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J. Biol. Chem., Vol. 276, Issue 18, 15337-15344, May 4, 2001
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From the Agonist-induced intracellular
Ca2+ signals following phospholipase C (PLC)
activation display a variety of patterns, including transient,
sustained, and oscillatory behavior. These Ca2+ changes
have been well characterized, but detailed kinetic analyses of PLC
activation in single living cells is lacking, due to the absence of
suitable indicators for use in vivo. Recently, green fluorescent protein-tagged pleckstrin homology domains have been employed to monitor PLC activation in single cells, based on (confocal) imaging of their fluorescence translocation from the membrane to the
cytosol that occurs upon hydrolysis of phosphatidylinositol bisphosphate. Here we describe fluorescence resonance energy transfer between pleckstrin homology domains of PLC
Monitoring Agonist-induced Phospholipase C Activation in Live
Cells by Fluorescence Resonance Energy Transfer*
,§,
Division of Cell Biology, The Netherlands
Cancer Institute, Plesmanlaan 121, 1066CX Amsterdam, The
Netherlands and the ¶ Endocrinology and Reproduction Research
Branch, National Institutes of Health,
Bethesda, Maryland 20892-4510
1 tagged with cyan and
yellow fluorescent proteins as a sensitive readout of
phosphatidylinositol bisphosphate metabolism for use both in cell
populations and in single cells. Fluorescence resonance energy transfer
requires significantly less excitation intensity, enabling prolonged
and fast data acquisition without the cell damage that limits confocal experiments. It also allows experiments on motile or extremely flat
cells, and can be scaled to record from cell populations as well as
single neurites. Characterization of responses to various agonists by
this method reveals that stimuli that elicit very similar
Ca2+ mobilization responses can exhibit widely different
kinetics of PLC activation, and that the latter appears to follow
receptor activation more faithfully than the cytosolic Ca2+ transient.
*
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.
To whom correspondence should be addressed. Tel.:
31-20-512-1933; Fax: 31-20-512-1944; E-mail: kees@nki.nl.
§
Current address: Swammerdam Institute for Life Sciences, University
of Amsterdam, Kruislaan 320, 1098SM Amsterdam.
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