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A more recent version of this article appeared on February 1, 2003
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Submitted on April 3, 2002
Revised on October 2, 2002
Accepted on October 11, 2002
1 Department of Cell Biology and Oncology, Istituto di Ricerche Farmacologiche "Mario Negri", Consorzio Mario Negri Sud, Via Nazionale, 66030 Santa Maria Imbaro, Chieti, Italy (present address: ABBOTT SpA, Via Pontina km 52-04010, Campoverde (Latina), Italy)
2 Department of Cell Biology and Oncology, Istituto di Ricerche Farmacologiche "Mario Negri", Consorzio Mario Negri Sud, Via Nazionale, 66030 Santa Maria Imbaro, Chieti, Italy (present address: Department of Oncology and Neuroscience, Universita' "G. D'Annunzio", Via dei Vestini 1, 66100 Chieti, Italy)
3 Department of Cell Biology and Oncology, Istituto di Ricerche Farmacologiche "Mario Negri", Consorzio Mario Negri Sud, Via Nazionale, 66030 Santa Maria Imbaro, Chieti, Italy
4 Department of Cell Biology and Oncology, Istituto di Ricerche Farmacologiche "Mario Negri", Consorzio Mario Negri Sud, Via Nazionale, 66030 Santa Maria Imbaro, Chieti, Italy (present address: Cutech Srl, Parkallee 22, D-23845 Borstel, Germany)
* Corresponding author. E-mail address: corda{at}negrisud.it.
Glycerophosphoinositol 4-phosphate (GroPIns-4P) is a biologically active, water-soluble phospholipase A metabolite derived from phosphatidylinositol 4-phosphate, whose cellular concentrations have been reported to increase in Ras-transformed cells. It is therefore important to understand its biological activities. Here, we have examined whether GroPIns- 4P can regulate the organization of the actin cytoskeleton, as this could be a Ras-related function involved in cell motility and metastatic invasion. We find that in serum-starved Swiss 3T3 cells, exogenously added GroPIns-4P rapidly and potently induces the formation of membrane ruffles, and, later, the formation of stress fibers. These actin structures can be regulated by the small GTPases Cdc42, Rac and Rho. To analyze the mechanism of action of GroPIns-4P, we selectively inactivated each of these GTPases. GroPIns-4P requires active Rac and Rho, but not Cdc42, for ruffle and stress fiber formation, respectively. Moreover, GroPIns-4P induces a rapid translocation of the green-fluorescent-protein-tagged Rac into ruffles, and increases the fraction of GTP-bound Rac, in intact cells. The activation of Rac by GroPIns-4P was near-maximal and long-lasting. Interestingly, this feature appears to be critical in the induction of actin ruffles by GroPIns-4P.
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