Dual regulation of actin rearrangement through lysophosphatidic acid receptor in neuroblast cell lines: Actin depolymerization by Ca2+-α-actinin and polymerization by Rho

Nobuyuki Fukushima, Isao Ishii, Yoshiaki Habara, Cara B. Allen, Jerold Chun

Research output: Contribution to journalArticle

50 Citations (Scopus)

Abstract

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 α-actinin activity and polymerization mediated by the activation of the small Rho GTPase. α-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.

Original languageEnglish
Pages (from-to)2692-2705
Number of pages14
JournalMolecular biology of the cell
Volume13
Issue number8
DOIs
Publication statusPublished - 2002 Aug

ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology

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