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A more recent version of this article appeared on August 1, 2002
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Submitted on September 24, 2001
Revised on April 11, 2002
Accepted on April 22, 2002
-ACTININ AND POLYMERIZATION BY RHO
1 Department of Biochemistry, Hokkaido University Graduate School of Medicine, Sapporo 060-8638, Japan; and Department of Pharmacology, School of Medicine, University of California, San Diego, La Jolla, California 92093-0636
2 Department of Pharmacology, School of Medicine, University of California, San Diego, La Jolla, California 92093-0636 (present address: Department of Molecular Genetics, National Institute of Neuroscience, 4-1-1 Ogawahigashi, Kodaira, Tokyo 187-8502, Japan)
3 Department of Biomedical Sciences, Hokkaido University Graduate School of Veterinary Medicine, Sapporo 060-0818, Japan
4 Neurosciences Program, School of Medicine, University of California, San Diego, La Jolla, California 92093-0636
5 Department of Pharmacology, Neurosciences Program, and Biomedical Sciences Program, School of Medicine, University of California, San Diego, La Jolla, California 92093-0636; and Molecular Neuroscience, Merck Research Laboratories, San Diego, CA 91212
* Corresponding author. E-mail address: nfuku{at}med.hokudai.ac.jp.
Lysophosphatidic acid (LPA) is a potent lipid mediator with actions on many cell types. Morphological changes involving actin polymerization are mediated by at least two, cognate G protein-coupled receptors, LPA1/EDG-2 or LPA2/EDG-4. Here we show that LPA can also induce actin depolymerization preceding actin polymerization within single TR mouse immortalized neuroblasts. Actin depolymerization resulted in immediate loss of membrane ruffling, whereas actin polymerization resulted in process retraction. Each pathway was found to be independent: depolymerization mediated by intracellular calcium mobilization and -actinin activity; and polymerization mediated by the activation of the small Rho GTPase. -Actinin-mediated depolymerization appears to be involved in growth cone collapse of primary neurons, indicating a physiological significance of LPA-induced actin depolymerization. Further evidence for dual regulation of actin rearrangement was found by heterologous retroviral transduction of either lpa1 or lpa2 in B103 cells that neither express LPA receptors nor respond to LPA, to confer both forms of LPA-induced actin rearrangements. These results suggest that diverging intracellular signals from a single type of LPA receptor could regulate actin depolymerization, as well as polymerization, within a single cell. This dual actin rearrangement may play a novel, important role in regulation of the neuronal morphology and motility during brain development.
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