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Sci. STKE, 9 October 2001
Vol. 2001, Issue 103, p. tw365
[DOI: 10.1126/stke.2001.103.tw365]

EDITORS' CHOICE

Chemotaxis The Long and Short of EDG-1 Signaling

Vascular endothelial cell migration is regulated in part by the bioactive lipid sphingosine 1-phosphate (S1P), which acts through the G protein-coupled receptor EDG-1. Lee et al. propose that EDG-1 may stimulate cell mobility by inducing the long-term cellular changes that commit cells to chemotaxis. Stimulation of endothelial cells with S1P induced the phosphorylation of the cytoplasmic protein kinase AKT and its subsequent association with EDG-1. Phosphorylation of a critical threonine residue in EDG-1 by AKT was required for EDG-1 to stimulate the assembly of cortical actin and chemotaxis. However, this modification was not required for rapid EDG-1-mediated signaling responses including intracellular calcium mobilization. Phosphorylation of the receptor by AKT may serve as a switch for EDG-1 to make the transition from rapid cellular responses to those that regulate motility.

M.-J. Lee, S. Thangada, J.-H. Paik, G. P. Sapkota, N. Ancellin, S.-S. Chae, M. Wu, M. Morales-Ruiz, W .C. Sessa, D. R. Alessi, T. Hla, Akt-meditaed phosphorylation of the G protein-coupled receptor EDG-1 is required for endothelial cell chemotaxis. Mol. Cell 8, 693-704 (2001). [Online Journal]

Citation: The Long and Short of EDG-1 Signaling. Sci. STKE 2001, tw365 (2001).


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