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Updated: Aug 20, 2026

Use of Label-free Optical Biosensors to Detect Modulation of Potassium Channels by G-protein Coupled Receptors
Published on: February 10, 2014
A phospholipid sensor controls mechanogating of the K+ channel TREK-1
Jean Chemin1, Amanda Jane Patel, Fabrice Duprat
1Institut de Pharmacologie, Moléculaire et Cellulaire, Institut Paul Hamel, Sophia Antipolis, Valbonne, France.
Abstract:
TREK-1 (KCNK2 or K(2P)2.1) is a mechanosensitive K(2P) channel that is opened by membrane stretch as well as cell swelling. Here, we demonstrate that membrane phospholipids, including PIP(2), control channel gating and transform TREK-1 into a leak K(+) conductance. A carboxy-terminal positively charged cluster is the phospholipid-sensing domain that interacts with the plasma membrane. This region also encompasses the proton sensor E306 that is required for activation of TREK-1 by cytosolic acidosis. Protonation of E306 drastically tightens channel-phospholipid interaction and leads to TREK-1 opening at atmospheric pressure. The TREK-1-phospholipid interaction is critical for channel mechano-, pH(i)- and voltage-dependent gating.
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