Roles for N-glycosylation in the dynamics of Edg-1/S1P1 in sphingosine 1-phosphate-stimulated cells

Glycoconj J. 2004;21(8-9):497-501. doi: 10.1007/s10719-004-5540-8.


Sphingosine 1-phosphate (Sph-1-P) is a bioactive lipid mediator released from activated platelets. To date, 5 seven-transmembrane-spanning receptors, Edg-1/S1P1, Edg-3/S1P3, Edg-5/S1P2, Edg-6/S1P4 and Edg-8/S1P5, have been identified as specific Sph-1-P receptors. Our recent novel studies established that Edg-1/S1P1 is glycosylated in its N-terminal extracellular portion and further identified the specific glycosylation site as asparagine 30. We also demonstrated that the structure of the N-terminal ectodomain of Edg-1/S1P1 affects both its transport to the cell surface and the N-glycosylation process. These studies revealed a possible regulatory role for the N-glycan on Edg-1/S1P1 in the dynamics of the receptor, such as its lateral and internal movements within the membrane, in ligand-stimulated mammalian cells.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Cell Line
  • Glycosylation
  • Lysophospholipids / metabolism*
  • Lysophospholipids / pharmacology
  • Molecular Sequence Data
  • Protein Transport
  • Receptors, Lysosphingolipid / metabolism*
  • Sequence Alignment
  • Sequence Homology, Amino Acid
  • Sphingosine / analogs & derivatives*
  • Sphingosine / metabolism*
  • Sphingosine / pharmacology


  • Lysophospholipids
  • Receptors, Lysosphingolipid
  • sphingosine 1-phosphate
  • Sphingosine