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Akt-mediated phosphorylation of the G protein-coupled receptor EDG-1 is required for endothelial cell chemotaxis.

Abstract：

:The role of the protein kinase Akt in cell migration is incompletely understood. Here we show that sphingosine-1-phosphate (S1P)-induced endothelial cell migration requires the Akt-mediated phosphorylation of the G protein-coupled receptor (GPCR) EDG-1. Activated Akt binds to EDG-1 and phosphorylates the third intracellular loop at the T(236) residue. Transactivation of EDG-1 by Akt is not required for G(i)-dependent signaling but is indispensable for Rac activation, cortical actin assembly, and chemotaxis. Indeed, T236AEDG-1 mutant sequestered Akt and acted as a dominant-negative GPCR to inhibit S1P-induced Rac activation, chemotaxis, and angiogenesis. Transactivation of GPCRs by Akt may constitute a specificity switch to integrate rapid G protein-dependent signals into long-term cellular phenomena such as cell migration.

journal_name

Mol Cell

journal_title

Molecular cell

authors

Lee MJ,Thangada S,Paik JH,Sapkota GP,Ancellin N,Chae SS,Wu M,Morales-Ruiz M,Sessa WC,Alessi DR,Hla T

doi

10.1016/s1097-2765(01)00324-0

subject

Has Abstract

pub_date

2001-09-01 00:00:00

pages

693-704

issue

3

eissn

1097-2765

issn

1097-4164

pii

S1097-2765(01)00324-0

journal_volume

8

pub_type

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