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Vol. 11, Issue 12, 4359-4368, December 2000
§
*Department of Pharmacology and G protein-coupled and tyrosine kinase receptor activation of
phospholipase D1 (PLD1) play key roles in agonist-stimulated cellular
responses such as regulated exocytosis, actin stress fiber formation,
and alterations in cell morphology and motility. Protein Kinase C,
ADP-ribosylation factor (ARF), and Rho family members activate PLD1 in
vitro; however, the actions of the stimulators on PLD1 in vivo have
been proposed to take place through indirect pathways. We have used the
yeast split-hybrid system to generate PLD1 alleles that fail to bind to
or to be activated by RhoA but that retain wild-type responses to ARF
and PKC. These alleles then were employed in combination with alleles
unresponsive to PKC or to both stimulators to examine the activation of
PLD1 by G protein-coupled receptors. Our results demonstrate that
direct stimulation of PLD1 in vivo by RhoA (and by PKC) is critical for significant PLD1 activation but that PLD1 subcellular localization and
regulated phosphorylation occur independently of these stimulatory pathways.
the Center for
Developmental Genetics, University Medical Center at Stony Brook, Stony
Brook, New York 11794-5140; and the Department of Life
Science, Division of Molecular and Life Sciences, Pohang University of
Science and Technology, Pohang, 790-784, Korea
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