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J. Biol. Chem., Vol. 269, Issue 34, 21403-21406, 08, 1994
M Liscovitch, V Chalifa, P Pertile, CS Chen and LC Cantley
The activation of phospholipase D (PLD) is a receptor-mediated event that
has been implicated in signal transduction and membrane traffic in
eukaryotic cells. Little is known about the biochemical and molecular
properties of signal-activated PLDs, and none has been isolated. Here we
report that phosphatidylinositol 4,5-bisphosphate (PIP2) potently
stimulates brain membrane PLD activity in vitro in a highly specific
manner. PIP2 increases 10-fold the maximal activity of a partially purified
PLD with an EC50 of < 0.5 mol %. Other acidic phospholipids, including
phosphatidylinositol 4-phosphate, phosphatidylinositol, phosphatidylserine,
and phosphatidic acid, are completely or nearly ineffective. Neomycin, a
high affinity ligand of PIP2, inhibits membrane-bound PLD but has no effect
on the activity of a detergent- solubilized or partially purified enzyme.
The addition of PIP2 restores the sensitivity of partially purified PLD to
neomycin inhibition, indicating that neomycin blocks membrane PLD activity
by binding to endogenous PIP2. These results define a novel function of
PIP2 as a cofactor for brain membrane PLD and suggest that PIP2 synthesis
and hydrolysis could be important determinants in regulating PLD action in
signal transduction and membrane transport.
Novel function of phosphatidylinositol 4,5-bisphosphate as a cofactor for brain membrane phospholipase D
Department of Hormone Research, Weizmann Institute of Science, Rehovot, Israel.
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