All members of the Kir super-family of potassium channels are thought to be directly gated by PIP.

For TRPV5, binding of PIP2 to a site in the transmembrane domain caused a conformational change that appeared to open the conduction pathway,[6] suggesting the channel is classically lipid-gated.

Kv: PA binding can also influence the midpoint of voltage activation (Vmid) for voltage-activated potassium channels.

The physiological signaling pathway is not well studied, but PLD can produce PG in the presence of glycerol[15] suggesting the same mechanism that is thought to generate local PA gradients could be generating high local PG gradients as well.

A specialized set of mechanosensitive ion channels is gated by lipid deformation in the membrane in response to mechanical force.

[10] Theoretical estimates suggest initial concentration of a signaling lipid produced near an ion channel are likely millimolar;[9] however, due to theoretical calculations of lipids diffusion in a membrane, the ligand was thought to diffuse away much to fast to activate a channel.

[21] However, Comoglio and colleagues showed experimentally that the enzyme phospholipase D2 bound directly to TREK-1 and produced the PA necessary to activate the channel.

[10] The conclusion of Comoglio et al was experimentally confirmed when it was shown that the dissociation constant of PA for TREK-1 is 10 micro molar,[11] a Kd much weaker than the bulk concentration in the membrane.

Combined these data show that PA must be local in concentration near 100 micro molar or more, suggesting the diffusion of the lipid is somehow restricted in the membrane.

In theory, ion channels can be activated by their diffusion or trafficking to high concentrations of a signaling lipid.

The competition of PEth on potassium channel is thought to contribute to the anesthetic effect of ethanol and perhaps hangover.