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Originally published In Press as doi:10.1074/jbc.M201391200 on April 11, 2002

J. Biol. Chem., Vol. 277, Issue 25, 22974-22979, June 21, 2002
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Detecting Protein-Phospholipid Interactions
EPIDERMAL GROWTH FACTOR-INDUCED ACTIVATION OF PHOSPHOLIPASE D1b IN SITU*

William E. HughesDagger §, Banafshé Larijani||, and Peter J. ParkerDagger ||**

From the Dagger  Protein Phosphorylation Laboratory and || Cell Biophysics Laboratory, Cancer Research United Kingdom London Research Institute, Lincoln's Inn Fields Laboratories, 44 Lincoln's Inn Fields, London WC2A 3PX, United Kingdom

Phospholipase D (PLD) proteins have been identified in secretory and endocytic vesicles, consistent with their proposed role in regulating membrane traffic. However, their sites of catalytic action remain obscure. We have developed here a novel, analytical approach to monitor PLD activation in intact cells employing lifetime imaging microscopy to measure fluorescence resonance energy transfer between protein and membrane phospholipid. Verification and application of this technique demonstrates a dispersed endosomal, epidermal growth factor-induced activation of the PLD1b isoform. Application of this approach will facilitate the spatial resolution of many protein-phospholipid interactions that are key events in the regulation of cellular processes.

* The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

§ Supported by a Royal Society Fellowship. Present address: The Garvan Institute of Medical Research, 384 Victoria Street, Sydney, NSW 2010, Australia.

These authors contributed equally to this work.

** To whom correspondence should be addressed. E-mail: peter.parker@cancer.org.uk.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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