Journal Article

Tyrosine Sulphation of Sphingosine 1-Phosphate 1 (S1P<sub>1</sub>) is Required for S1P-mediated Cell Migration in Primary Cultures of Human Umbilical Vein Endothelial Cells

Yuan-Li Huang, Hsiao-Sheng Lin, Shee-Uan Chen and Hsinyu Lee

in The Journal of Biochemistry

Published on behalf of The Japanese Biochemical Society

Volume 146, issue 6, pages 815-820
Published in print December 2009 | ISSN: 0021-924X
Published online August 2009 | e-ISSN: 1756-2651 | DOI:

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Sphingosine 1-phosphate (S1P), a lysophospholipid mediator, regulates diverse functions of many types of cells by binding to specific G protein-coupled receptors termed S1P1–S1P5. In T-cells, tyrosine sulphation of S1P1 is required for high-affinity binding of S1P and fully functional signalling. In this study, we showed that tyrosine sulphation of S1P1 is necessary for S1P-induced Src phosphorylation and migration in human umbilical vein endothelial cells (HUVECs). Both substitution of phenylalanine (F) for tyrosine (Y) in S1P1 and inhibition of tyrosine sulphation blocked c-Src phosphorylation and migration in HUVECs. In addition, overexpression of mutant (F19, 22F) S1P1, lacking tyrosine sulphation sites, suppressed native S1P1 effects on migration, actin rearrangement and lamellipodia formation. Therefore, tyrosine sulphation of S1P1 is required for its optimal transduction of signals from S1P in HUVECs.

Keywords: endothelial cells; migration; sphingosine 1-phosphate; Src; tyrosine sulphation

Journal Article.  2747 words.  Illustrated.

Subjects: Biochemistry