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Vol. 273, Issue 3, 1506-1510, January 16, 1998
From We have functionally expressed the human cDNA
encoding the putative lysophosphatidic acid (LPA) receptor Edg-2
(Vzg-1) in Saccharomyces cerevisiae in an attempt to
determine the agonist specificity of this G-protein-coupled receptor.
LPA activated the pheromone response pathway in S. cerevisiae
expressing Edg-2 in a time- and dose-dependent manner
as determined by induction of a pheromone-responsive
FUS1::lacZ reporter gene. LPA-mediated activation
of the pheromone response pathway was dependent on mutational
inactivation of the SST2 gene, the GTPase-activating protein for the yeast G
Edg-2/Vzg-1 Couples to the Yeast Pheromone Response Pathway
Selectively in Response to Lysophosphatidic Acid
,,,,, and
LXR Biotechnology Inc., Richmond, California
94804 and ¶ University of Tennessee College of Medicine,
Department of Physiology and Biophysics, Memphis, Tennessee 38163
protein (the GPA1
gene product). This indicates that, in sst2
yeast
cells, Edg-2 can efficiently couple to the yeast heterotrimeric
G-protein in response to LPA and activate the yeast mitogen-activated
protein kinase pathway. The Edg-2 receptor showed a high degree of
specificity for LPA; other lyso-glycerophospholipids, sphingosine
1-phosphate, and diacyl-glycerophospholipids did not activate
FUS1::lacZ. LPA analogs including a cyclic
phosphoester form and ether-linked forms of LPA activated
FUS1::lacZ, although fatty acid chains of 6 and 10 carbons did not activate FUS1::lacZ,
suggesting a role for the side chain in ligand binding or receptor
activation. These results indicate that Edg-2 encodes a highly specific
LPA receptor.
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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