Journal
CELLULAR SIGNALLING
Volume 18, Issue 11, Pages 1906-1913Publisher
ELSEVIER SCIENCE INC
DOI: 10.1016/j.cellsig.2006.02.005
Keywords
PIP kinase; protein kinase D; inositol lipid; protein phosphorylation
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Funding
- Wellcome Trust [063581] Funding Source: Medline
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The type II PIP kinases phosphorylate the poorly understood inositol lipid PtdIns5P, producing the multi-functional lipid product PtdIns(4,5) P-2. To investigate the regulation of these enzymes by phosphorylation, we partially purified a protein kinase from pig platelets that phosphorylated type II alpha PIP kinase on an activation loop threonine residue, T376. Pharmacological studies suggested this protein kinase was protein kinase D (PKD), and in vitro experiments confirmed this identification. A phospho-specific antibody was developed and used to demonstrate phosphorylation of T376 in living cells, and its enhancement under conditions in which PKD was activated. Although we were unable to determine the effects of phosphorylation on PIP kinase activity directly, mutation of T376 to aspartate significantly inhibited enzyme activity. We conclude that the type II PIP kinases are physiological targets for PKD phosphorylation, and that this modification is likely to regulate inositol lipid turnover by inhibition of these lipid kinases. (c) 2006 Elsevier Inc. All rights reserved.
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