The pore structure and gating mechanism of K2P channelsK2P potassium channels are important regulators of cellular excitability. This study reveals that in contrast to most other K+ channels the primary gating mechanism in the K2P channel TREK-1 does not involve opening and closure of the cytoplasmic bundle crossing, but takes place close to or within the selectivity filter.

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more direct role of G i/o proteins in TRPC4/C5 activation is supported by the demonstration that Ga i and Ga o subunits physically bind to the C-terminus of TRPC4. We suggest that a concerted action of G q/11 -and G i/o -mediated signaling pathways is required for the full activation of TRPC4/C5, making these channels coincident detectors of multiple environmental cues. We have tested the co-dependence of native TRPC4/C5-like currents in smooth muscle cells, endothelial cells and neurons.