.2004.12.003
dc.sourceScopus
dc.typeArticle
dc.contributor.departmentBIOCHEMISTRY
dc.contributor.departmentPHARMACOLOGY
dc.description.doi10.1016/j.cellsig.2004.12.003
dc.description.sourcetitleCellular Signalling
dc.description.volume17
dc.description.issue9
dc.description.page1084-1097
dc.description.codenCESIE
dc.identifier.isiut000230612100005
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