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Vol. 10, Issue 4, 1179-1190, April 1999
and
*Center for Vascular Biology, Department of Physiology, University
of Connecticut School of Medicine, Farmington, Connecticut 06030; and
The endothelial-derived G-protein-coupled receptor EDG-1 is a
high-affinity receptor for the bioactive lipid mediator
sphingosine-1-phosphate (SPP). In the present study, we
constructed the EDG-1-green fluorescent protein (GFP) chimera to
examine the dynamics and subcellular localization of SPP-EDG-1
interaction. SPP binds to EDG-1-GFP and transduces intracellular
signals in a manner indistinguishable from that seen with the wild-type
receptor. Human embryonic kidney 293 cells stably transfected with the
EDG-1-GFP cDNA expressed the receptor primarily on the plasma
membrane. Exogenous SPP treatment, in a dose-dependent manner, induced
receptor translocation to perinuclear vesicles with a
Department of Biochemistry and Molecular Biology,
Georgetown University School of Medicine, Washington, DC 20007
1/2 of ~15 min. The EDG-1-GFP-containing vesicles
are distinct from mitochondria but colocalize in part with endocytic
vesicles and lysosomes. Neither the low-affinity agonist
lysophosphatidic acid nor other sphingolipids, ceramide, ceramide-1-phosphate, or sphingosylphosphorylcholine, influenced receptor trafficking. Receptor internalization was completely inhibited
by truncation of the C terminus. After SPP washout, EDG-1-GFP recycles
back to the plasma membrane with a 1/2 of ~30 min. We
conclude that the high-affinity ligand SPP specifically induces the
reversible trafficking of EDG-1 via the endosomal pathway and that the
C-terminal intracellular domain of the receptor is critical for this process.
Corresponding author. E-mail address:
hla{at}sun.uchc.edu.
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