Abstract
The activities of several membrane proteins are modulated by the presence of non-lamellar forming lipids. Although several proteins are activated by the presence of these lipids, the molecular mechanism by which this activation occurs is different for different proteins. We have studied two enzymes that are activated by non-lamellar forming lipids in different ways; protein kinase C (PKC) and CTP:phosphocholine cytidylyltransferase (CT). CT is the enzyme that regulates the rate of synthesis of phosphatidylcholine. For many lipid systems, there is a quantitative correlation between the calculated curvature strain of the membrane and the activation of this enzyme. For many lipid systems, including liposomes containing a series of homologous di-18:l phosphatidylethanolamines, there is a quantitative correlation between the extent of activation of CT and the curvature strain in the membrane. In contrast, the order in which this series of di-18:l phosphatidylethanolamines enhances the activity of protein kinase C does not correlate with membrane curvature strain. However, the order in which these lipids affect the quenching of the fluorescent probe 4-[(n-dodecylthio)-methyl]-7-(N,N-dimethylamino)-coumarin by doxyl groups positioned in the acyl chain region of the membrane is well correlated with the extent of activation of protein kinase C. This fluorescent probe is monitoring a property of the membrane that is affected by the presence of non-lamellar forming lipids.
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Epand, R.M., Cornell, R., Davies, S.M.A., Kraayenhof, R. (2002). Mechanisms of the Modulation of Membrane Interfacial Enzyme Catalysis by Non-lamellar Forming Lipids: Comparison with the Behavior of a Fluorescent Probe in Membranes. In: Kraayenhof, R., Visser, A.J.W.G., Gerritsen, H.C. (eds) Fluorescence Spectroscopy, Imaging and Probes. Springer Series on Fluorescence, vol 2. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-56067-5_16
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DOI: https://doi.org/10.1007/978-3-642-56067-5_16
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