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J Biol Chem, Vol. 274, Issue 1, 494-502, January 1, 1999
From the Department of Pharmacological Sciences and the Institute
for Cell and Developmental Biology, State University of New York at
Stony Brook, Stony Brook, New York 11794-8651
The mammalian phosphatidylcholine-specific
phospholipase D (PLD) enzymes PLD1 and PLD2 have been proposed to play
roles in signal transduction and membrane vesicular trafficking in
distinct subcellular compartments. PLD1 is activated in a synergistic
manner in vitro by protein kinase C-
Molecular Analysis of Mammalian Phospholipase D2
, ADP-ribosylation
factor 1 (ARF1), and Rho family members. In contrast, PLD2 is
constitutively active in vitro. We describe here molecular
analysis of PLD2. We show that the NH2-terminal 308 amino
acids are required for PLD2's characteristic high basal activity.
Unexpectedly, PLD2 lacking this region becomes highly responsive to ARF
proteins and displays a modest preference for activation by ARF5.
Chimeric analysis of PLD1 and PLD2 suggests that the ARF-responsive
region is in the PLD carboxyl terminus. We also inserted into PLD2 a
region of sequence unique to PLD1 known as the "loop" region, which
had been proposed initially to mediate effector stimulation but that subsequently was shown instead to be required in part for the very low
basal activity characteristic of PLD1. The insertion decreased PLD2
activity, consistent with the latter finding. Finally, we show that the
critical role undertaken by the conserved carboxyl terminus is unlikely
to involve promoting PLD association with membrane surfaces.
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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