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J Biol Chem. 2005 Feb 11;280(6):4415-21. Epub 2004 Nov 30.

Lysophosphatidic acid-operated K+ channels.

Author information

1
Institut de Pharmacologie Moléculaire et Cellulaire, CNRS-UMR 6097, Institut Paul Hamel, 660 route des Lucioles, Sophia-Antipolis, 06560 Valbonne, France.

Erratum in

  • J Biol Chem. 2013 Sep 6;288(36):26178.

Abstract

Lysophosphatidic acid (LPA) is an abundant cellular lipid with a myriad of biological effects. It plays an important role in both inter- and intracellular signaling. Activation of the LPA1-3 G-protein-coupled receptors explains many of the extracellular effects of LPA, including cell growth, differentiation, survival, and motility. However, LPA also acts intracellularly, activating the nuclear hormone receptor peroxisome proliferator-activated receptor-gamma that regulates gene transcription. This study shows that the novel subfamily of mechano-gated K2P channels comprising TREK-1, TREK-2, and TRAAK is strongly activated by intracellular LPA. The LPA-activated 2P domain K+ channels are intracellular ligand-gated K+ channels such as the Ca2+- or the ATP-sensitive K+ channels. LPA reversibly converts these mechano-gated, pH- and voltage-sensitive channels into leak conductances. Gating conversion of the 2P domain K+ channels by intracellular LPA represents a novel form of ion channel regulation. Thus, the TREK and TRAAK channels should be included in the LPA-associated physiological and disease states.

PMID:
15572365
DOI:
10.1074/jbc.M408246200
[Indexed for MEDLINE]
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