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Originally published as MBC in Press, 10.1091/mbc.01-09-0465 on June 6, 2002
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Vol. 13, Issue 8, 2692-2705, August 2002

Dual Regulation of Actin Rearrangement through Lysophosphatidic Acid Receptor in Neuroblast Cell Lines: Actin Depolymerization by Ca2+-alpha -Actinin and Polymerization by Rho

Nobuyuki Fukushima,*dagger Isao Ishii,dagger § Yoshiaki Habara,|| Cara B. Allen, and Jerold Chundagger #@

 *Department of Molecular Biochemistry, Hokkaido University Graduate School of Medicine, Sapporo 060-8638, Japan;  dagger Department of Pharmacology,  Neurosciences Program,  #Biomedical Sciences Program, School of Medicine, University of California, San Diego, La Jolla, California 92093-0636;  @Molecular Neuroscience, Merck Research Laboratories, San Diego, California 91212; and  ||Department of Biomedical Sciences, Hokkaido University Graduate School of Veterinary Medicine, Sapporo 060-0818, Japan

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. Herein, 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 alpha -actinin activity and polymerization mediated by the activation of the small Rho GTPase. alpha -Actinin-mediated depolymerization seems 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.

§ Present address: Department of Molecular Genetics, National Institute of Neuroscience, 4-1-1 Ogawahigashi, Kodaira, Tokyo 187-8502, Japan

Molecular Biology of the Cell
Vol. 13, 2692-2705, August 2002
Copyright © 2002 by The American Society for Cell Biology


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