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J Biol Chem, Vol. 273, Issue 8, 4653-4659, February 20, 1998
From the Institut für Pharmakologie, Freie Universität
Berlin, Thielallee 67-73, D-14195 Berlin, Germany
Lysophosphatidic acid (LPA) utilizes a
G-protein-coupled receptor to activate the small GTP-binding protein
Rho and to induce rapid remodeling of the actin cytoskeleton. We
studied the signal transduction from LPA receptors to Rho activation.
Analysis of the G-protein-coupling pattern of LPA receptors by labeling
activated G-proteins with [
-32P]GTP azidoanilide
revealed interaction with proteins of the Gq, Gi, and G12 subfamilies. We could show that in
COS-7 cells, expression of GTPase-deficient mutants of
G12 and G13 triggered Rho activation as
measured by increased Rho-GTP levels. In Swiss 3T3 cells, incubation with LPA or microinjection of constitutively active mutants of G12 and G13 induced formation of actin
stress fibers and assembly of focal adhesions in a
Rho-dependent manner. Interestingly, the LPA-dependent cytoskeletal reorganization was suppressed by
microinjected antibodies directed against G13, whereas
G12-specific antibodies showed no inhibition. The
tyrosine kinase inhibitor tyrphostin A 25 and the epidermal growth
factor (EGF) receptor-specific tyrphostin AG 1478 completely blocked
actin stress fiber formation caused by LPA or activated
G13 but not the effects of activated G12. Also, expression of the dominant negative EGF receptor mutant EGFR-CD533 markedly prevented the LPA- and G13-induced
actin polymerization. Coexpression of EGFR-CD533 and activated
G13 in COS-7 cells resulted in decreased Rho-GTP levels
compared with expression of activated G13 alone. These
data indicate that in Swiss 3T3 cells, G13 but not
G12 is involved in the LPA-induced activation of Rho.
Moreover, our results suggest an involvement of the EGF receptor in
this pathway.
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