In our recent article published in Nature Communications entitled: “Swapped and non-swapped TRAAK states co-exist in membranes at a ratio influenced by temperature” we used pulsed Dipolar EPR Spectroscopy (PDS), PELDOR/DEER to show that the human K2P potassium mechanosensitive ion channel TRAAK coexists in the swapped and non-swapped states in native membranes, and demonstrate that the swapped conformation dominates, with the ratio being influenced by temperature. We further perfom native lipid analysis, which shows that TRAAK selectively associates with and is activated by signalling lipids to the exclusion of membrane-dominant phosphatidylcholine lipids from its vicinity, forming a distinct microdomain. Our approach can identify the immediate lipid environment, detect and quantify cap state populations in homo-/hetero-K2P channels and link domain swapping to specific triggers. More information could be found here.
