Lysophosphatidic acid- and Gbeta-dependent activation of Dictyostelium MAP kinase ERK2

Biochem Biophys Res Commun. 2001 Apr 6;282(3):765-72. doi: 10.1006/bbrc.2001.4649.

Abstract

Exogenous lysophosphatidic acid (LPA) has been shown to evoke a chemotactic response in aggregative cells of the social amoeba Dictyostelium discoideum. In this paper, we demonstrate that extracellular LPA is also able to induce activation of mitogen-activated protein (MAP) kinase DdERK2 (extracellular signal regulated kinase 2) in these cells. This activation is independent of cyclic AMP receptors, yet fully dependent on the single Gbeta subunit, hinting to the presence of functional heptahelical LPA receptors in a primitive eukaryote. We did not observe LPA-dependent cyclic GMP accumulation, which suggests that the pathways for LPA-induced and "classical" chemotaxis of D. discoideum cells are substantially different.

MeSH terms

  • Animals
  • Chemotaxis / drug effects
  • Cyclic AMP / metabolism
  • Cyclic GMP / metabolism
  • Dictyostelium / drug effects
  • Dictyostelium / genetics
  • Dictyostelium / physiology*
  • Enzyme Activation / drug effects
  • Heterotrimeric GTP-Binding Proteins / metabolism*
  • Lysophospholipids / metabolism
  • Lysophospholipids / pharmacology*
  • Mitogen-Activated Protein Kinase 1 / metabolism*
  • Receptors, Cell Surface / drug effects
  • Receptors, Cell Surface / metabolism
  • Receptors, G-Protein-Coupled*
  • Receptors, Lysophosphatidic Acid
  • Signal Transduction

Substances

  • Lysophospholipids
  • Receptors, Cell Surface
  • Receptors, G-Protein-Coupled
  • Receptors, Lysophosphatidic Acid
  • Cyclic AMP
  • Mitogen-Activated Protein Kinase 1
  • Heterotrimeric GTP-Binding Proteins
  • Cyclic GMP