Mechano- or Acid Stimulation, Two Interactive Modes of Activation of the TREK-1 Potassium Channel*

@article{Maingret1999MechanoOA,
  title={Mechano- or Acid Stimulation, Two Interactive Modes of Activation of the TREK-1 Potassium Channel*},
  author={François Maingret and A. J. Patel and Florian Lesage and Michel Lazdunski and Eric Honor{\'e}},
  journal={The Journal of Biological Chemistry},
  year={1999},
  volume={274},
  pages={26691 - 26696}
}
TREK-1 is a member of the novel structural class of K+ channels with four transmembrane segments and two pore domains in tandem (1, 2). TREK-1 is opened by membrane stretch and arachidonic acid. It is also an important target for volatile anesthetics (2, 3). Here we show that internal acidification opens TREK-1. Indeed, lowering pH i shifts the pressure-activation relationship toward positive values and leads to channel opening at atmospheric pressure. The pH i -sensitive region in the carboxyl… Expand
Regulation of the Mechano-Gated K2P Channel TREK-1 by Membrane Phospholipids.
This chapter discusses the regulation of the mechano-gated K(2P) channel, TREK-1 by membrane phospholipids. TREK-1 (KCNK2 or K2P2.1) is a polymodal K(+) channel that is activated by membrane stretch,Expand
Up- and down-regulation of the mechano-gated K2P channel TREK-1 by PIP2 and other membrane phospholipids
TLDR
This study shows that the inner leaflet membrane phospholipids, including PIP2, exert a mixed stimulatory and inhibitory effect on TREK-1, the first report of an ion channel dually regulated by membrane phosphOLipids. Expand
Synergistic interaction and the role of C-terminus in the activation of TRAAK K+ channels by pressure, free fatty acids and alkali
TLDR
Rat TRAAK is an alkali-sensing K+ channel that shows synergistic activation with pressure, and that the mechanism of activation of rTRAAK and TREK by free fatty acids are different. Expand
An intracellular proton sensor commands lipid‐ and mechano‐gating of the K+ channel TREK‐1
TLDR
It is concluded that protonation of E306 tunes the TREK‐1 mechanical setpoint and thus sets lipid sensitivity, and the cAMP/PKA down‐modulation is abolished. Expand
Mechanosensitive TREK-1 two-pore-domain potassium (K2P) channels in the cardiovascular system.
TLDR
The functional role of TREK-1 in the heart and its putative contribution to cardiac mechanoelectrical coupling are focused on, as well as the significance oftreK- 1 in the development of cardiac hypertrophy, cardiac fibrosis and heart failure. Expand
Extracellular acidification exerts opposite actions on TREK1 and TREK2 potassium channels via a single conserved histidine residue
TLDR
It is shown that acidification of the extracellular medium strongly inhibits TREK1 with an apparent pK near to 7.4 corresponding to the physiological pH, which discriminates between these two K+ channels that otherwise share the same regulations by physical and chemical stimuli, and by hormones and neurotransmitters. Expand
Triple arginine residues in the proximal C-terminus of TREK K+ channels are critical for biphasic regulation by phosphatidylinositol 4,5-bisphosphate.
TLDR
It is proposed that the PIP2-dependent converse regulation of TREKs by Lys and R3-pCt with Gly implies structural flexibility. Expand
Disruption of palmitate-mediated localization; a shared pathway of force and anesthetic activation of TREK-1 channels.
TLDR
Palmitate-mediated localization of PLD2 emerges as a central control mechanism of TREK-1 responding to mechanical force and anesthetic action, a putative model for excitatory and inhibitory mechano-effectors and anesthesia sensitive ion channels in a biological context. Expand
Localization of TREK-2 K+ channel domains that regulate channel kinetics and sensitivity to pressure, fatty acids and pHi
TLDR
The C-terminus endows TREK-2 with unique channel kinetics and the ability to be gated by free fatty acids and low pHi, and with increased mechanosensitivity. Expand
Molecular basis of the voltage-dependent gating of TREK-1, a mechano-sensitive K(+) channel.
TLDR
Deletional and chimeric analysis demonstrates that the carboxy terminal domain of TREK-1, but not the PKA phosphorylation site S333, is responsible for voltage-dependent gating. Expand
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