Homodimerization and heterodimerization of S1P/EDG sphingosine-1-phosphate receptors.
Sphingosine-1-phosphate (S1P) binds to and signals through several members of a group of G protein-coupled receptors (GPCRs) known as the S1P/EDG family. Several of these receptors are coexpressed in various cell types and recent reports have shown that biological effects of S1P often require more than one S1P receptor subtype. Recent evidence indicates that many GPCRs exist as dimers. We show that S1P receptors form both homodimers as well as heterodimers with other members of the S1P subfamily of receptors. We also discuss the role that GPCR dimers play in receptor function and what this may mean for S1P signaling.
Van Brocklyn
James R
JR
Department of Pathology, The Ohio State University, 4164 Graves Hall, 333 W. 10th Ave., Columbus, OH 43210, USA. van-brocklyn.1@osu.edu
Behbahani
Babak
B
Lee
Norman H
NH
D000818:Animals; D002454:Cell Differentiation / Q000235:genetics; D019281:Dimerization; D004730:Endothelium, Vascular / Q000166:cytology; D019204:GTP-Binding Proteins / Q000502:physiology*; D006801:Humans; D011956:Receptors, Cell Surface / Q000502:physiology*; D043562:Receptors, G-Protein-Coupled; D049312:Receptors, Lysophospholipid; D015398:Signal Transduction
D011956:Receptors, Cell Surface; D043562:Receptors, G-Protein-Coupled; D049312:Receptors, Lysophospholipid; D019204:GTP-Binding Proteins